ORIGINAL_ARTICLE
Epigenetic: A missing paradigm in cellular and molecular pathways of sulfur mustard lung: a prospective and comparative study
Sulfur mustard (SM, bis- (2-chloroethyl) sulphide) is a chemical warfare agent that causes DNA alkylation, protein modification and membrane damage. SM can trigger several molecular pathways involved in inflammation and oxidative stress, which cause cell necrosis and apoptosis, and loss of cells integrity and function. Epigenetic regulation of gene expression is a growing research topic and is addressed by DNA methylation, histone modification, chromatin remodeling, and noncoding RNAs expression. It seems SM can induce the epigenetic modifications that are translated into change in gene expression. Classification of epigenetic modifications long after exposure to SM would clarify its mechanism and paves a better strategy for the treatment of SM-affected patients. In this study, we review the key aberrant epigenetic modifications that have important roles in chronic obstructive pulmonary disease (COPD) and compared with mustard lung.
https://ijbms.mums.ac.ir/article_4722_d8da4a345c758824da593c74149d17ec.pdf
2015-08-01
723
736
10.22038/ijbms.2015.4722
Cellular and molecular-modification
Epigenetic modification
Inflammation
Sulfur mustard
Saber
Imani
1
Systems Biology Institute, Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Yunes
Panahi
yunespanahieq@yahoo.com
2
Systems Biology Institute, Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Jafar
Salimian
jafar.salimian@gmail.com
3
Systems Biology Institute, Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Junjiang
Fu
fujunjianga@hotmail.com
4
Key Laboratory of Epigenetics and Oncology, the Research Center for Preclinical Medicine, Sichuan Medical University, Luzhou, Sichuan, China
AUTHOR
Mostafa
Ghanei
ghahri14@yahoo.com
5
Systems Biology Institute, Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
1. Case RA, Lea AJ. Mustard gas poisoning, chronic bronchitis, and lung cancer; an investigation into the possibility that poisoning by mustard gas in the 1914-18 war might be a factor in the production of neoplasia. Br J Prev Soc Med 1955; 9:62-72.
1
2. Niu T, Matijasevic Z, Austin-Ritchie P, Stering A, Ludlum DB. A 32P-postlabeling method for the detection of adducts in the DNA of human fibroblasts exposed to sulfur mustard. Chem Biol Interact 1996; 100:77-84.
2
3. Ludlum DB, Kent S, Mehta JR. Formation of O6-ethylthioethylguanine in DNA by reaction with the sulfur mustard, chloroethyl sulfide, and its apparent lack of repair by O6-alkylguanine-DNA alkyltransferase. Carcinogenesis 1986; 7:1203-1206.
3
4. Jowsey PA, Williams FM, Blain PG. DNA damage responses in cells exposed to sulphur mustard. Toxicol Lett 2012; 209:1-10.
4
5. Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281:1309-1312.
5
6. Nguewa PA, Fuertes MA, Alonso C, Perez JM. Pharmacological modulation of Poly(ADP-ribose) polymerase-mediated cell death: exploitation in cancer chemotherapy. Mol Pharmacol 2003; 64: 1007-1014.
6
7. Chiarugi A, Moskowitz MA. Cell biology. PARP-1--a perpetrator of apoptotic cell death? Science 2002; 297:200-201.
7
8. Kehe K, Raithel K, Kreppel H, Jochum M, Worek F, Thiermann H. Inhibition of poly(ADP-ribose) polymerase (PARP) influences the mode of sulfur mustard (SM)-induced cell death in HaCaT cells. Arch Toxicol 2008; 82:461-470.
8
9. GP. W. Studies related to the mechanisms of cytotoxic alkylating agents: a review. Cancer Res 1962; 22:651-688.
9
10. Ghanei M. Respiratory Diseases. Rijeka, Croatia: InTech; 2012.
10
11. Majid Shohrati IK, Amin Saburi, Hossein Khalili, Mostafa Ghanei. The role of N-acetylcysteine in the management of acute and chronic pulmonary complications of sulfur mustard: a literature review. Inhalation Toxicology 2014; 26: 507-523.
11
12. Boskabady MH, Farhadi J. The possible prophylactic effect of Nigella sativa seed aqueous extract on respiratory symptoms and pulmonary function tests on chemical war victims: a randomized, double-blind, placebo-controlled trial. J Altern Complement Med 2008; 14:1137-1144.
12
13. Hamid Saber AS, Mostafa Ghanei. Clinical and paraclinical guidelines for management of sulfur mustard induced bronchiolitis obliterans; from bench to bedside. Inhalation Toxicology 2012; 24:900-906.
13
14. Adcock IM, Ford P, Ito K, Barnes PJ. Epigenetics and airways disease. Respir Res 2006; 7:21.
14
15. Pohanka M, Sobotka J, Jilkova M, Stetina R. Oxidative stress after sulfur mustard intoxication and its reduction by melatonin: efficacy of antioxidant therapy during serious intoxication. Drug Chem Toxicol 2011; 34:85-91.
15
16. Naghii MR. Sulfur mustard intoxication, oxidative stress, and antioxidants. Mil Med 2002; 167:573-575.
16
17. Pant SC, Vijayaraghavan R, Kannan GM, Ganesan K. Sulphur mustard induced oxidative stress and its prevention by sodium 2,3-dimercapto propane sulphonic acid (DMPS) in mice. Biomed Environ Sci 2000; 13:225-232.
17
18. Ghanei M, Harandi AA. Molecular and cellular mechanism of lung injuries due to exposure to sulfur mustard: a review. Inhal Toxicol 2011; 23:363-371.
18
19. Repine JE BA, Lankhorst I. Oxidative stress in chronic obstructive pulmonary disease. Am J Respir Crit Care Med 1997:341-357.
19
20. Boskabady MH, Amery S, Vahedi N, Khakzad MR. The effect of vitamin E on tracheal responsiveness and lung inflammation in sulfur mustard exposed guinea pigs. Inhal Toxicol 2011; 23:157-165.
20
21. Rahman I. Oxidative stress in pathogenesis of chronic obstructive pulmonary disease: cellular and molecular mechanisms. Cell Biochem Biophys 2005; 43:167-188.
21
22. Rahman I. Oxidative stress, chromatin remodeling and gene transcription in inflammation and chronic lung diseases. J Biochem Mol Biol 2003; 36:95-109.
22
23. Carter AB, Monick MM, Hunninghake GW. Both Erk and p38 kinases are necessary for cytokine gene transcription. Am J Respir Cell Mol Biol 1999; 20: 751-758.
23
24. Barreiro E, Fermoselle C, Mateu-Jimenez M, Sanchez-Font A, Pijuan L, Gea J, et al. Oxidative stress and inflammation in the normal airways and blood of patients with lung cancer and COPD. Free Radic Biol Med 2013; 65:859-71.
24
25. Radi R, Cassina A, Hodara R. Nitric oxide and peroxynitrite interactions with mitochondria. Biol Chem 2002; 383:401-409.
25
26. Reiter TA. NO* chemistry: a diversity of targets in the cell. Redox Rep 2006; 11:194-206.
26
27. Szabo C. Poly(ADP-ribose) polymerase activation by reactive nitrogen species--relevance for the pathogenesis of inflammation. Nitric Oxide 2006; 14: 169-179.
27
28. Coppey LJ, Gellett JS, Davidson EP, Dunlap JA, Lund DD, Yorek MA, et al. Effect of antioxidant treatment of streptozotocin-induced diabetic rats on endoneurial blood flow, motor nerve conduction velocity, and vascular reactivity of epineurial arterioles of the sciatic nerve. Diabetes 2001; 50:1927-1937.
28
29. Paromov V, Qui M, Yang H, Smith M, Stone WL. The influence of N-acetyl-L-cysteine on oxidative stress and nitric oxide synthesis in stimulated macrophages treated with a mustard gas analogue. BMC Cell Biol 2008; 9:33.
29
30. Gould NS, White CW, Day BJ. A role for mitochondrial oxidative stress in sulfur mustard analog 2-chloroethyl ethyl sulfide-induced lung cell injury and antioxidant protection. J Pharmacol Exp Ther 2009; 328: 732-739.
30
31. Vijayaraghavan R, Sugendran K, Pant SC, Husain K, Malhotra RC. Dermal intoxication of mice with bis(2-chloroethyl)sulphide and the protective effect of flavonoids. Toxicology 1991; 69:35-42.
31
32. Mehrani H, Ghanei M, Aslani J, Tabatabaei Z. Plasma proteomic profile of sulfur mustard exposed lung diseases patients using 2-dimensional gel electrophoresis. Clin Proteomics 2011; 8: 2.
32
33. Shahriary A, Mehrani H, Ghanei M, Parvin S. Comparative proteome analysis of peripheral neutrophils from sulfur mustard-exposed and COPD patients. J Immunotoxicol 2015; 12:132-139.
33
34. Ghazanfari T, Faghihzadeh S, Aragizadeh H, Soroush MR, Yaraee R, Mohammad Hassan Z, Foroutan A, Vaez-Mahdavi MR, Javadi MA, Moaiedmohseni S, et al. Sardasht-Iran cohort study of chemical warfare victims: design and methods. Arch Iran Med 2009; 12:5-14.
34
35. Ghazanfari T, Kariminia A, Yaraee R, Faghihzadeh S, Ardestani SK, Ebtekar M, et al. Long term impact of sulfur mustard exposure on peripheral blood mononuclear subpopulations - Sardasht-Iran Cohort Study (SICS). Int Immunopharmacol 2013; 17:931-935.
35
36. Mostafa Ghanei AAH. Molecular and cellular mechanism of lung injuries due to exposure to sulfur mustard: a review. Inhal Toxicol 2011; 23:363-371.
36
37. Boskabady MH, Vahedi N, Amery S, Khakzad MR. The effect of Nigella sativa alone, and in combination with dexamethasone, on tracheal muscle responsiveness and lung inflammation in sulfur mustard exposed guinea pigs. J Ethnopharmacol 2011; 137:1028-1034.
37
38. Boskabady MH, Attaran D, Shaffei MN. Airway responses to salbutamol after exposure to chemical warfare. Respirology. 2008; 13: 288-293.
38
39. Boskabady MH, Tabatabayee A, Amiri S, Vahedi N. The effect of vitamin E on pathological changes in kidney and liver of sulphur mustard-exposed guinea pigs. Toxicol Ind Health 2012; 28: 216-221.
39
40. Brigati C, Banelli B, di Vinci A, Casciano I, Allemanni G, Forlani A, et al. Inflammation, HIF-1, and the epigenetics that follows. Mediators Inflamm 2010; 2010:263914.
40
41. Mechali M. DNA replication origins: from sequence specificity to epigenetics. Nat Rev Genet 2001; 2:640-5.
41
42. Cheung P LP. Epigenetic regulation by histone methylation and histone variants. Mol Endocrinol 2005; 19:563-573.
42
43. Lee KK WJ. Histone acetyltransferase complexes: one size doesn’t fit all. Nat Rev Mol Cell Biol 2007; 8: 284-295.
43
44. Wright RJ. Epidemiology of stress and asthma: from constricting communities and fragile families to epigenetics. Immunol Allergy Clin North Am 2011; 31:19-39.
44
45. Durham A, Chou PC, Kirkham P, Adcock IM. Epigenetics in asthma and other inflammatory lung diseases. Epigenomics 2010; 2: 523-537.
45
46. Li CY, Guo XJ, Gan LX. [The epigenetics in asthma]. Zhonghua Jie He He Hu Xi Za Zhi 2009; 32:759-761.
46
47. Lovinsky-Desir S, Miller RL. Epigenetics, asthma, and allergic diseases: a review of the latest advancements. Curr Allergy Asthma Rep 2012; 12: 211-220.
47
48. Langevin SM, Kratzke RA, Kelsey KT. Epigenetics of lung cancer. Transl Res 2014; 165:74-90.
48
49. Sundar IK, Mullapudi N, Yao H, Spivack SD, Rahman I. Lung cancer and its association with chronic obstructive pulmonary disease: update on nexus of epigenetics. Curr Opin Pulm Med 2011; 17: 279-285.
49
50. Ho SM. Environmental epigenetics of asthma: an update. J Allergy Clin Immunol. 2010; 126: 453-65.
50
51. Martino D, Prescott S. Epigenetics and prenatal influences on asthma and allergic airways disease. Chest 2011; 139: 640-647.
51
52. Shaheen SO, Adcock IM. The developmental origins of asthma: does epigenetics hold the key? Am J Respir Crit Care Med 2009; 180: 690-691.
52
53. Stower H. Epigenetics: Dynamic DNA methylation. Nat Rev Genet 2011; 13:75.
53
54. Lan F, Shi Y. Epigenetic regulation: methylation of histone and non-histone proteins. Sci China C Life Sci 2009; 52: 311-322.
54
55. Durham AL, Wiegman C, Adcock IM. Epigenetics of asthma. Biochim Biophys Acta 2011; 1810: 1103-1109.
55
56. Kabesch M, Adcock IM. Epigenetics in asthma and COPD. Biochimie 2012; 94: 2231-2241.
56
57. Koppelman GH, Nawijn MC. Recent advances in the epigenetics and genomics of asthma. Curr Opin Allergy Clin Immunol 2011; 11: 414-419.
57
58. Lee SH, Park JS, Park CS. The search for genetic variants and epigenetics related to asthma. Allergy Asthma Immunol Res 2011; 3: 236-244.
58
59. Bartova E, Krejci J, Hajek R, Harnicarova A, Kozubek S. Chromatin structure and epigenetics of tumour cells: a review. Cardiovasc Hematol Disord Drug Targets 2009; 9: 51-61.
59
60. Diaw L, Woodson K, Gillespie JW. Prostate cancer epigenetics: a review on gene regulation. Gene Regul Syst Bio 2007; 1: 313-325.
60
61. Katoh M. Therapeutics targeting angiogenesis: Genetics and epigenetics, extracellular miRNAs and signaling networks (Review). Int J Mol Med 2013; 32:763-767.
61
62. Mungall AJ. Meeting review: Epigenetics in Development and Disease. Comp Funct Genomics 2002; 3: 277-281.
62
63. Weber M, Schubeler D. Genomic patterns of DNA methylation: targets and function of an epigenetic mark. Curr Opin Cell Biol 2007; 19: 273-280.
63
64. Herman JG, Baylin SB. Gene silencing in cancer in association with promoter hypermethylation. N Engl J Med 2003; 349: 2042-2054.
64
65. Illingworth RSB, A. P. CpG islands--'a rough guide'. FEBS Lett 2009; 583: 1713-1720.
65
66. Maric NP, Svrakic DM. Why schizophrenia genetics needs epigenetics: a review. Psychiatr Danub 2012; 24: 2-18.
66
67. Cheng X, Blumenthal RM. Coordinated chromatin control: structural and functional linkage of DNA and histone methylation. Biochemistry 2010; 49:2999-3008.
67
68. McCabe MT, Brandes JC, Vertino PM. Cancer DNA methylation: molecular mechanisms and clinical implications. Clin Cancer Res 2009; 15: 3927-3937.
68
69. Bhattacharya SK, Ramchandani S, Cervoni N, Szyf M. A mammalian protein with specific demethylase activity for mCpG DNA. Nature 1999; 397:579-583.
69
70. Anest V HJ, Cogswell PC, Steinbrecher KA, Strahl BD, Baldwin AS A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression. Nature 2003; 423:659-663.
70
71. Ito S, Shen L, Dai Q, Wu SC, Collins LB, Swenberg JA, et al. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 2011; 333:1300-1303.
71
72. Benakanakere MR LQ, Eskan MA, Singh AV, Zhao J, Galicia JC, et al. Modulation of TLR2 protein expression by miR-105 in human oral keratinocytes. J Biol Chem 2009; 284: 23107-23115.
72
73. Zhang H, Zhu JK. Active DNA demethylation in plants and animals. Cold Spring Harb Symp Quant Biol 2012; 77:161-173.
73
74. Zhu JK. Active DNA demethylation mediated by DNA glycosylases. Annu Rev Genet. 2009; 43: 143-66.
74
75. Hackett JA, Sengupta R, Zylicz JJ, Murakami K, Lee C, Down TA, et al. Germline DNA demethylation dynamics and imprint erasure through 5-hydroxymethylcytosine. Science 2013; 339: 448-452.
75
76. Ma DK, Jang MH, Guo JU, Kitabatake Y, Chang ML, Pow-Anpongkul N, et al. Neuronal activity-induced Gadd45b promotes epigenetic DNA demethylation and adult neurogenesis. Science 2009; 323: 1074-1077.
76
77. Guo JU, Su Y, Zhong C, Ming GL, Song H. Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain. Cell 2011; 145: 423-434.
77
78. Campos EI, Reinberg D. Histones: annotating chromatin. Annu Rev Genet 2009; 43: 559-599.
78
79. Rajendrasozhan S, Yang SR, Edirisinghe I, Yao H, Adenuga D, Rahman I. Deacetylases and NF-kappaB in redox regulation of cigarette smoke-induced lung inflammation: epigenetics in pathogenesis of COPD. Antioxid Redox Signal 2008; 10: 799-811.
79
80. Wierda RJ, Geutskens SB, Jukema JW, Quax PH, van den Elsen PJ. Epigenetics in atherosclerosis and inflammation. J Cell Mol Med 2010; 14: 1225-1240.
80
81. Shanmugam MK, Sethi G. Role of epigenetics in inflammation-associated diseases. Subcell Biochem 2012; 61: 627-657.
81
82. Cruickshank MN, Besant P, Ulgiati D. The impact of histone post-translational modifications on developmental gene regulation. Amino Acids 2010; 39: 1087-1105.
82
83. Yla-Herttuala S, Glass CK. Review focus on epigenetics and the histone code in vascular biology. Cardiovasc Res 2011; 90: 402-403.
83
84. Timmermann S, Lehrmann H, Polesskaya A, Harel-Bellan A. Histone acetylation and disease. Cell Mol Life Sci. 2001; 58: 728-736.
84
85. Adamopoulou E, Naumann U. HDAC inhibitors and their potential applications to glioblastoma therapy. Oncoimmunology 2013; 2: e25219.
85
86. Barnes PJ. Reduced histone deacetylase in COPD: clinical implications. Chest 2006; 129: 151-155.
86
87. Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, Wang Z, et al. High-resolution profiling of histone methylations in the human genome. Cell 2007; 129: 823-837.
87
88. Cheung P, Lau P. Epigenetic regulation by histone methylation and histone variants. Mol Endocrinol 2005; 19: 563-573.
88
89. Bhan A, Mandal SS. Long Noncoding RNAs: Emerging Stars in Gene Regulation, Epigenetics and Human Disease. Chem Med Chem 2014; 9:1932-1956.
89
90. Blelloch R, Gutkind JS. Epigenetics, noncoding RNAs, and cell signaling--crossroads in the regulation of cell fate decisions. Curr Opin Cell Biol 2013; 25: 149-151.
90
91. Friedman JM, Jones PA, Liang G. The tumor suppressor microRNA-101 becomes an epigenetic player by targeting the polycomb group protein EZH2 in cancer. Cell Cycle 2009; 8: 2313-2314.
91
92. Shaked I, Meerson A, Wolf Y, Avni R, Greenberg D, Gilboa-Geffen A, Soreq H. MicroRNA-132 potentiates cholinergic anti-inflammatory signaling by targeting acetylcholinesterase. Immunity 2009; 31: 965-973.
92
93. Tili E, Michaille JJ. Resveratrol, MicroRNAs, Inflammation, and Cancer. J Nucleic Acids 2011; 2011: 102431.
93
94. Sonkoly E, Pivarcsi A. microRNAs in inflammation. Int Rev Immunol 2009; 28: 535-561.
94
95. Cao J. The functional role of long non-coding RNAs and epigenetics. Biol Proced Online 2014; 16: 11.
95
96. Beckedorff FC, Amaral MS, Deocesano-Pereira C, Verjovski-Almeida S. Long non-coding RNAs and their implications in cancer epigenetics. Biosci Rep 2013; 33.
96
97. Najafi A, Masoudi-Nejad A, Imani Fooladi AA, Ghanei M, Nourani MR. Microarray gene expression analysis of the human airway in patients exposed to sulfur mustard. J Recept Signal Transduct Res 2014; 34: 283-289.
97
98. Medzhitov R, Horng T. Transcriptional control of the inflammatory response. Nat Rev Immunol 2009; 9: 692-703.
98
99. Piantadosi CA, Suliman HB. Transcriptional control of mitochondrial biogenesis and its interface with inflammatory processes. Biochim Biophys Acta 2012; 1820: 532-541.
99
100. Medzhitov R. Origin and physiological roles of inflammation. Nature 2008; 454: 428-35.
100
101. McKeever T LS, Smith C, Hubbard R. The importance of prenatal exposures on the development of allergic disease: a birth cohort study using the West Midlands General Practice Database. Am J Respir Crit Care Med 2002; 166: 827-832.
101
102. Chowdhury S, Ammanamanchi S, Howell GM. Epigenetic Targeting of Transforming Growth Factor beta Receptor II and Implications for Cancer Therapy. Mol Cell Pharmacol 2009; 1: 57-70.
102
103. Allfrey VG, Faulkner R, Mirsky AE. Acetylation and Methylation of Histones and Their Possible Role in the Regulation of Rna Synthesis. Proc Natl Acad Sci USA 1964; 51:786-794.
103
104. Kipnis E, Dessein R. Bacterial modulation of Tregs/Th17 in intestinal disease: a balancing act? Inflamm Bowel Dis 2012; 18: 1389-1390.
104
105. Ballestar E. Epigenetics lessons from twins: prospects for autoimmune disease. Clin Rev Allergy Immunol 2010; 39: 30-41.
105
106. Krupanidhi S, Sedimbi SK, Sanjeevi CB. Epigenetics and epigenetic mechanisms in disease with emphasis on autoimmune diseases. J Assoc Physicians India 2008; 56: 875-880.
106
107. Callinan PA FA. The emerging science of epigenomics. Hum Mol Genet 2006; 15: 95–101.
107
108. Marwick JA, Ito K, Adcock IM, Kirkham PA. Oxidative stress and steroid resistance in asthma and COPD: pharmacological manipulation of HDAC-2 as a therapeutic strategy. Expert Opin Ther Targets 2007; 11: 745-55.
108
109. Korkmaz A, Yaren H, Kunak Zl, Uysal B, Kurt B, Topal T, et al. Epigenetic perturbations in the pathogenesis of mustard toxicity; hypothesis and preliminary results. Interdisc Toxicol 2008; 1: 236–241.
109
110. Mielcarek M, Benn CL, Franklin SA, Smith DL, Woodman B, Marks PA, Bates GP. SAHA decreases HDAC 2 and 4 levels in vivo and improves molecular phenotypes in the R6/2 mouse model of Huntington's disease. PLoS One 2011; 6: e27746.
110
111. Mosley AL, Ozcan S. The pancreatic duodenal homeobox-1 protein (Pdx-1) interacts with histone deacetylases Hdac-1 and Hdac-2 on low levels of glucose. J Biol Chem 2004; 279: 54241-54247.
111
112. Wagner M, Brosch G, Zwerschke W, Seto E, Loidl P, Jansen-Durr P. Histone deacetylases in replicative senescence: evidence for a senescence-specific form of HDAC-2. FEBS Lett. 2001; 499: 101-6.
112
113. Ito K, Hanazawa T, Tomita K, Barnes PJ, Adcock IM. Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration. Biochem Biophys Res Commun 2004; 315: 240-245.
113
114. Egger G LG, Aparicio A, Jones PA. Epigenetics in human disease and prospects for epigenetic therapy. Nature 2004; 429: 457-463.
114
115. Ghanei M, Harandi AA. Long term consequences from exposure to sulfur mustard: a review. Inhal Toxicol 2007; 19: 451-456.
115
116. Pourfarzam S, Ghazanfari T, Yaraee R, Ghasemi H, Hassan ZM, Faghihzadeh S, Ardestani SK, Kariminia A, Fallahi F, Soroush MR, et al. Serum levels of IL-8 and IL-6 in the long term pulmonary complications induced by sulfur mustard: Sardasht-Iran Cohort Study. Int Immunopharmacol 2009; 9: 1482-1488.
116
117. Panahi Y, Ghanei M, Ghabili K, Ansarin K, Aslanabadi S, Poursaleh Z, Eslam Jamal Golzari S, Etemadi J, Khalili M, Mohajel Shoja M. Acute and chronic pathological effects of sulfur mustard on genitourinary system and male fertility. Urol J 2013; 10: 837-846.
117
118. Ghanei M, Vosoghi AA. An epidemiologic study to screen for chronic myelocytic leukemia in war victims exposed to mustard gas. Environ Health Perspect 2002; 110: 519-521.
118
119. Emad A, Emad Y. Increased granulocyte-colony stimulating factor (G-CSF) and granulocyte-macrophage colony stimulating factor (GM-CSF) levels in BAL fluid from patients with sulfur mustard gas-induced pulmonary fibrosis. J Aerosol Med 2007; 20: 352-360.
119
120. Mostafa Ghanei HF, Mohammad Mir Mohammad, Jafar Aslani, Fariborz Nematizadeh. Long-Term Respiratory Disorders of Claimers with Subclinical Exposure to Chemical Warfare Agents. Inhalation Toxicology 2004; 16: 491-495.
120
121. Gerecke DR, Chen M, Isukapalli SS, Gordon MK, Chang YC, Tong W, Androulakis IP, Georgopoulos PG. Differential gene expression profiling of mouse skin after sulfur mustard exposure: Extended time response and inhibitor effect. Toxicol Appl Pharmacol 2009; 234: 156-165.
121
122. Nishimoto Y, Yamakido M, Ishioka S, Shigenobu T, Yukutake M. Epidemiological studies of lung cancer in Japanese mustard gas workers. Princess Takamatsu Symp 1987; 18: 95-101.
122
123. Norman JE, Jr. Lung cancer mortality in World War I veterans with mustard-gas injury: 1919-1965. J Natl Cancer Inst 1975; 54: 311-317.
123
124. Emad A, Rezaian GR. Characteristics of bronchoalveolar lavage fluid in patients with sulfur mustard gas-induced asthma or chronic bronchitis. Am J Med 1999; 106: 625-628.
124
125. Tang FR, Loke WK. Sulfur mustard and respiratory diseases. Crit Rev Toxicol. 2012; 42: 688-702.
125
126. Paromov V, Suntres Z, Smith M, Stone WL. Sulfur mustard toxicity following dermal exposure: role of oxidative stress, and antioxidant therapy. J Burns Wounds. 2007; 7: e7.
126
127. Emad A, Emad V. Elevated levels of MCP-1, MIP-alpha and MIP-1 beta in the bronchoalveolar lavage (BAL) fluid of patients with mustard gas-induced pulmonary fibrosis. Toxicology 2007; 240: 60-69.
127
128. Emad A, Emad Y. Relationship between eosinophilia and levels of chemokines (CCL5 and CCL11) and IL-5 in bronchoalveolar lavage fluid of patients with mustard gas-induced pulmonary fibrosis. J Clin Immunol 2007; 27: 605-612.
128
129. Sanders YY, Pardo A, Selman M, Nuovo GJ, Tollefsbol TO, Siegal GP, Hagood JS. Thy-1 promoter hypermethylation: a novel epigenetic pathogenic mechanism in pulmonary fibrosis. Am J Respir Cell Mol Biol 2008; 39: 610-618.
129
130. Korkmaz A, Tan DX, Reiter RJ. Acute and delayed sulfur mustard toxicity; novel mechanisms and future studies. Interdiscip Toxicol. 2008; 1: 22-6.
130
131. Shuto T, Furuta T, Oba M, Xu H, Li JD, Cheung J, Gruenert DC, Uehara A, Suico MA, Okiyoneda T, et al. Promoter hypomethylation of Toll-like receptor-2 gene is associated with increased proinflammatory response toward bacterial peptidoglycan in cystic fibrosis bronchial epithelial cells. FASEB J. 2006; 20: 782-784.
131
132. Takahashi K SY, Hosono A, Kaminogawa S. Epigenetic regula-tion of TLR4 gene expression in intestinal epithelial cells for the main-tenance of intestinal homeostasis. J Immunol 2009; 183: 6522-6529.
132
133. Sullivan KE RA, Dietzmann K, Suriano AR, Kocieda VP, Stewart M, et al. Epigenetic regulation of tumor necrosis factor alpha. Mol Cell Biol 2007; 27: 5147-5160.
133
134. Katayama Y TM, Kuwayama H. Helicobacter pylori causes runx3 gene methylation and its loss of expression in gastric epithelial cells, which is mediated by nitric oxide produced by macrophages. Biochem Biophys Res Commun 2009; 388: 496-500.
134
135. Hu JL ZB, Zhang RR, Zhang KL, Zhou JQ, Xu GL. The N-terminus of histone H3 is required for de novo DNA methylation in chromatin. Proc Natl Acad Sci USA 2009; 106: 22187-22192.
135
136. Ishii M WH, Corsa CA, Liu T, Coelho AL, Allen RM, et al. Epigenetic regulation of the alternatively activated macrophage pheno-type. Blood 2009; 114: 3244-3254.
136
137. De Santa F NV, Yap ZH, Tusi BK, Burgold T, Austenaa L, Bucci G, Caganova M, Notarbartolo S, Casola S, Testa G, Sung WK, Wei CL, Natoli G. Jmjd3 contributes to the control of gene expression in LPS-activated macrophage. EMBO J 2009; 28: 3341-3352.
137
138. El Gazzar M YB, Chen X, Hu J, Hawkins GA, McCall CE G9a and HP1 couple histone and DNA methylation to TNFαtranscription silencing during endotoxin tolerance. J Biol Chem 2008; 283: 32198-32208.
138
139. Visel A BM, Li Z, Zhang T, Akiyama JA, Holt A, Plajzer-Frick I, Shoukry M, Wright C, Chen F, Afzal V, Ren B, Rubin EM, Pennacchio LA. ChIP-seq accurately predicts tissue-specific activity of enhancers. Nature. 2009: 854-858.
139
140. Yang J PY, Zhang H, Xu X, Laine GA, Dellsperger KC, Zhang C. Feed-forward signaling of TNF-alpha and NF-kappaB via IKK-beta pathway contributes to insulin resistance and coronary arteriolar dysfunction in type 2 diabetic mice. F Am J Physiol Heart Circ Physiol. 2009; 296: 1850-1858.
140
141. Taganov KD BM, Chang KJ, Baltimore D NF-kappaB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses. Proc Natl Acad Sci USA. 2006; 103: 12481-12486.
141
142. O’Connell RM CA, Rao DS, Baltimore D. Inositol phos-phatase SHIP1 is a primary target of miR-155. Proc Natl Acad Sci USA 2009; 106: 7113-7118.
142
143. Liu G FA, Yang Y, Park YJ, Tsuruta Y, Abraham E. miR-147, a microRNA that is induced upon Toll-like receptor stimulation, regu-lates murine macrophage inflammatory responses. Proc Natl Acad Sci USA 2009; 160: 15819-15824.
143
144. Fabbri M GR, Cimmino A, Liu Z, Zanesi N, Callegari E, et al. MicroRNA-29 family reverts aberrant methylation in lung cancer by targeting DNA methyltransferases 3A and 3. Proc Natl Acad Sci USA. 2007; 104: 15805-15810.
144
145. Hu JL ZB, Zhang RR, Zhang KL, Zhou JQ, Xu GL. The N-terminus of histone H3 is required for de novo DNA methylation in chromatin. Proc Natl Acad Sci USA. 2009; 106: 22187-22192.
145
146. Tuddenham L WG, Ntounia-Fousara S, Waters J, Hajihosseini MK, Clark I, et al. The cartilage specific microRNA-140 targets histone deacetylase 4 in mouse cells. FEBS Lett. 2006; 580: 4214-4217.
146
147. Esposito E, Iacono A, Muia C, Crisafulli C, Mattace Raso G, Bramanti P, Meli R, Cuzzocrea S. Signal transduction pathways involved in protective effects of melatonin in C6 glioma cells. J Pineal Res. 2008; 44: 78-87.
147
148. Deng WG, Tang ST, Tseng HP, Wu KK. Melatonin suppresses macrophage cyclooxygenase-2 and inducible nitric oxide synthase expression by inhibiting p52 acetylation and binding. Blood. 2006; 108: 518-524.
148
149. Nourani MR, Ebrahimi M, Roudkenar MH, Vahedi E, Ghanei M, Imani Fooladi AA. Sulfur mustard induces expression of metallothionein-1A in human airway epithelial cells. Int J Gen Med. 2011; 4: 413-419.
149
150. Mirbagheri L, Habibi Roudkenar M, Imani Fooladi AA, Ghanei M, Nourani MR. Downregulation of super oxide dismutase level in protein might be due to sulfur mustard induced toxicity in lung. Iran J Allergy Asthma Immunol. 2013; 12: 153-160.
150
151. Wynn TA. Integrating mechanisms of pulmonary fibrosis. J Exp Med. 2011; 208: 1339-50.
151
152. Yunes Panahi RM-L, Farshid Alaeddini, Mohammad Mehdi Naghizadeh, Jafar Aslani, Mostafa Ghanei. Furosemide Inhalation in Dyspnea of Mustard Gas-Exposed Patients: A Triple-Blind Randomized Study. Inhalation Toxicology. 2008; 20: 873-877.
152
153. Adelipour M, Imani Fooladi AA, Yazdani S, Vahedi E, Ghanei M, Nourani MR. Smad molecules expression pattern in human bronchial airway induced by sulfur mustard. Iran J Allergy Asthma Immunol. 2011; 10: 147-154.
153
154. Mostafa Ghanei AAH. Molecular and cellular mechanism of lung injuries due to exposure to sulfur mustard: a review. Inhalation Toxicology. 2011; 23: 363-371.
154
155. Mirsadraee M, Attaran D, Boskabady MH, Towhidi M. Airway hyperresponsiveness to methacholine in chemical warfare victims. Respiration. 2005; 72: 523-528.
155
156. Ghanei M MN, Ali Morad Kosar, Ali Amini Harandi, Nicholas S. Hopkinson, Zohreh Poursaleh. Long-term pulmonary complications of chemical warfare agent exposure in Iraqi Kurdish civilians. Inhalation Toxicology. 2010; 22: 719-724.
156
157. Panahi Y, Ghanei M, Vahedi E, Ghazvini A, Parvin S, Madanchi N, Bagheri M, Sahebkar A. Effect of recombinant human IFNgamma in the treatment of chronic pulmonary complications due to sulfur mustard intoxication. J Immunotoxicol. 2014; 11: 72-77.
157
158. Panahi Y, Sarayani A, Beiraghdar F, Amiri M, Davoudi SM, Sahebkar A. Management of sulfur mustard-induced chronic pruritus: a review of clinical trials. Cutan Ocul Toxicol. 2012; 31: 220-225.
158
ORIGINAL_ARTICLE
Electrophysiologic and clinico-pathologic characteristics of statin-induced muscle injury
Objective(s):In this study, we aimed at evaluation of electrophysiological and histopathalogical characteristics of statin-induced muscle injury as well as clinical features of patients who develop this condition in terms of frequency and pattern of evolution. Materials and Methods: Forty patients (age 39-74 years) including 25 subjects with type 2 diabetes mellitus, 9 with cardiovascular diseases and 6 with hyperlipidemia, who were receiving atrovastatin 40 mg/day for variable period, were studied. Thirty three healthy subjects (age 31-74 years) served as control group. Creatine phosphokinease level, thyroid function, motor unit potential parameters and muscle fiber conduction velocity of biceps brachii and tibialis anterior muscles were measured.Results: Creatine phosphokinase level was elevated in statin users, particularly in those with diabetes mellitus. Less than 50% of statinusers experienced symptoms related to muscle injury. Muscle fiber conduction velocity of the biceps brachii muscle was significantly reduced. Statinusers with diabetes mellitus showed significant changes in electrophysiological parameters as compared to those with cardiovascular diseases and hyperlipidemia. Muscle biopsies showed muscle fiber variation in size, fibrosis and mild inflammatory cell infiltration. Immunohistochemical evaluation of muscle biopsies showed positive expression of Bcl-2 and one patient showed positive P53 immunohistochemical expression with elevated level of creatine phosphokinase. Conclusion: Atorvastatin increased average creatine kinase, suggesting, statins produce mild muscle injury even in asymptomatic subjects. Diabetic statin users were more prone to develop muscle injury than others. Muscle fiber conduction velocity evaluation is recommended as a simple and reliable test to diagnose statin-induced myopathy instead of invasive muscle biopsy.
https://ijbms.mums.ac.ir/article_4723_84cffbbb8a65638d1831d54eb76d5a10.pdf
2015-08-01
737
744
10.22038/ijbms.2015.4723
Statin
EMG
MFCV
Histopathology
Immune histochemistry
Muscle injury
Mohammed
Abdulrazaq
1
Department of Physiology, College of Medicine, Al-Nahrain University, Baghdad, Iraq
AUTHOR
Farqad
Hamdan
farqadbhamdan@colmed-alnahrain.edu.iq
2
Department of Physiology, College of Medicine, Al-Nahrain University, Baghdad, Iraq
LEAD_AUTHOR
Waseem
Al-Tameemi
abualameer72@yahoo.com
3
Department of Medicine, College of Medicine, Al-Nahrain University, Baghdad, Iraq
AUTHOR
1. Abd TT, Jacobson TA. Statin-induced myopathy: a review and update. Expert Opin Drug Saf 2011; 10:373-387.
1
2. Parker BA, Capizzi JA, Grimaldi AS, Clarkson PM, Cole SM, Keadle J, et al. Effect of statins on skeletal muscle function. Circulation 2013; 127:96-103.
2
3. Banach M, Serban C, Sahebkar A, Ursoniu S, Rysz J, Muntner P, et al. Effects of coenzyme Q10 on statin-induced myopathy: A Meta-analysis of randomized controlled trials. Mayo Clin Proc 2015; 90:24-34.
3
4. Al-Sulaiman AA, Al-Khamis FA. Statin-induced myopathy: a clinical perspective. Bahrain Med Bull 2009; 31.
4
5. Joy TR, Hegele RA. Narrative review: statin-related myopathy. Ann Intern Med 2009; 150:858-68.
5
6. McKenney JM, Davidson MH, Jacobson TA, Guyton JR. National lipid association statin safety assessment task force. Final conclusions and recommendations of the National Lipid Association Statin Safety Assessment Task Force. Am J Cardiol 2006; 97:89C-94C.
6
7. Tomaszewski M, Stępień KM, Tomaszewska J, Czuczwar SJ. Statin-induced myopathies. Pharmacol Rep 2011; 63:859-66.
7
8. Paganoni S, Amato A. Electrodiagnostic Evaluation of myopathies. Phys Med Rehabil Clin N Am 2013; 24:193-207.
8
9. Baer AN, Wortmann RL. Myotoxicity associated with lipid-lowering drugs. Curr Opin Rheumatol 2007; 19:67-73.
9
10. Phillips PS, Haas RH, Bannykh S, Hathaway S, Gray NL, Kimura BJ, et al. Statin-associated myopathy with normal creatine kinase levels. Ann Intern Med 2002; 137:581-585.
10
11. Findling O, Meier N, Sellner J, Nedeltchev K, Arnold M. Clinical reasoning: rhab- domyolysis after combined treatment with simvastatin and fluconazole. Neurology 2008; 71:e34-e37.
11
12. Radcliffe KA, Campbell WW. Statin myopathy. Curr Neurol Neurosci Rep 2008; 8:66-72.
12
13. Sinzinger H, Wolfram R, Peskar BA. Muscular side effects of statins. J Cardiovasc Pharmacol 2002; 40:163-71.
13
14. Huynh T, Cordato D, Yang F, Choy T, Johnstone K, Bagnall F, et al. HMG CoA reductase-inhibitor-related myopathy and the influence of drug interactions. Intern Med J 2002; 32:486-490.
14
15. Grable-Esposito P, Katzberg HD, Greenberg SA, Srinivasan J, Katz J, Amato AA. Immune-mediated necrotizing myopathy associated with statins. Muscle Nerve 2010; 41:185-190.
15
16. American Diabetes Association. Standards of medical care in diabetes -2014. Diab Care 2014; 37:S1.
16
17. Ahmad Z. Statin intolerance. Am J Cardiol 2014; 113:1765-1767.
17
18. Gloth FM III, Scheve AA, Stober CV, Chow S, Prosser J. The functional pain scale: reliability, validity, and responsiveness in an elderly population. J Am Med Dir Assoc 2001; 2:110-114.
18
19. Troni W, Cantello R, Rainero I. Conduction velocity along human muscle fibers in situ. Neurology 1983; 33:1453-1459.
19
20. Wald JJ. The effects of toxins on muscle. Neurol Clin 2000; 18:695-717.
20
21. Sieb JP, Gillessen T. Iatrogenic and toxic myopathies. Muscle Nerve 2003; 27:142-156.
21
22. Dalakas MC. Toxic and drug-induced myopathies. J Neurol Neurosurg Psychiat 2009; 80:832-838.
22
23. Mammen AL, Amato AA. Statin myopathy: a review of recent progress. Curr Opin Rheumatol 2010; 22: 644-650.
23
24. Karas RH , Mohaupt MG, Babiychuk EB, Sanchez-Freire V, Monastyrskaya K, Iyer L, et al. Association between statin-associated myopathy and skeletal muscle damage. CMAJ 2009; 181:E11-E18.
24
25. Valiyil R, Christopher-Stine L. Drug-related myopathies of which the clinician should be aware. Curr Rheumatol Rep 2010; 12:213-220.
25
26. Bruckert E, Hayem G, Dejager S, Yau C, Bégaud B. Mild to moderate muscular symptoms with high-dosage statin therapy in hyperlipidemic patients – the PRIMO study. Cardiovasc Drugs Ther 2005; 19:403-414.
26
27. Kashani A, Phillips CO, Foody JM, Wang Y, Mangalmurti S, Ko DT, et al. Risks associated with statin therapy: a systematic overview of randomized clinical trials. Circulation 2006; 114:2788-2797.
27
28. Chatzizisis Y, Koskinas KC, Misirli G, Vaklavas C, Hatzitolios A, Giannoglou GD. Risk factors and drug interactions predisposing to statin-induced myopathy. Drug Saf 2010; 33:171-187.
28
29. Hansen KE, Hildebrand JP, Ferguson EE, Stein JH. Outcomes in 45 patients with statin associated myopathy. Arch Intern Med 2005; 165:2671-2676.
29
30. Mantel-Teeuwisse AK, Klungel OH, Herings RM, van Puijenbroek EP, Porsius AJ, de Boer A. Myopathy due to statin/fibrate use in the Netherlands. Ann Pharmacother 2002; 36:1957-1960.
30
31. Wright RS, Murphy JG, Bybee KA, Kopecky SL, LaBlanche JM. Statin lipid-lowering therapy for acute myocardial infarction and unstable angina: efficacy and mechanism of benefit. Mayo Clin Proc 2002; 77:1085-1092.
31
32. Rubin DI, Daube JR. Application of clinical neurophysiology: assessing peripheral neuromuscular symptom complexes. In: Daube JR, Rubin DI. Linical Neurophysiology.3rd ed. Chapter 47. Oxford University Press; 2009. p.827.
32
33. Strommen JA, Johns JS, Kim CT, Williams FH, Weiss LD, Weiss JM, et al. Neuromuscular rehabilitation and electrodiagnosis. 3. Diseases of muscles and neuromuscular junction. Arch Phys Med Rehabil 2005; 86:S18-27.
33
34. Hanaoka BY, Peterson CA, Horbinski C, Crofford LJ. Implications of glucocorticoid therapy in idiopathic inflammatory myopathies. Nat Rev Rheumatol 2012; 8:448-457.
34
35. Gutiérrez GG, Lopez CB, Navacerrada F, Martínez AM. Use of electromyography in the diagnosis of inflammatory myopathies. Reumatol Clin 2012; 8:195-200.
35
36. Andreassen S, Arendt-Nielsen L. Muscle fiber conduction velocity in motor units of the human anterior tibial muscle: a new size principle parameter. J Physiol 1987; 391:561-571.
36
37. Blijham PJ, Ter Laak HJ, Schelhaas HJ, van Engelen BG, Stegeman DF, Zwarts MJ. Relation between muscle fiber conduction velocity and fiber size in neuromuscular disorders. J Appl Physiol 2006; 100:1837-1841.
37
38. Minetto MA, Botter A, Lanfranco F, Baldi M, Ghigo E, Arvat E. Muscle fiber conduction slowing and decreased levels of circulating muscle proteins after short-term dexamethasone administration in healthy subjects. J Clin Endocrinol Metab 2010; 95:1663-1671.
38
39. Sacher J, Weigl L, Werner M, Szegedi C, Hohenegger M. Delineation of myotoxicity induced by 3-hydroxy-3-methylglutaryl CoA reductase inhibitors in human skeletal muscle cells. J Pharmacol Exp Ther 2005; 314:1032-1041.
39
40. Matzno S, Yasuda S, Juman S, Yamamoto Y, Nagareya-Ishida N, Tazuya-Murayama K, et al. Statin-induced apoptosis linked with membrane farnesylated Ras small G protein depletion, rather than geranylated Rho protein. J Pharm Pharmacol 2005; 57:1475-1484.
40
41. Achanta G, Huang P. Role of p53 in sensing oxidative DNA damage in response to reactive oxygen species generating agents. Cancer Res 2004; 64:6233-6239.
41
42. Cafforio P, Dammacco F, Gernone A, Silvestris F. Statins activate the mitochondrial pathway of apoptosis in human lymphoblasts and myeloma cells. Carcinogenesis 2005; 26:883-891.
42
43. Seicean S, Seicean A, Plana JC, Budd GT, Marwick TH. Effect of statin therapy on the risk for incident heart failure in patients with breast cancer receiving anthracycline chemotherapy an observational clinical cohort study. J Am Coll Cardiol 2012; 60:2384-2390.
43
44. Alzira A, Carvalho S, Poti Lima ÜW, Valiente RA. Statin and fibrate associated myopathy: Study of eight patients. Arq Neuropsiquiatr 2004; 62:257-261.
44
45. Law M, Rudnicka AR. Statin safety: A systematic review. Am J Cardiol 2006; 97: 52c-60c.
45
46. Josan K, Majumdar SR, McAlister FA. The Efficacy and safety of intensive statin therapy: A Meta-analysis of randomized trials. CMAJ 2008; 178:576-84.
46
47. Dostalek M, Sam WJ, Paryani KR, Macwan JS, Gohh RY, Akhlaghi F. Diabetes mellitus reduces the clearance of atorvastatin lactone: results of a population pharmacokinetic analysis in renal transplant recipients and in vitro studies using human liver microsomes. Clin Pharmacokinet 2012; 51:591-606.
47
48. Marcoff L, Thompson PD. The role of coenzyme Q10 in statin-associated myopathy. J Am Coll Cardiol 2007; 49:2231-2237.
48
ORIGINAL_ARTICLE
Antidiabetic effect of honey feeding in noise induced hyperglycemic rat: involvement of oxidative stress
Objective(s):In this study the effect of oral administration of honey on serum glucose, lipids, stress oxidative markers, and morphology of langerhans islets in noise induced hyperglycemic rats was investigated.
Materials and Methods: Male Wistar rats were divided into control, hyperglycemic, honey treated control, and honey treated hyperglycemic groups. For induction of hyperglycemia, noise stress was used. Serum glucose, triglyceride (TG), total cholesterol, low density lipoprotein (LDL), and high density lipoprotein (HDL)-cholesterol levels were determined before the study and at 4th and 8th weeks after the study. Markers of oxidative stress in brain were also measured. Morphology of langerhans islets in four groups was evaluated using Gomori staining method.
Results: Treatment of noise induced hyperglycemic rats with honey produced a hypoglycemic effect and appropriate changes regarding serum lipids in treated diabetic group at 4th and 8th weeks as compared to the control group. Meanwhile, honey treatment significantly ameliorated the increased malondialdehyde (MDA) content and reduced the activity of superoxide dismutase (SOD) in brain. Histology of langerhans islets in hyperglycemic group showed a lower number and granularity of beta cells; honey treatment produced beneficial change in this respect.
Conclusion: Oral administration of honey in experimental model of diabetes showed a significant hypoglycemic effect and led to appropriate changes in serum lipid profiles.
https://ijbms.mums.ac.ir/article_4724_f5512d5dfbc71675872d7e5c0f7ebe7d.pdf
2015-08-01
745
751
10.22038/ijbms.2015.4724
Beta cell
Diabetes Mellitus
Glucose
Honey
Lipid
Noise
Rat
Saiedeh
Arabmoazzen
s_moazzen83@yahoo.com
1
Deptartment of Biology, Basic Sciences Faculty, Sciences and Researches, Azad University, Tehran, Iran
AUTHOR
Alireza
Sarkaki
sarkaki_a@ajums.ac.ir
2
Deptartment of Physiology, Physiology Research Center, School of Medicine, Jundishapur University of Medical Sciences, Ahvaz, Iran
AUTHOR
Ghasem
saki
3
Deptartment of Anatomy, Physiology Research Center, School of Medicine, Jundishapur University of Medical Sciences, Ahvaz, Iran
AUTHOR
Mohammad Ali
Mirshekar
ma_mib78@yahoo.com
4
Department of Physiology, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran
LEAD_AUTHOR
1. Mahmood R, Khan GJ, Alam S, Safi AJ. Effect of 90 decibel noise of 4000 hertz on blood pressure in young adults. J Ayub Med Coll Abbottabad 2003; 16:30-33.
1
2. Babisch W. The noise/stress concept, risk assessment and research needs. Noise Health 2002; 4:1.
2
3. Babisch W. Epidemiological studies of the cardiovascular effects of occupational noise-a critical appraisal. Noise Health 1998; 1:24.
3
4. Theebe MA. Planes, trains, and automobiles: the impact of traffic noise on house prices. J Real Estate Finance and Economics 2004; 28:209-234.
4
5. Van Kempen EE, Kruize H, Boshuizen HC, Ameling CB, Staatsen BA, de Hollander AE. The association between noise exposure and blood pressure and ischemic heart disease: a meta-analysis. Environ Health Perspect 2002; 110:307.
5
6. Maschke C, Harder J, Ising H, Hecht K, Thierfelder W. Stress hormone changes in persons exposed to simulated night noise Noise Health 2002; 5:35.
6
7. Gate L, Paul J, Ba GN, Tew K, Tapiero H. Oxidative stress induced in pathologies: the role of antioxidants. Biomed Pharmacol 1999; 53:169-180.
7
8. Packer L, Tritschler HJ, Wessel K. Neuroprotection by the metabolic antioxidant [alpha]-lipoic acid. Free Radic Biol Med 1997; 22:359-378.
8
9. Fridovich I. Superoxide anion radical (O• ̄2), superoxide dismutases, and related matters. J Biol Chem 1997; 272:18515-18517.
9
10. Madrigal JL, Olivenza R, Moro MA, Lizasoain I, Lorenzo P, Rodrigo J, et al. Glutathione depletion, lipid peroxidation and mitochondrial dysfunction are induced by chronic stress in rat brain. Neuropsychopharm 2001; 24:420-429.
10
11. Van Campen LE, Murphy WJ, Franks JR, Mathias PI, Toraason MA. Oxidative DNA damage is associated with intense noise exposure in the rat. Hear Res 2002; 164:29-38.
11
12. Molan PC. The antibacterial activity of honey: 2. Variation in the potency of the antibacterial activity. 1992.
12
13. Molan P. Honey as an antimicrobial agent. Bee Products: Springer; 1997.p.27-37.
13
14. Beretta G, Granata P, Ferrero M, Orioli M, Maffei Facino R. Standardization of antioxidant properties of honey by a combination of spectrophotometric/fluorimetric assays and chemometrics. Anal Chim Acta 2005; 533:185-191.
14
15. Nagai T, Inoue R, Kanamori N, Suzuki N, Nagashima T. Characterization of honey from different floral sources. Its functional properties and effects of honey species on storage of meat. Food Chem 2006; 97:256-262.
15
16. Martos I, Ferreres F, Yao L, D'Arcy B, Caffin N, Tomás-Barberán FA. Flavonoids in monospecific Eucalyptus honeys from Australia. J Agric Food Chem 2000; 48:4744-4748.
16
17. Machha A, Mustafa MR. Chronic treatment with flavonoids prevents endothelial dysfunction in spontaneously hypertensive rat aorta. J Cardiovasc Pharmacol 2005; 46:36-40.
17
18. Estevinho L, Pereira AP, Moreira L, Dias LG, Pereira E. Antioxidant and antimicrobial effects of phenolic compounds extracts of Northeast Portugal honey. Food Chem Tox 2008; 46:3774-3779.
18
19. Roghani M, Baluchnejadmojarad T. Chronic epigallocatechin-gallate improves aortic reactivity of diabetic rats: underlying mechanisms. Vascul Pharmacol 2009; 51:84-89.
19
20. Roghani M, Baluchnejadmojarad T. Hypoglycemic and hypolipidemic effect and antioxidant activity of chronic epigallocatechin-gallate in streptozotocin-diabetic rats. Pathophysiology 2010; 17:55-59.
20
21. Roghani M, Baluchnejadmojarad T. Mechanisms underlying vascular effect of chronic resveratrol in streptozotocin‐diabetic rats. Phytother Res 2010; 24:S148-S54.
21
22. Friedewald WT, Levy RI, Fredrickson DS. Estimation of the concentration of low-density lipoprotein cholesterol in plasma, without use of the preparative ultracentrifuge. Clin Chem 1972; 18:499-502.
22
23. Carrasco GA, Van de Kar LD. Neuroendocrine pharmacology of stress. Euro J Pharm 2003; 463:235-272.
23
24. Makino S, Asaba K, Nishiyama M, Hashimoto K. Decreased type 2 corticotropin-releasing hormone receptor mRNA expression in the ventromedial hypothalamus during repeated immobilization stress. Neuroendocrinology 1999; 70:160-167.
24
25. la Fleur SE, Akana SF, Manalo SL, Dallman MF. Interaction between corticosterone and insulin in obesity: regulation of lard intake and fat stores. Endocrinology 2004; 145:2174-2185.
25
26. Gao B, Kikuchi-Utsumi K, Ohinata H, Hashimoto M, Kuroshima A. Repeated immobilization stress increases uncoupling protein 1 expression and activity in Wistar rats. Jpn J Physiol 2003; 53:205-214.
26
27. Akana SF, Strack AM, Hanson ES, Horsley CJ, Mulligan ED, Bhatnagar S, et al. Interactions among chronic cold, corticosterone and puberty on energy intake and deposition. Stress 1999; 3:131-46.
27
28. Lin YH, Liu AH, Xu Y, Tie L, Yu HM, Li XJ. Effect of chronic unpredictable mild stress on brain–pancreas relative protein in rat brain and pancreas. Behav Brain Res 2005; 165:63-71.
28
29. Toleikis PM, Godin DV. Alteration of antioxidant status in diabetic rats by chronic exposure to psychological stressors. Pharmacol Biochem Behav 1995; 52:355-366.
29
30. Gill-Sharma M, D’Souza S, Parte P, Balasinor N, Choudhuri J, Majramkar D, et al. Effect of oral tamoxifen on semen characteristics and serum hormone profile in male bonnet monkeys. Contraception 2003; 67:409-413.
30
31. Abdul-Ghani AS, Dabdoub N, Muhammad R, Abdul-Ghani R, Qazzaz M. Effect of palestinian honey on spermatogenesis in rats. J Med Food 2008; 11:799-802.
31
32. Siti A. Honey and reproductive hormones. Malays J Med Sci 2007; 14:105-106.
32
33. Kenjerić D, Mandić ML, Primorac L, Bubalo D, Perl A. Flavonoid profile of< i> Robinia</i> honeys produced in Croatia. Food Chem 2007; 102:683-690.
33
34. Mirshekar M, Roghani M, Khalili M, Baluchnejadmojarad T, Moazzen SA. Chronic oral pelargonidin alleviates streptozotocin-induced diabetic neuropathic hyperalgesia in rat: involvement of oxidative stress. Iran Biomed J 2010; 14:33.
34
35. Yanardağ R, Bolkent Ş, Özsoy‐Saçan Ö, Karabulut‐Bulan Ö. The effects of chard (Beta vulgaris L. var. cicla) extract on the kidney tissue, serum urea and creatinine levels of diabetic rats. Phytother Res 2002; 16:758-761.
35
ORIGINAL_ARTICLE
Antinociceptive effects of maprotiline in a rat model of peripheral neuropathic pain: possible involvement of opioid system
Objective(s): Neuropathic pain remains a clinical problem and is poorly relieved by conventional analgesics. This study was designed to determine whether maprotiline administration was effective in alleviating symptoms of neuropathic pain and whether the antinociceptive effect of maprotiline mediated through the opioid system.
Materials and Methods: Neuropathic pain was induced by chronic constriction injury (CCI) of the sciatic nerve in rats, which resulted in thermal hyperalgesia, and mechanical and cold allodynia. Maprotiline (10, 20 and 40 mg/kg, IP) was administered on the 7th and 14th days after surgery. To study the role of the opioid system in the antinociceptive effects of maprotiline, maprotiline (20 mg/kg, IP) was administered in combination with naloxone (1 mg/kg, SC) on the 7th post-surgery day. Behavioral tests were done at 45 min after drug injections on the 7th and 14th days after surgery.
Results:Systemic administration of maprotiline blocked heat hyperalgesia, cold allodynia and reduced mechanical allodynia. Also antihyperalgesic effect of maprotiline was reversed by pretreatment with naloxone.
Conclusion: Our results suggest that maprotiline can be considered a potential therapeutic for the treatment of neuropathic pain, and the opioid system may be involved in the antihyperalgesic effects of maprotiline.
https://ijbms.mums.ac.ir/article_4725_f76f2556875f5908f429ac6286afb603.pdf
2015-08-01
752
757
10.22038/ijbms.2015.4725
Maprotiline
Naloxone
Neuropathic pain
Opioids
Rat
Hamid Reza
Banafshe
1
Physiology Research Center, Kashan University of Medical Sciences, Kashan, Iran
AUTHOR
Valiollah
Hajhashemi
hajhashemi@ pharm.mui.ac.ir
2
Department of Pharmacology and Toxicology and Isfahan Pharmaceutical Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Mohsen
Minaiyan
miniyan@pharm.mui.ac.ir
3
Department of Pharmacology and Toxicology and Isfahan Pharmaceutical Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Azam
Mesdaghinia
mesdaghiniaazam@yahoo.com
4
Physiology Research Center, Kashan University of Medical Sciences, Kashan, Iran
AUTHOR
Alireza
Abed
dralirezaabed@yahoo.com
5
Department of Pharmacology, School of Medicine, Kashan University of Medical Sciences, Kashan, Iran
LEAD_AUTHOR
1. Zhuo M. Neuronal mechanism for neuropathic pain. Mol Pain 2007; 3:1–9.
1
2. Ro L S, Jacobs J M. The role of the saphenous nerve in experimental sciatic nerve mononeuropathy produced by loose ligatures: a behavioral study. Pain 1993; 52:359-369.
2
3. Guindon J, Hohmann AG. Recent advances in the pharmacological management of pain. Drugs 2007; 67:2121–2133.
3
4. Bennett G, Xie YK. A peripheral mononeuropathy in rat that produces disorders of pain sensation like those seen in man. Pain 1988; 33:87-107.
4
5. Zychowska M, Rojewska E, Makuch W, Przewlocka B, Mika J. The influence of microglia activation on the efficacy of amitriptyline, doxepin, milnacipran, venlafaxine and fluoxetine in a rat model of neuropathic pain. Eur J Pharmacol. 2015; 749:115-123.
5
6. Hajhashemi V, Banafshe HR, Minaiyan M, Mesdaghinia A, Abed A. Antinociceptive effects of venlafaxine in a rat model of peripheral neuropathy: Role of alpha2-adrenergic receptors. Eur J Pharmacol. 2014; 5:230-236.
6
7. Ahles S, Gwirtsman H, Halaris A, Shah P, Schwarcz G, Hill MA. Comparative cardiac effects of maprotiline and doxepin in elderly depressed patients. J Clin Psychiatry 1984; 45:460–465.
7
8. Gruter W, Poldinger W, Maprotiline. Mod Probl Pharmacopsychiatry. 1982; 18:17–48.
8
9. Nakajima K, Obata H, Iriuchijima N, Saito S. An increase in spinal cord noradrenaline is a major contributor to the antihyperalgesic effect of antidepressants after peripheral nerve injury in the rat. Pain 2012; 153:990-997.
9
10. Yokogawa F, Kiuchi Y, Ishikawa Y, Otsuka N, Masuda Y, Oguchi K, et al. An investigation of monoamine-receptorsinvolved in antinociceptiveeffects of antidepressants. Anesth Analg 2002; 95:163-168.
10
11. Korzeniewska-Rybicka I, Plaznik A. Supraspinally mediated analgesic effect of antidepressant drugs. Pol J Pharmacol 2000; 52:93–99.
11
12. Vrethem M, Boivie J, Arnqvist H, Holmgren H, Lindstrom T, Thorell LH. A comparison of amitriptyline and maprotiline in the treatment of painful polyneuropathy in diabetics and nondiabetics. Clin J Pain 1997; 13:313-323.
12
13. Watson CP, Chipman M, Reed K, Evans RJ, Birkett N. Amitriptyline versus maprotiline in postherpetic neuralgia: a randomized, double-blind, crossover trial. Pain 1992; 48: 29-36.
13
14. Obata H, Saito S, Koizuka S, Nishikawa K, Goto F. The monoamine-mediated antiallodyniceffects of intrathecally administered milnacipran, a serotonin noradrenaline reuptake inhibitor, in a rat model of neuropathic pain. Anesth Analg 2005; 100:1406-1410.
14
15. Pettersen VL, Zapata-Sudo G, Raimundo JM, Trachez MM, Sudo RT. The synergistic interaction between morphine and maprotiline after intrathecal injection in rats. Anesth Analg 2009; 109:1312-1317.
15
16. Lee RL, Spencer PS. Effect of tricyclic antidepressants on analgesic activity in laboratory animals. Postgrad Med J 1980; 1:19-24.
16
17. Verdi J, Jafari-Sabet M, Mokhtari R, Mesdaghinia A, Banafshe HR. The effect of progesterone on expression and development of neuropathic pain in a rat model of peripheral neuropathy. Eur J Pharmacol 2013; 699:207-212.
17
18. Amin B, Hajhashemi V, Hosseinzadeh H, Abnous Kh. Antinociceptive evaluation of ceftriaxone and minocycline alone and in combination in a neuropathic pain model in rat. Neuroscience 2012; 224:15-25.
18
19. Banafshe HR, Mesdaghinia A, Arani MN, Ramezani MH, Heydari A, HamidiGA. Lithium attenuates pain-related behavior in a rat model of neuropathic pain: possible involvement of opioid system. Pharmacol Biochem Behav 2012; 100:425-430.
19
20. Banafshe H, Hamidi GA, Noureddini M, Mirhashemi M, Mokhtaria M, Shoferpour M. Effect of curcumin on diabetic peripheral neuropathic pain: possible involvement of opioid system. Eur J Pharmacol 2014; 723:202-206.
20
21. Hamidi GA, Ramezani MH, Arani MN, Talaei SA, Mesdaghinia A, Banafshe HR. Ethosuximide reduces allodynia and hyperalgesia and potentiates morphine effects in the chronic constriction injury model of neuropathic pain. Eur J Pharmacol 2012; 674:260-264.
21
22. Hajhashemi V, Sadeghi H, Minaiyan M, Movahedian A, Talebi A. Central and peripheral anti-inflammatory effects of maprotiline on carrageenan-induced paw edema in rats. Inflamm Res 2012; 59:1053-1059.
22
23. Darcym P, Dredge K, Kellehir P, Kelly JP, Leonard BE, Chambers PL. Acutetoxicityprofile of maprotiline in the rat. Pharmacol Toxicol 1999; 85:276-281.
23
24. Collins SL, Moore RA, McQuay HJ, Wiffen P. Antidepressants and anticonvulsants for diabetic neuropathy and postherpetic neuralgia: a quantitative systematic review. J Pain Symptom Manage 2000; 20:449–458.
24
25. Fishbain DA, Cutler R, Rosomoff HL, Rosomoff RS. Evidence-based data from animal and human experimental studies on pain relief with antidepressants: a structured review. Pain Med 2000; 1:310–316.
25
26. McQuay JH, Tramer M, Nue BA, Carroll D, Wiffen PJ, Moore RA. A systematic review of antidepressants in neuropathic pain. Pain 1996; 68:217–227.
26
27. Jia HB, Wang XM, Qiu LL, Liu XY, Shen JC, Ji Q, et al. Spinal neuroimmune activation inhibited by repeated administration of pioglitazone in rats after L5 spinal nerve transection. Neurosci Lett 2013; 543:130-135.
27
28. Brittain JM, Duarte DB, Wilson SM, Zhu W, Ballard C, Johnson PL, et al. Suppression of inflammatory and neuropathic pain by uncoupling CRMP-2 from the presynapthic Ca²⁺ channel complex. Nat Med 2011; 17:822-829.
28
29. Goff JR, Burkey AR, Goff DJ, Jasmin L. Reorganization of the spinal dorsal horn in models of chronic pain: correlation with behaviour. Neuroscience 1998; 82:559–574.
29
30. Porreca F, Tang QB, Bian D, Riedl M, Elde R, Lai J. Spinal opioid mu receptor expressionin lumbar spinal cord of rats following nerve injury. Brain Res 1998; 795:197-203.
30
31. Rashid MH, Inoue M, Toda K, Ueda H. Loss of peripheral morphine analgesia contributesto the reduced effectiveness of systemic morphine in neuropathic pain. J Pharmacol Exp Ther 2004; 309: 380–387.
31
32. Back SK, Lee J, Hong SK, Na HS. Loss of spinal mu-opioid receptor is associated with mechanical allodynia in a rat model of peripheral neuropathy. Pain 2006; 123:117-126.
32
33. Yeomans DC, Proudfit HK. Nociceptive responses to high and low rates of noxious cutaneous heating are mediated by different nociceptors in the rat: behavioral evidence. Pain 1996; 68:133–140.
33
34. Gautron M, Jazat F, Ratinahirana H, Hauw JJ, Guilbaud G. Alterations in myelinated fibres in the sciatic nerve of rats after constriction: possible relationships between the presence of abnormal small myelinated fibres and pain-related behavior. Neurosci Lett 1990; 111:28–33.
34
35. Dhaka A, Murray AN, Mathur J, Earley TJ, Petrus MJ, Patapoutian A. TRPM8 is required for cold sensation in mice. Neuron 2007; 54:371–378.
35
ORIGINAL_ARTICLE
Inhibition of Pseudomonas aeruginosa biofilm formation by 2,2’-bipyridyl, lipoic, kojic and picolinic acids
Objective(s):The inhibitory effects of iron chelators, and FeCl3 chelation on biofilm formation and swarming motility were investigated against an opportunistic human pathogen Pseudomonas aeruginosa. Materials and Methods:The inhibitory activity of 2,2’-bipyridyl, lipoic acid, kojic acid and picolinic acidonbiofilm formation of P. aeruginosa strain PAO1 and three clinical isolates (P. aeruginosa PAK01,P. aeruginosa PAK02 and P. aeruginosa PAK03) were investigated, based on crystal violet assay, and swarming motility test. Results:The kojic, lipoic and picolinic acid inhibited biofilm formation by 5-33% in all tested P. aeruginosa isolates. When chelated iron was added, biofilm inhibition rates were determined to be 39-57%. Among the tested chelators against P. aeruginosa, lipoic acid (84%) and kojic acid (68%) presented the highest inhibition of swarming motility. This is the first study to report the inhibitory effect of lipoic acid on biofilm formation and swarming motility of P. aeruginosa. Conclusion: It is considered that lipoic and picolinic acids can serve as alternatives for the treatment of the P. aeruginosa infections by inhibiting biofilm formation.
https://ijbms.mums.ac.ir/article_4726_bca48e854e39f5fe8906b93594d70418.pdf
2015-08-01
758
763
10.22038/ijbms.2015.4726
Alpha lipoic acid
Biofilm
Kojic acid
Picolinic acid
Pseudomonas aeruginosa
Swarming motility
Kübra
Çevik
1
Department of Biology, Suleyman Demirel University, 32260 Isparta, Türkiye
AUTHOR
Seyhan
Ulusoy
seyhanulusoy@sdu.edu.tr
2
Department of Biology, Suleyman Demirel University, 32260 Isparta, Türkiye
LEAD_AUTHOR
1. Van Delden C, Iglewski BH. Cell-to-cell signaling and Pseudomonas aeruginosa infection. Emerg Infect Dis 1998; 4:551-560.
1
2. Costerton JW, Stewart PS, Greenberg EP. Bacterial biofilms: a commoncause of persistent infections. Science 1999; 284:1318-1322.
2
3. Parsek MR, Singh PK. Bacterial biofilms: an emerging link to disease pathogenesis. Ann Rev Microbiol 2003; 57:677-701.
3
4. Banin E, Vasil ML, Greenberg EP. Iron and Pseudomonas aeruginosa biofilm formation. Proc Natl Acad Sci USA 2005; 102:11076-11081.
4
5. Oglesby AG, Farrow JM, Lee JH, Tomaras AP, Greenberg EP, Pesci EC, et al. The Influence of iron on Pseudomonas aeruginosa physiology. J Biol Chem 2008; 283:15558-15567.
5
6. Braud A, Hannauer M, Mislin GLA, and Schalk IJ. The Pseudomonas aeruginosa Pyochelini iron uptake pathway and its metal specificity. J Bacteriol 2009; 191:3517-3525.
6
7. Bjorn MJ, Sokol PA, Iglewski BH. Influence of iron on yields of extracellular products in Pseudomonas aeruginosa cultures. J Bacteriol 1979; 138:193-200.
7
8. Johnson MK, Boese-Marrazzo D. Production and properties of heat-stable extracellular hemolysin from Pseudomonas aeruginosa. Infect Immun 1980; 29:1028-1033.
8
9. Pearson JP, Pesci EC, and Iglewski BH. Roles of Pseudomonas aeruginosa las and rhl quorum sensing systems in control of elastase and rhamnolipid biosynthesis genes. J Bacteriol 1997; 179:5756-5767.
9
10. Steindler L, Bertani I, De Sordi L, Schwager S, Eberl, Venturi V. LasI/R and RhlI/R quorum sensing in a strain of Pseudomonas aeruginosa beneficial to plants. Appl Environ Microbiol 2009; 75:5131-5140.
10
11. Ochsner UA, Reiser J. Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa. Proc Natl Acad Sci USA 1995; 92:6424-6428.
11
12. Brint JM, Ohman DE. Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhlR-RhlI, another set of regulators in strain PAO1 with homology to the autoinducer-responsive luxR-luxI family. J Bacteriol 1995; 177:7155-7163.
12
13. Davies DG, Parsek MR, Pearson, JP, Iglewski, BH, Costerton, JW, Greenberg, EP. The involvement of cell-to-cell signals in the development of a bacterial biofilm. Science 1998; 280:295–298.
13
14. Kociolek MG. Quorum-sensing inhibitors and biofilms. Antiinfect Agents J Med Chem(Formerly Current Medicinal Chemistry-Anti-Infective Agents) 2009; 8:315-326.
14
15. Lewis K. Persister cells, dormancy and infectious disease. Nat Rev Microbiol 2007; 5:48-56.
15
16. Andrews SC, Robinson AK, Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol Rev 2003; 27:215-237.
16
17. Singh PK, Parsek MR, Greenberg EP, Welsh MJ. A component of innate immunity prevents bacterial biofilm development. Nature 2002; 417:552-555.
17
18. Poole K, McKay GA. Iron acquisition and its control in Pseudomonas aeruginosa: Many roads lead to rome. Front Biosci 2003; 8:661-686.
18
19. Singh PK. Iron sequestration by human lactoferrin stimulates P. aeruginosa surface motility and blocks biofilm formation. Biometals 2004; 17:267-270.
19
20. Bertulutti F, Morea C, Battistoni A, Sarli S, Cipriani P, Superti F, Ammendolia MG, Valenti P. Iron availability influences aggregation, biofilm, adhesion and invasion of Pseudomonas aeruginosa and Burkholderia cenocepacia. Int J Immunopathol Pharmocol 2005; 18:661-670.
20
21. Reid DW, Withers NJ, Francis L, Wilson JW, Kotsimbos TC. Iron deficiency in Cytisc Fibrosis relationship to lung disease severity and chronic Pseudomonas aeruginosa infection. Chest 2002; 121:48-54.
21
22. Musk DJ, Banko DA, Hergenrother PJ. Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa. Chem Biol 2005; 12:789–796.
22
23. Musk DJ, Hergenrother PJ. Chelated iron sources are inhibitors of Pseudomonas aeruginosa biofilms and distribute efficiently in an in vitro model of drug delivery to the human lung. J Appl Microbiol 2008; 105:380-388.
23
24. O’Toole GA, Kolter R. Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Mol Microbiol 1998; 30:295-304.
24
25. Rashid MH, Kornberg A. Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa. Proc Natl Acad Sci USA 2000; 97:4885-4890.
25
26. Chen X, Stewart PS. Role of electrostatic interactions in cohesion of bacterial biofilms. Appl Microbiol Biotechnol 2002; 59:718–720.
26
27. Raad I, Kassar R, Ghannam D, Chaftari AM, Hachem R, Jiang Y. Management of the catheter in documented catheter-related coagulase-negative staphylococcal bacteremia: remove or retain? Clin Infect Dis 2009; 49:1187-1194.
27
28. Moreau-Marquis S, O'Toole GA, Stanton BA. Tobramycin and FDA-approved iron chelators eliminate Pseudomonas aeruginosa biofilms on cystic fibrosis cells. Am J Resp Cell Mol 2009; 41:305-313.
28
29. Kaneko Y, Thoendel M, Olakanmi O, Britigan BE, Singh PK. The transition metal gallium disrupts Pseudomonas aeruginosa iron metabolism and has antimicrobial and antibiofilm activity. J Clin Invest 2007; 117:877-888.
29
30. Banin E, Lozinski A, Brady KM, Berenshtein E, Butterfield PW, Moshe M, et al. The potential of desferrioxaminegallium as an anti-Pseudomonas therapeutic agent. Proc Natl Acad Sci USA 2008; 105:16761–16765.
30
31. Mah Thien-Fah C, O'Toole GA. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol 2001; 9:34-39.
31
ORIGINAL_ARTICLE
Improved viability of random pattern skin flaps with the use of bone marrow mesenchymal-derived stem cells and chicken embryo extract
Objective(s): Covering tissue defects using skin flaps is a basic surgical strategy for plastic and reconstructive surgery. The aim of this study was to evaluate the effects of chicken embryo extract (CEE) and bone marrow derived mesenchymal stem cells (BM-MSCs) on random skin flap survival (RSF) in rats. Using chicken embryo extract can be an ideal environment for the growth and proliferation of transplanted cells. Materials and Methods: Forty albino male Wistar rats were divided into 4 groups; each group consisted of 10 rats. BM-MSCs and CEE were transplanted into subcutaneous tissue in the area, where the flap would be examined. On the 7th postoperative day, the survival areas of the flaps were measured by using digital imaging with software assistance, and tissue was collected for evaluation. Results: Survival area was 19.54±2 in the CEE group and 17.90±2 in the CEE/BM-MSC group when compared to the rates of the total skin flaps, which were significantly higher than the control group (13.47±2) (P<0.05). The biomechanical assessment showed a slight difference, although there was no statistically significant difference between the experimental groups and the control group (P>0.05). Conclusion: The findings from this study demonstrated that in operative treatment with BM-MSCs and CEE transplantation could promote flap survival, but the biomechanical parameters were not contrasted with a saline injection.
https://ijbms.mums.ac.ir/article_4727_1e2c1271cb53b0112a1a25d69b1f66e0.pdf
2015-08-01
764
772
10.22038/ijbms.2015.4727
bone marrow
Chicken
Stem cells
Surgical flaps
Survival rate
Wistar rats
Farzaneh
Chehelcheraghi
fr.chehelcheraghi@gmail.com
1
Department of Anatomy, Medical Faculty, Baqyiatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Hossein
Eimani
2
Department of Anatomy, Medical Faculty, Baqyiatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Seyed Homayoon
Sadraie
3
Department of Anatomy, Medical Faculty, Baqyiatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Giti
Torkaman
4
Department of Physical Therapy, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran
AUTHOR
Abdollah
Amini
d.amini2005@yahoo.com
5
Department of Anatomy, Medical Faculty, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
Hashem
SHemshadi
6
Department of Speech Therapy, University of Welfare and Rehabilitation Sciences, Tehran, Iran
AUTHOR
Hamid
Alavi Majd
7
Department of Biostatistics, Faculty of Paramedicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
1. Harder Y, Amon M, Laschke MW, Schramm R, Rücker M, Wettstein R, et al. An old dream revitalised: preconditioning strategies to protect surgical flaps from critical ischaemia and ischaemia-reperfusion injury. J Plast Reconstr Aesthet Surg 2008; 61:503-511.
1
2. Siemionow M, Arslan E. Ischemia/reperfusion injury: a review in relation to free tissue transfers". Microsurgery 2004; 24:468-475.
2
3. Tapuria N, Kumar Y, Habib MM, Amara MA, Seifalian AM, Davidson BR, et al. Remote ischemic preconditioning: a novel protective method from ischemia reperfusion injury—a review. J Surg Res 2008; 150:304-330.
3
4. Bauer SM, Goldstein LJ, Bauer RJ, Chen H, Putt M, Velazquez OC. The bone marrow-derived endothelial progenitor cell response is impaired in delayed wound healing from ischemia. J Vasc Surg 2006; 43:134-141.
4
5. Wang W Z. Investigation of reperfusion injury and ischemic preconditioning in microsurgery. Microsurgery 2009; 29:72-79.
5
6. Caiado F, Carvalho T, Silva F, Castro C, Clode N, Dye J, et al. The role of fibrin E on the modulation of endothelial progenitors adhesion, differentiation and angiogenic growth factor production and the promotion of wound healing. Biomaterials 2011; 32:7096-7105.
6
7 .Küntscher MV, Hartmann B, Germann G. Remote ischemic preconditioning of flaps: a review. Microsurgery 2005; 25:346-352.
7
8. Bayat M, Chelcheraghi F, Piryaei A, Rakhshan M, Mohseniefar Z, Rezaie F, et al. The effect of 30-day pretreatment with pentoxifylline on the survival of arandom skin flap in the rat: An ultrastructural and biomechanical evaluation. Med Sci Monit 2006; 12:BR201-207.
8
9 .van den Heuvel MG, Buurman WA, Bast A, van der Hulst RR.. Review: ischaemia–reperfusion injury in flap surgery. J Plast Reconstr Aesthet Surg 2009; 62:721-726.
9
10. Singer AJ,Clark RA. Cutaneous wound healing. N Engl J Med 1999; 341:738-746.
10
11. Tonnesen MG, Feng X, Clark RA. Angiogenesis in wound healing. J Investig Dermatol Symp Proc 2000 ; 5:40-46.
11
12. Murohara T. Therapeutic vasculogenesis using human cord blood-derived endothelial progenitors. Trends Cardiovasc Med 2001; 11:303-307.
12
13. Kim JY, Sun HS, Koung LK, Ko JJ, Im JE, Yie SW, et al. Human cord blood-derived endothelial progenitor cells and their conditioned media exhibit therapeutic equivalence for diabetic wound healing. Cell Transplant 2010; 19:1635-1644.
13
14. Barcelos LS, Duplaa C, Kränkel N, Graiani G, Invernici G, Katare R, et al. Human CD133 progenitor cells promote the healing of diabetic ischemic ulcers by paracrine stimulation of angiogenesis and activation of Wnt signaling. Circ Res 2009; 104:1095-1102.
14
15. Kamihata H, Matsubara H, Nishiue T, Fujiyama S, Tsutsumi Y, Ozono R, et al. Implantation of bone marrow mononuclear cells into ischemic myocardium enhances collateral perfusion and regional function via side supply of angioblasts, angiogenic ligands, and cytokines. Circulation 2001; 104:1046-1052.
15
16. Hiasa KI, Egashira K, Kitamoto S, Ishibashi M, Inoue S, Ni W, et al. Bone marrow mononuclear cell therapy limits myocardial infarct size through vascular endothelial growth factor. Basic Res Cardiol 2004; 99:165-172.
16
17. Tse HF, Siu CW, Zhu SG, Songyan L, Zhang Q Y, Lai WH, et al. Paracrine effects of direct intramyocardial implantation of bone marrow derived cells to enhance neovascularization in chronic ischaemic myocardium. Eur J Heart Fail 2007; 9:747-753.
17
18. Fu X, Li H. Mesenchymal stem cells and skin wound repair and regeneration: possibilities and questions. Cell Tissue Res 2009; 335:317-321.
18
19. Hamou C, Callaghan MJ, Thangarajah H, Chang E, Chang EI, Grogan RH, et al. Mesenchymal stem cells can participate in ischemic neovascularization. Plast Reconstr Surg 2009; 123:45S-55S.
19
20. Abdollahi H, Harris LJ, Zhang P, McIlhenny S, Srinivas V, Tulenko T, et al. The role of hypoxia in stem cell differentiation and therapeutics. J Surg Res 2011; 165:112-117.
20
21. Chen L, Tredget EE, Wu PY, Wu Y, Wu Y. Paracrine factors of mesenchymal stem cells recruit macrophages and endothelial lineage cells and enhance wound healing. PLoS One 2008; 3:e1886.
21
22. Wang JC, Xia L, Song XB, Wang CE, Wei FC. "Transplantation of hypoxia preconditioned bone marrow mesenchymal stem cells improves survival of ultra-long random skin flap. Chin Med J 2011; 124:2507-2511.
22
23. Zacchigna S, Papa G, Antonini A, Novati F, Moimas S, Carrer A, et al. Improved survival of ischemic cutaneous and musculocutaneous flaps after vascular endothelial growth factor gene transfer using adeno-associated virus vectors. Am J Pathol 2005; 167:981-991.
23
24. Zhang F, Waller W, Lineaweaver WC. Growth factors and flap survival. Microsurgery 2004; 24:162-167.
24
25. Zavan B, Vindigni V, Vezzù K, Zorzato G, Luni C, Abatangelo G, et al. Hyaluronan based porous nano-particles enriched with growth factors for the treatment of ulcers: a placebo-controlled study. J Mater Sci Mater Med 2009; 20:235-247.
25
26. Ichioka S, Kudo S, Shibata M, Ando J, Sekiya N, Nakatsuka T, Bone marrow cell implantation improves flap viability after ischemia-reperfusion injury. Ann Plast Surg 2004; 52:414-418.
26
27. Lu F, Mizuno H, Uysal CA, Cai X, Ogawa R, Hyakusoku H. Improved viability of random pattern skin flaps through the use of adipose-derived stem cells. Plast Reconstr Surg 2008; 121:50-58.
27
28. Uysal AC, Mizuno H, Tobita M, Ogawa R, Hyakusoku H. The effect of adipose-derived stem cells on ischemia-reperfusion injury: immunohistochemical and ultrastructural evaluation. Plast Reconstr Surg 2009; 124:804-815.
28
29. Christman SA, Kong BW, Landry MM, Foster DN. Chicken embryo extract mitigates growth and morphological changes in a spontaneously immortalized chicken embryo fibroblast cell line. Poult Sci 2005; 84:1423-1431.
29
30. Oberley TD, Muth JV, Murphy-Ullrich JE. Growth and maintenance of glomerular cells under defined conditions. Am J Pathol 1980; 101:195-204.
30
31. Suh W, Kim KL, Kim JM, Shin IS, Lee YS, et al. Transplantation of endothelial progenitor cells accelerates dermal wound healing with increased recruitment of monocytes/macrophages and neovascularization. Stem Cells 2005; 23:1571-1578.
31
32. Maharlooei MK, Bagheri M, Solhjou Z, Jahromi BM, Akrami M, Rohani L, et al. Adipose tissue derived mesenchymal stem cell (AD-MSC) promotes skin wound healing in diabetic rats. Diabetes Res Clin Pract 2011; 93:228-234.
32
33. Barcelos LS, Duplaa C, Kränkel N, Graiani G, Invernici G, Katare R, et al. Human CD133+ progenitor cells promote the healing of diabetic ischemic ulcers by paracrine stimulation of angiogenesis and activation of Wnt signaling. Circ Res 2009; 104:1095-1102.
33
34. Azizi SA, Stokes D, Augelli BJ, DiGirolamo C, Prockop DJ. Engraftment and migration of human bone marrow stromal cells implanted in the brains of albino rats—similarities to astrocyte grafts. Proc Natl Acad Sci USA 1998; 95:3908-3913.
34
35. Yang M, Sheng L, Li H, Weng R, Li QF. Improvement of the skin flap survival with the bone marrow‐derived mononuclear cells transplantation in a rat model. Microsurgery 2010; 30:275-281.
35
36. Strober W. Trypan blue exclusion test of cell viability. Curr Protoc Immunol 2001; A-3B.
36
37. Ohara H, Kishi K, Nakajima T. Rat dorsal paired island skin flaps: a precise model for flap survival evaluation. Keio J Med 2008; 57:211-216.
37
38. Rah DK, Yun IS, Yun CO, Lee SB, Lee WJ. Gene therapy using hepatocyte growth factor expressing adenovirus improves skin flap survival in a rat model. J Korean Med Sci 2014; 29:S228-236.
38
39. Quirinia A, Viidik A. The effect of hyperbaric oxygen on different phases of healing of ischaemic flap wounds and incisional wounds in skin. Br J Plast Surg 1995; 48:583-589.
39
40. Quirinia A, Jensen FT, Viidik A. Ischemia in wound healing I: Design of a flap model-changes in blood flow. Scand J Plast Reconstr Surg Hand Surg 1992; 26:21-28.
40
41. Quirina A. Ischemia in wound Healing II: Design of a flap model—biomechanical properties. Scand J Plast Reconstr Surg Hand Surg 1992; 26:133-139.
41
42. Morimoto A, Tomita S, Imanishi M, Shioi G, Kihira Y, Izawa-Ishizawa Y, et al. Overexpressed HIF-2α in endothelial cells promotes vascularization and improves random pattern skin flap survival. Plast Reconstr Surg Glob Open 2014; 2:e132.
42
43. Wang C, Cai Y, Zhang Y, Xiong Z, Li G, Cui L. Local injection of deferoxamine improves neovascularization in ischemic diabetic random flap by increasing HIF-1α and VEGF expression. PLoS One 2014; 9:e100818.
43
44. Reichenberger MA, Mueller W, Schäfer A, Heimer, S., Leimer, U, Lass, U, et al. Fibrin-embedded adipose derived stem cells enhance skin flap survival. Stem Cell Rev 2012; 8:844-853
44
45. Richard S, Craft C, McKinney B. Improved survival of ischemic random skin flaps through the use of bone marrow nonhematopoietic stem cells and angiogenic growth factors. Ann Plast Surg 2005; 54:546-552.
45
46. Khouri RK, Brown DM, Leal-Khouri SM, Tark KC, Shaw WW. The effect of basic fibroblast growth factor on the neovascularisation process: skin flap survival and staged flap transfers. Br J Plast Surg 1991; 44:585-588.
46
47. Mogford JE, Tawil B, Jia S, Mustoe TA. Fibrin sealant combined with fibroblasts and platelet‐derived growth factor enhance wound healing in excisional wounds. Wound Repair Regen 2009; 17:405-410.
47
48. Hu G, Xu JJ, Deng ZH, Feng J, Jin Y. Supernatant of bone marrow mesenchymal stromal cells induces peripheral blood mononuclear cells possessing mesenchymal features. Int J Biol Sci 2011; 7:364-375.
48
49. Niknejad H, Peirovi H, Ahmadiani A, Ghanavi J, Jorjani M. Differentiation factors that influence neuronal markers expression in vitro from human amniotic epithelial cells. Eur Cell Mater 2010; 19:22-29.
49
50. Mödder UI, Khosla S. Skeletal stem/osteoprogenitor cells: current concepts, alternate hypotheses, and relationship to the bone remodeling compartment. J Cell Biochem 2008; 103:393-400.
50
51. Hirschi KK,Goodell MA. Hematopoietic, vascular and cardiac fates of bone marrow-derived stem cells. Gene Ther 2002; 9:648-652.
51
52. Sheng L, Yang M, Li H, Du Z, Yang Y, Li Q. Transplantation of adipose stromal cells promotes neovascularization of random skin flaps. Tohoku J Exp Med 2011; 224:229-234.
52
53. Fam NP, Verma S, Kutryk M, Stewart DJ. Clinician guide to angiogenesis. Circulation 2003 25; 108:2613-2618.
53
54. Michlits W, Mittermayr R, Schäfer R, Redl H, Aharinejad S. Fibrin‐embedded administration of VEGF plasmid enhances skin flap survival. Wound Repair Regen 2007; 15:360-367.
54
55. Zacchigna S, Papa G, Antonini A, Novati F, Moimas S, Carrer A, et al. Improved survival of ischemic cutaneous and musculocutaneous flaps after vascular endothelial growth factor gene transfer using adeno-associated virus vectors. Am J Pathol 2005; 167:981-991.
55
56. Seify H, Bilkay U, Jones G. Improvement of TRAM flap viability using human VEGF-induced angiogenesis: a comparative study of delay techniques. Plast Reconstr Surg 2003; 112:1032-1039.
56
ORIGINAL_ARTICLE
N-myc downstream regulated gene 2 overexpression reduces matrix metalloproteinase-2 and -9 activities and cell invasion of A549 lung cancer cell line in vitro
Objective(s):N-myc downstream regulated gene 2 (NDRG2) is a candidate gene for tumor suppression. The expression of NDRG2 is down-regulated in several tumors including lung cancer. The aim of this study was to explore the effect of NDRG2 overexpression on invasion, migration, and enzymatic activity of matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) in human lung adenocarcinoma A549 cells. Materials and Methods: A recombinant plasmid encoding green fluorescent protein (GFP)-tagged NDRG2 (pCMV6-AC-NDRG2-GFP) was used to overexpress GFP-tagged NDRG2 in A549 cells. The cells in the experimental group and those in the control group were transfected with pCMV6-AC-NDRG2-GFP and a control plasmid without NDRG2 (pCMV6-AC-GFP), respectively. Fluorescent microscopy and flowcytometry analysis of GFP expression were used to evaluate the cellular expression of GFP-tagged NDRG2 and the efficiency of transfection. The effects of NDRG2 expression on cell invasion and migration were evaluated using transwell filter migration assay. The gelatinase activity of secreted MMP-2 and MMP-9 was measured by gelatin zymography. Results:Our results demonstrated the expression of GFP-tagged NDRG2 in the cytoplasm and nucleus of A549 cells. The findings of transwell assay showed that NDRG2 overexpression reduced migration and invasion of A549 cells compared to control cells. Gelatin zymography analyses revealed that NDRG2 overexpression decreased the gelatinase activity of secreted MMP-2 and MMP-9. Conclusion: These findings suggest that NDRG2 may be a new anti-invasion factor in lung cancer that inhibits MMPs activities.
https://ijbms.mums.ac.ir/article_4728_dd68cf6bcfd5bffc09817acb7d6fb0a6.pdf
2015-08-01
773
779
10.22038/ijbms.2015.4728
Invasion
Lung cancer
Matrix metalloproteinase
Migration
N-myc downstream-regulated gene 2
Seyed Nooredin
Faraji
snf.biotech@yahoo.com
1
Diagnostic Laboratory Sciences and Technology Research Center, School of Paramedical Sciences, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Zahra
Mojtahedi
mojtahediz@sums.ac.ir
2
Shiraz Institute for Cancer Research, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Ghasem
Ghalamfarsa
ghalamfarsa@yahoo.com
3
Department of Immunology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Mohammad Ali
Takhshid
takhshid2001@yahoo.co.uk
4
Diagnostic Laboratory Sciences and Technology Research Center, School of Paramedical Sciences, Shiraz University of Medical Sciences, Shiraz, Iran
LEAD_AUTHOR
1. Yang J, Li Y, Wu L, Zhang Z, Han T, Guo H, et al. NDRG2 in rat liver regeneration: role in proliferation and apoptosis. Wound Repair Regen 2010; 18:524-531.
1
2. Chen X, Su Y, Fingleton B, Acuff H, Matrisian LM, Zent R, et al. Increased plasma MMP9 in integrin alpha1-null mice enhances lung metastasis of colon carcinoma cells. Int J Cancer 2005 10; 116:52-61.
2
3.Papi A, Ferreri AM, Guerra F, Orlandi M. Anti-invasive effects and proapoptotic activity induction by the rexinoid IIF and valproic acid in combination on colon cancer cell lines. Anticancer Res 2012; 32:2855-2862.
3
4. Umesalma S, Nagendraprabhu P, Sudhandiran G. Antiproliferative and apoptotic-inducing potential of ellagic acid against 1,2-dimethyl hydrazine-induced colon tumorigenesis in Wistar rats. Mol Cell Biochem 2014; 388:157-172.
4
5. Hwang J, Kim Y, Kang HB, Jaroszewski L, Deacon AM, Lee H, et al. Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor. J Biol Chem 2011 8; 286:12450-12460.
5
6.Hu XL, Liu XP, Deng YC, Lin SX, Wu L, Zhang J, et al. Expression analysis of the NDRG2 gene in mouse embryonic and adult tissues. Cell Tissue Res 2006; 325:67-76.
6
7. Okuda T, Kokame K, Miyata T. Differential expression patterns of NDRG family proteins in the central nervous system. J Histochem Cytochem 2008; 56:175-182.
7
8. Enayat S, Banerjee S. The ethanolic extract of bark from Salix aegyptiaca L. inhibits the metastatic potential and epithelial to mesenchymal transition of colon cancer cell lines. Nutr Cancer 2014; 66:999-1008.
8
9. Kim YJ, Yoon SY, Kim JT, Song EY, Lee HG, Son HJ, et al. NDRG2 expression decreases with tumor stages and regulates TCF/beta-catenin signaling in human colon carcinoma. Carcinogenesis 2009; 30:598-605.
9
10. Lorentzen A, Lewinsky RH, Bornholdt J, Vogel LK, Mitchelmore C. Expression profile of the N-myc Downstream Regulated Gene 2 (NDRG2) in human cancers with focus on breast cancer. BMC Cancer 2011; 11:14.
10
11. Feng L, Xie Y, Zhang H, Wu Y. Down-regulation of NDRG2 gene expression in human colorectal cancer involves promoter methylation and microRNA-650. Biochem Biophys Res Commun 2011 25; 406:534-538.
11
12. Ma J, Jin H, Wang H, Yuan J, Bao T, Jiang X, et al. Expression of NDRG2 in clear cell renal cell carcinoma. Biol Pharm Bull 2008;31:1316-1320.
12
13. Zhou B, Tang Z, Deng Y, Hou S, Liu N, Lin W, et al. Tumor suppressor candidate gene, NDRG2 is frequently inactivated in human glioblastoma multiforme. Mol Medicine Rep 2014; 10:891-896.
13
14. Lee DC, Kang YK, Kim WH, Jang YJ, Kim DJ, Park IY, et al. Functional and clinical evidence for NDRG2 as a candidate suppressor of liver cancer metastasis. Cancer Res 2008; 68:4210-4220.
14
15. Li SJ, Wang WY, Li B, Chen B, Zhang B, Wang X, et al. Expression of NDRG2 in human lung cancer and its correlation with prognosis. Med Oncol 2013; 30:421.
15
16. Gao L, Wu GJ, Liu XW, Zhang R, Yu L, Zhang G, et al. Suppression of invasion and metastasis of prostate cancer cells by overexpression of NDRG2 gene. Cancer Lett 2011 1; 310:94-100.
16
17. Kim YJ, Yoon SY, Kim JT, Choi SC, Lim JS, Kim JH, et al. NDRG2 suppresses cell proliferation through down-regulation of AP-1 activity in human colon carcinoma cells. Int J Cancer 2009 1; 124:7-15.
17
18. Li R, Yu C, Jiang F, Gao L, Li J, Wang Y, et al. Overexpression of N-Myc downstream-regulated gene 2 (NDRG2) regulates the proliferation and invasion of bladder cancer cells in vitro and in vivo. PloS one 2013 16; 8:e76689.
18
19. Zheng J, Li Y, Yang J, Liu Q, Shi M, Zhang R, et al. NDRG2 inhibits hepatocellular carcinoma adhesion, migration and invasion by regulating CD24 expression. BMC cancer 2011; 251:1-9.
19
20. Shon SK, Kim A, Kim JY, Kim KI, Yang Y, Lim JS. Bone morphogenetic protein-4 induced by NDRG2 expression inhibits MMP-9 activity in breast cancer cells. Biochem Biophys Res Commun 2009; 385:198-203.
20
21. Xu C, Gui Q, Chen W, Wu L, Sun W, Zhang N, et al. Small interference RNA targeting tissue factor inhibits human lung adenocarcinoma growth in vitro and in vivo. J Exp Clin Cancer Res 2011; 30:63.
21
22. Cheung LW, Leung PC, Wong AS. Gonadotropin-releasing hormone promotes ovarian cancer cell invasiveness through c-Jun NH2-terminal kinase-mediated activation of matrix metalloproteinase (MMP)-2 and MMP-9. Cancer Res 2006; 66:10902-10910.
22
23. Dong W, Li H, Zhang Y, Yang H, Guo M, Li L, et al. Matrix metalloproteinase 2 promotes cell growth and invasion in colorectal cancer. Acta Biochim Biophys Sin (Shanghai) 2011; 43:840-848.
23
24. Ikari A, Sato T, Takiguchi A, Atomi K, Yamazaki Y, Sugatani J, et al. Claudin-2 knockdown decreases matrix metalloproteinase-9 activity and cell migration via suppression of nuclear Sp1 in A549 cells Life Sci 2011; 286:628-633.
24
25. Zheng J, Liu Q, Li Y, Yang J, Ma J, Yu F, et al. NDRG2 expression regulates CD24 and metastatic potential of breast cancer cells. Asian Pac J Cancer Prev 2010; 11:1817-1821.
25
26. Cao W, Zhang JL, Feng DY, Liu XW, Li Y, Wang LF, et al. The effect of adenovirus-conjugated NDRG2 on p53-mediated apoptosis of hepatocarcinoma cells through attenuation of nucleotide excision repair capacity. Biomaterials 2014; 35:993-1003
26
ORIGINAL_ARTICLE
Construction of expressing vectors including melanoma differentiation-associated gene-7 (mda-7) fused with the RGD sequences for better tumor targeting
Objective(s): Up to now, many researches have been performed to improve the antitumoral effect of melanoma differentiation-associated gene-7 (mda-7) protein. The purpose of our research was to construct 3 expression vectors producing mda-7 in fusion with RGD (Arginine-Glycine-Aspartic acid) peptide and evaluate their expression.
Materials and Methods: mda-7 gene with two different RGD sequences was amplified by PCR then was cloned by TA–cloning system. The colonies including these genes were selected by blue–white screening, colony PCR, and sequencing, respectively. Afterward, the genes were sub-cloned into the expression vector following confirmation by colony PCR and sequencing. In addition, these constructs were transfected into 293 and Huh-7 cells for further expression analysis. The mda-7 gene expression was evaluated by RT-PCR and IF (immunofluorescence assay). DNA laddering test and trypan blue exclusion assays were performed to screen cytotoxicity of prepared plasmids.
Results: Three different mda-7 genes with terminal RGD peptide were cloned correctly into the expression vectors and their expression was confirmed to be suitable by RT-PCR and IF assay. It was shown that expressions were limited to those transfected, GFP shining cells. No significant cytotoxicity was observed by simple assays in all plasmid treated cells. In expressing cells, all forms of mda-7 protein were localized mainly around ER prenuclear compartment while GFP protein was distributed evenly among them.
Conclusion: Theoretically RGD tagged mda-7 would be able to induce apoptosis with more specificity and stronger than the standard one, therefore, these new constructs may have the potential for further researches.
https://ijbms.mums.ac.ir/article_4729_a18967cb67f59481f0c7af90d9d12829.pdf
2015-08-01
780
787
10.22038/ijbms.2015.4729
Mda-7
RGD peptide
Tumor targeting
Mahboobeh
Khodadad
khodadad.mahboobeh@yahoo.com
1
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Seyed Younes
Hosseini
hoseiniy@sums.ac.ir
2
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
LEAD_AUTHOR
Fatemeh
Shenavar
3
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Nasrollah
Erfani
erfanin@sums.ac.ir
4
Cancer Immunology Research Group, Shiraz Institute for Cancer Research, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Samaneh
Bina
5
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Shahin
Ahmadian
ahmadian@ut.ac.ir
6
Sciences Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
AUTHOR
Mohammad-Reza
Fattahi
7
Gastroenterohepatology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Reza
Hajhosseini
8
Department Of Biochemistry, Payame Noor University, Tehran Shargh Branch, Tehran, Iran
AUTHOR
1. Fisher P.B. Is mda-7/IL-24 a magic bullet for cancer? Cancer Res. 2005. 65:10128–10138.
1
2. Xue XB, Xiao Ch Wen, Zhang H, Lu AG, Gao W, Zhou ZhQ, Guo XL. Oncolytic adenovirus SG600-IL24 selectively kills hepatocellular carcinoma cell lines. World J Gastroenterol 2010; 16:4677-4684.
2
3. Jiang H, Su ZZ, Lin JJ, Goldstein NI, Young CS, Fisher PB. The melanoma differentiation associated gene mda-7 suppresses cancer cell growth. Proc Nat Acad Sci 1996; 93:9160-9165.
3
4. Sarkar D, Su Z-Z, Lebedeva IV, Sauane M, Gopalkrishnan RV, Valerie K, et al. mda-7 (IL-24) mediates selective apoptosis in human melanoma cells by inducing the coordinated overexpression of the GADD family of genes by means of p38 MAPK. Proc Nat Acad Sci 2002; 99:10054-10059.
4
5. Mhashilkar AM, Schrock RD, Hindi M, Liao J, Sieger K, Kourouma F, et al. Melanoma differentiation associated gene-7 (mda-7): a novel anti-tumor gene for cancer gene therapy. Mol Med 2001; 7:12.
5
6. Lebedeva IV, Su ZZ, Chang Y, Kitada S, Reed JC, Fisher PB. The cancer growth suppressing gene mda-7 induces apoptosis selectively in human melanoma cells. Oncogene 2002; 21:708-718.
6
7. Saeki T, Mhashilkar A, Chada S, Branch C, Roth JA, Ramesh R. Tumor-suppressive effects by adenovirus-mediated mda-7 gene transfer in non-small cell lung cancer cell in vitro. Gene Ther 2000; 7.
7
8. Cao XX I, Mohuiddin S, Chada AM, Mhashilkar MK, Ozvaran DJ, McConkey SD, et al. Adenoviral transfer of mda-7 leads to BAX up-regulation and apoptosis in mesothelioma cells, and is abrogated by over-expression of BCL-XL. Mol Med 2002; 8:869-876.
8
9. Saeki T, Mhashilkar A, Swanson X, Zou-Yang XH, Sieger K, Kawabe S, et al. Inhibition of human lung cancer growth following adenovirus-mediated mda-7 gene expression in vivo. Oncogene 2002; 21:4558-4566.
9
10. Weber WA, Haubner R, Vabuliene E, Kuhnast B, Wester HJ,Schwaiger M. Tumor angiogenesis targeting using imaging agents. Q J Nucl Med 2001; 45:179-182.
10
11. Wang M, Tan Z, Zhang R, Kotenko SV, Liang P. Interleukin 24 (MDA-7/MOB-5) Signals through Two Heterodimeric Receptors, IL-22R1/IL-20R2 and IL-20R1/IL-20R2. J Biol Chem 2002; 277:7341-7347.
11
12. Sauane M, Su Z-z, Gupta P, Lebedeva IV, Dent P, Sarkar D, et al. Autocrine regulation of mda-7/IL-24 mediates cancer-specific apoptosis. Proc Nat Acad Sci 2008; 105:9763-9768.
12
13. Cunningham CC, Chada S, Merritt JA, Tong A, Senzer N, Zhang Y, et al. Clinical and local biological effects of an intratumoral injection of mda-7 (IL24; INGN 241) in patients with advanced carcinoma: a phase I study. Mol Ther 2005; 11:149-159.
13
14. Liu JJ, Zhang BF, Yin XX, Pei DS, Yang ZX, Di JH, et al. Expression, purification, and characterization of RGD-mda-7, a His-tagged mda-7/IL 24 mutant protein. J Immunoassay Immunochem 2012; 33:352-368.
14
15. Jin H, Varner J. Integrins: roles in cancer development and as treatment targets. Br J Cancer 2004; 90:561-565.
15
16. Zitzmann S, Ehemann V, Schwab M. Arginine-glycine-aspartic acid (RGD)-peptide binds to both tumor and tumor-endothelial cells in vivo. Cancer Res 2002; 62:5139-5143.
16
17. Kumar cc. Integrin alpha v beta 3 as a therapeutic target for blocking tumor-induced angiogenesis. Curr Drug Targets 2003; 4:9.?
17
18. Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin [alpha]5[beta]1 in complex with fibronectin. EMBO J 2003; 22:4607-4615.
18
19. Xiao B, Li W, Yang J, Guo G, Mao X-H, Zou Q-M. RGD-IL-24, a novel tumor-targeted fusion cytokine: expression, purification and functional evaluation. Mol Biotechnol 2009; 41:138-144.
19
20. Pei D-S, Yang Z-X, Zhang B-F, Yin X-X, Li L-T, Li H-Z, et al. Enhanced apoptosis-inducing function of MDA-7/IL-24 RGD mutant via the increased adhesion to tumor cells. J Interferon Cytokine Res 2012; 32:66-73.
20
21. Craig R, Cutrera J, Zhu S, Xia X, Lee Y-H, Li S. Administering Plasmid DNA Encoding Tumor vessel–anchored IFN-α for Localizing Gene Product Within or Into Tumors. Mol Ther 2008; 16:901-906.
21
22. Wang X, Bai C, Zhang J, Sun A, Wang X, Wei D. Improving the mda-7/IL-24 refolding and purification process using optimized culture conditions based on the structure characteristics of inclusion bodies. Bioresources and Bioprocessing 2014, 1:21.
22
23. Kreis S, Philippidou D, Margue C, Rolvering C, Haan C, Dumoutier L, et al. Recombinant interleukin-24 lacks apoptosis-inducing properties in melanoma cells. PloS One 2007; 2:e1300.
23
24. Temming K, Schiffelers RM, Molema G, Kok RJ. RGD-based strategies for selective delivery of therapeutics and imaging agents to the tumour vasculature. Drug Resist Update 2005; 8:381-402.
24
25. Momtazi-borojeni Aa, Behbahani M, Sadeghi-aliabadi H. Antiproliferative activity and apoptosis induction of crude extract and fractions of avicennia marina. Iran J Basic Med Sci 2013; 16:1204-1208.
25
26. Sauane M, Gopalkrishnan RV, Lebedeva I, Mei MX, Sarkar D, Su ZZ, et al. Mda-7/IL-24 induces apoptosis of diverse cancer cell lines through JAK/STAT-independent pathways. J Cell Physiol 2003; 196:334-345.
26
27. Wang CJ, Xue XB, Yi JL, Chen K, Zheng JW, Wang J, et al. Melanoma differentiation-associated gene-7, MDA-7/IL-24, selectively induces growth suppression, apoptosis in human hepatocellular carcinoma cell line HepG2 by replication-incompetent adenovirus vector. World J Gastroenterol 2006; 12:1774-1779.
27
28. Chen WY, Cheng YT, Lei HY, Chang CP, Wang CW, Chang MS. IL-24 inhibits the growth of hepatoma cells in vivo. Genes Immun 2005; 6:493-499.
28
29. Hynes RO. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 1992; 69:11-25.
29
30. Jin ZH, Furukawa T, Claron M, Boturyn D, Coll JL, Fukumura T, et al. Positron emission tomography imaging of tumor angiogenesis and monitoring of antiangiogenic efficacy using the novel tetrameric peptide probe 64Cu-cyclam-RAFT-c(-RGDfK-)4. Angiogenesis 2012; 15:569-580.
30
ORIGINAL_ARTICLE
Decellularized kidney in the presence of chondroitin sulfate as a natural 3D scaffold for stem cells
Objective(s): Use of biological scaffolds and automating the cells directing process with materials such as growth factors and glycosaminoglycans (GAGs) in a certain path may have beneficial effects in tissue engineering and regenerative medicine in future. In this research, chondroitin sulfate sodium was used for impregnation of the scaffolds. It is a critical component in extracellular matrix and plays an important role in signaling pathway; however, little is known about its role within mammalian development and cell linage specification.
Materials and Methods: Due to its porous and appropriate structure and for putting cells in 3D space, the kidney of BALB/c mouse was selected and decellulalized using physical and chemical methods. After decellularization, the scaffold was impregnated in chondroitin sulfate solution (CS) for 24 hr. Then, 60×10 5 human adipose-derived mesenchymal stem cells were seeded on the scaffold to assess their behavior on day 5, 10, 15, 20, and 25.
Result: After 48 hr, DAPI staining approved completed decellularized kidney by 1% SDS (sodium dodecyl sulfate). Migration and establishment of a number of cells to the remaining area of the glomerulus was observed. In addition, cell accumulation on the scaffold surface as well as cells migration to the depth of kidney formed an epithelium-like structure. Up to the day 15, microscopic study of different days of seeding showed the gradual adhesion of large number of cells to the scaffold.
Conclusion: Glycosaminoglycan could be a right option for impregnation. It is used for smartification and strengthening of natural scaffolds and induction of some behaviors in stem cells.
https://ijbms.mums.ac.ir/article_4730_2de571fb7803a8cb9938f01935647b8e.pdf
2015-08-01
788
798
10.22038/ijbms.2015.4730
Acellular scaffold
Chondroitin sulfate
Mesenchymal stem cell
Cell communication
Cell interaction
Extracellular matrix
Alireza
Rafighdoust
arafighdoost@yahoo.com
1
Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran
AUTHOR
Nasser
Mahdavi Shahri
mahdavi@um.ac.ir.
2
Department of Biology, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran
LEAD_AUTHOR
Javad
Baharara
baharara78@gmail.com
3
Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran
AUTHOR
1. Badylak SF. Regenerative medicine and developmental biology: the role of the extracellular matrix. Anat Rec B New Anat 2005; 287:36-41.
1
2. Badylak SF, Freytes DO, Gilbert TW. Extracellular matrix as a biological scaffold material: Structure and function. Acta Biomaterialia 2009; 5:1-13.
2
3. Nakayama KH, Batchelder CA, Lee CI, Tarantal AF. Decellularized rhesus monkey kidney as a three-dimensional scaffold for renal tissue engineering. Tissue Engineering Part A 2010; 16:2207-16.
3
4. Mardani M, Hashemibeni B, Ansar MM, Zarkesh Esfahani SH, Kazemi M, Goharian V, et al. Comparison between chondrogenic markers of differentiated chondrocytes from adipose derived stem cells and articular chondrocytes in vitro. Iran J Basic Med Sci 2013; 16:763-73.
4
5. Strachan LR, Condic ML. Neural crest motility and integrin regulation are distinct in cranial and trunk populations. Developmental Biology 2003; 259:288-302.
5
6. Rozario T, DeSimone DW. The extracellular matrix in development and morphogenesis: a dynamic view. Developmental Biology 2010; 341:126-140.
6
7. Linton JM, Martin GR, Reichardt LF. The ECM protein nephronectin promotes kidney development via integrin alpha8beta1-mediated stimulation of Gdnf expression. Development 2007; 134:2501-2509.
7
8. Neu R, Adams S, Munz B. Differential expression of entactin-1/nidogen-1 and entactin-2/nidogen-2 in myogenic differentiation. Differentiation 2006; 74:573-582.
8
9. Guilak F, Cohen DM, Estes BT, Gimble JM, Liedtke W, Chen CS. Control of stem cell fate by physical interactions with the extracellular matrix. Cell Stem Cell 2009 Jul 2; 5:17-26.
9
10. Zuk PA, Zhu M, Ashjian P, De Ugarte DA, Huang JI, Mizuno H, et al. Human adipose tissue is a source of multipotent stem cells. Molecular Biology Of The Cell 2002; 13:4279-4295.
10
11. Casteilla L, Planat-Benard V, Laharrague P, Cousin B. Adipose-derived stromal cells: Their identity and uses in clinical trials, an update. World J Stem Cells 2011; 3:25-33.
11
12. Lindroos B, Suuronen R, Miettinen S. The potential of adipose stem cells in regenerative medicine. Stem Cell Rev 2011; 7:269-291.
12
13. Mohammadzadeh E, Nikravesh MR, Jalali M, Fazel A, Ebrahimi V, Ebrahimzadeh-Bideskan AR. Immunohistochemical study of type III collagen expression during pre and post-natal rat skin morphogenesis. Iran J Basic Med Sci 2014; 17:196-200.
13
14. Hodde JP, Badylak SF, Brightman AO, Voytik-Harbin SL. Glycosaminoglycan content of small intestinal submucosa: a bioscaffold for tissue replacement. Tissue Eng 1996; 2:209-217.
14
15. Prinz RD, Willis CM, van Kuppevelt TH, Kluppel M. Biphasic role of chondroitin sulfate in cardiac differentiation of embryonic stem cells through inhibition of Wnt/beta-catenin signaling. PLoS One 2014; 9:e92381.
15
16. Crapo PM, Gilbert TW, Badylak SF. An overview of tissue and whole organ decellularization processes. Biomaterials 2011; 32:3233-3243.
16
17. Naderi S, Khayat Zadeh J, Mahdavi Shahri N, Nejad Shahrokh Abady K, Cheravi M, Baharara J, et al. Three-dimensional scaffold from decellularized human gingiva for cell cultures: glycoconjugates and cell behavior. Cell J 2013; 15: 166-175.
17
18. Gilbert TW, Sellaro TL, Badylak SF. Decellularization of tissues and organs. Biomaterials 2006; 27:3675-3683.
18
19. Mahdavi Shahri N, Baharara J, Takbiri M, Khajeh Ahmadi S. In vitro decellularization of rabbit lung tissue. Cell J 2013; 15:83-88.
19
20. Haddad-Mashadrizeh A, Bahrami AR, Matin MM, Edalatmanesh MA, Zomorodipour A, Gardaneh M, et al. Human adipose-derived mesenchymal stem cells can survive and integrate into the adult rat eye following xenotransplantation. Xenotransplantation 2013; 20:165-176.
20
21. Badylak SF. The extracellular matrix as a scaffold for tissue reconstruction. Semin Cell Dev Biol 2002; 13:377-383.
21
22. Ross EA, Williams MJ, Hamazaki T, Terada N, Clapp WL, Adin C, et al. Embryonic stem cells proliferate and differentiate when seeded into kidney scaffolds. J Am Soc of Nephrol 2009 ; 20:2338-2347.
22
23. Nakayama KH, Batchelder CA, Lee CI, Tarantal AF. Renal tissue engineering with decellularized rhesus monkey kidneys: age-related differences. Tissue Engin Part A 2011; 17:2891-2901.
23
24. Cebotari S, Tudorache I, Jaekel T, Hilfiker A, Dorfman S, Ternes W, et al. Detergent decellularization of heart valves for tissue engineering: toxicological effects of residual detergents on human endothelial cells. Artif Organs 2010; 34:206-210.
24
25. Sullivan DC, Mirmalek-Sani SH, Deegan DB, Baptista PM, Aboushwareb T, Atala A, et al. Decellularization methods of porcine kidneys for whole organ engineering using a high-throughput system. Biomaterials 2012;33:7756-7764.
25
26. Liu CX, Liu SR, Xu AB, Kang YZ, Zheng SB, Li HL, et al. Preparation of whole-kidney acellular matrix in rats by perfusion. Nan Fang Yi Ke Da Xue Xue Bao 2009; 29:979-982.
26
27. Walker PD. Alterations in renal tubular extracellular matrix components after ischemia-reperfusion injury to the kidney. Lab Investig 1994; 70:339-345.
27
28. Li HY, Liao CY, Lee KH, Chang HC, Chen YJ, Chao KC, et al. Collagen IV significantly enhances migration and transplantation of embryonic stem cells: involvement of alpha2beta1 integrin-mediated actin remodeling. Cell Transplant 2011; 20:893-907.
28
29. Vorotnikova E, McIntosh D, Dewilde A, Zhang J, Reing JE, Zhang L, et al. Extracellular matrix-derived products modulate endothelial and progenitor cell migration and proliferation in vitro and stimulate regenerative healing in vivo. Matrix Biol 2010; 29:690-700.
29
30. Kleinman HK, Klebe RJ, Martin GR. Role of collagenous matrices in the adhesion and growth of cells. J Cell Biol 1981; 88:473-485.
30
31. Michelini M, Franceschini V, Sihui Chen S, Papini S, Rosellini A, Ciani F, et al. Primate embryonic stem cells create their own niche while differentiating in three-dimensional culture systems. Cell Prolifer 2006; 39:217-229.
31
32. Gerecht-Nir S, Ziskind A, Cohen S, Itskovitz-Eldor J. Human embryonic stem cells as an in vitro model for human vascular development and the induction of vascular differentiation. Lab investig 2003; 83:1811-1820.
32
33. Baharvand H, Hashemi SM, Kazemi Ashtiani S, Farrokhi A. Differentiation of human embryonic stem cells into hepatocytes in 2D and 3D culture systems in vitro. Int J Dev Biol 2006; 50:645-652.
33
34. Wight TN, Kinsella MG, Qwarnstrom EE. The role of proteoglycans in cell adhesion, migration and proliferation. Curr Opin Cell Biol 1992; 4:793-801.
34
35. Brendan AC, Lorna J. In vivo and in vitro applications of collagen-GAG scaffolds. Chem Engin J 2008; 137:102-121.
35
36. Huang KF, Hsu WC, Chiu WT, Wang JY. Functional improvement and neurogenesis after collagen-GAG matrix implantation into surgical brain trauma. Biomaterials 2012; 33:2067-2075.
36
37. Tierney CM, Jaasma MJ, O'Brien FJ. Osteoblast activity on collagen-GAG scaffolds is affected by collagen and GAG concentrations. J Biomed Mater Res A 2009; 91:92-101.
37
38. Vickers SM, Squitieri LS, Spector M. Effects of cross-linking type II collagen-GAG scaffolds on chondrogenesis in vitro: dynamic pore reduction promotes cartilage formation. Tissue Engin 2006; 12:1345-1355.
38
39. Frisch SM, Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 1994; 124:619-626.
39
40. Sugiyama H, Kashihara N, Maeshima Y, Okamoto K, Kanao K, Sekikawa T, et al. Regulation of survival and death of mesangial cells by extracellular matrix. Kidney Int 1998; 54:1188-1196.
40
41. Makino H, Sugiyama H, Kashihara N. Apoptosis and extracellular matrix-cell interactions in kidney disease. Kidney Int 2000; 77:S67-75.
41
42. Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 2010; 141:52-67.
42
43. Friedl P. Prespecification and plasticity: shifting mechanisms of cell migration. Curr Opin Cell Biol 2004; 16:14-23.
43
ORIGINAL_ARTICLE
Estrogen treatment enhances neurogenic differentiation of human adipose derived stem cells in vitro
Objective(s):Estrogen is a sexual hormone that has prominent effects on reproductive and non-reproductive tissues. The aim of this study is to evaluate the effects of estrogen on the proliferation and neural differentiation of human adipose derived stem cells (ADSCs) during neurogenic differentiation.
Materials and Methods: Isolated human ADSCs were trans-differentiated in neural induction medium containing neurobasal medium, N2 and B27 with or without 17β-estradiol (E2) treatment. Proliferation rate and neural differentiation of human ADSCs were assessed using MTT assay, immunostaining and real time RT- PCR analysis, respectively.
Results: Analysis of data show that estradiol treatment can significantly increase proliferation rate of differentiated cells (P<0.05). Immunocytochemical and real time RT-PCR analysis revealed that the expression of precursor and mature neuronal markers (nestin and MAP2) was significantly higher in the E2 treated cell cultures when compared to the untreated cell cultures (P<0.05).
Conclusion: According to our findings, estrogen can promote proliferation and neuronal differentiation of human ADSCs.
https://ijbms.mums.ac.ir/article_4731_1c3319a667b51daa283ac8d8016f3001.pdf
2015-08-01
799
804
10.22038/ijbms.2015.4731
Adipose derived stem cells Cell proliferation
Neurogenic differentiation
17β-estradiol
Shahnaz
Razavi
razavi@med.mui.ac.ir
1
Department of Anatomical Sciences and Molecular Biology, Isfahan University of Medical Sciences, Isfahan, Iran
LEAD_AUTHOR
Mohamad Reza
Razavi
mrrazavi@yahoo.com
2
Molecular Parasitology Laboratory, Pasteur Institute of Iran, Tehran, Iran
AUTHOR
Nafiseh
Ahmadi
3
Department of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran
AUTHOR
Mohammad
Kazemi
m. kazemi@mut.ac.ir
4
Department of Genetic, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
1. Kang SK, Lee DH, Bae YC, Kim HK, Baik SY, Jung JS. Improvement of neurological de3 cits by intracerebral transplant of human adipose-derived stem cells after ischemia in rats. Exp Neurol 2003; 83: 355–366.
1
2. Kang SK, Shin MJ, Jung JS, Kim YG, Kim CH. Autologous adipose tissue-derived stromal cells for treatment of spinal cord injury. Stem Cells Dev 2006; 15: 583–594.
2
3. Zuk PA, Zhu M, Mizuno H, Huang J, Futrell JW, Katz AJ, Benhaim P, Lorenz HP, Hedrick MH. Multilineage cells from human adipose tissue: implications for cell-based therapies. Tissue Eng 2001; 7: 211-228.
3
4. Zuk PA, Zhu M, Ashjian P, De Ugarte DA, Huang JI, Mizuno H, Alfonso ZC, Fraser JK, Benhaim P, Hedrick MH. Human adipose tissue is a source of multipotent stem cells. Mol Biol Cell 2002; 13: 4279-4295.
4
5. Kern S, Eichler H, Stoeve J, Klüter H, Bieback K. Comparative analysis of mesenchymal stem cells from bone marrow, umbilical cord blood or adipose tissue. Stem Cells 2006; 24:1294–1301.
5
6. Brann DW, Dhandapani K, Wakade C, Mahesh VB, Khan MM. Neurotrophic and neuroprotective actions of estrogen: basic mechanisms and clinical implications. Steroids 2007; 72: 381–405.
6
7. Garcia-Segura LM, Azcoitia I, DonCarlos LL. DonCarlos, Neuroprotection by estradiol. Prog. Neurobiol. 2001; 63: 29-60.
7
8. Garcia-Segura LM, Veiga S, Sierra A, Melcangi RC, Azcoitia I. Aromatase: a neuroprotective enzyme. Prog. Neurobiol. 2003; 71: 31–41.
8
9. Suzuki S, Brown CM, Wise PM.Mechanisms of neuroprotection by estrogen. Endocrine 2006; 29: 209–215.
9
10. Suzuki S, Gerhold LM, Böttner M, Rau SW, Dela Cruz C, Yang E, Zhu H, Yu J, Cashion AB, Kindy MS, Merchenthaler I, Gage FH, Wise PM.Estradiol enhances neurogenesis following ischemic stroke through estrogen receptors alpha and beta, J. Comp. Neurol. 2007; 500: 1064–1075.
10
11. Brannvall K, Korhonen L, Lindholm D. Estrogen-receptor-dependent regulation of neural stem cell proliferation and differentiation. Mol Cell Neurosci 2002; 21:512–520.
11
12. Singh M, Meyer EM, MillardWJ, Simpkins JW. Ovariectomy reduces ChAT activity and NGF mRNA levels in the frontal cortex and hippocampus of the female Sprague–Dawley rat. Soc Neurosci Abstr 1993; 19:254.
12
13. Singh M, Meyer EM, Simpkins JW. The effect of ovariectomy and estradiol replacement on brain-derived neurotrophic factor messenger ribonucleic acid expression in cortical and hippocampal brain regions of female Sprague–Dawley rats. Endocrinology 1995; 136: 2320–2324.
13
14. Bimonte-Nelson CA, Nelson ME, Granholm AC. Progesterone counteracts estrogen-induced increases in neurotrophins in the aged female rat brain. Neuroreport 2004; 15:2659–2663.
14
15. Ivanov T, Karolczak M, Beyer C. Estradiol stimulates GDNF expression in developing hypothalamic neurons. Endocrinology 2002; 143:3175–3178.
15
16. Zhang L, Chang YH, Barker JL, Hu Q, Maric D, Li BS, Rubinow DR. Testosterone and estrogen affect neuronal differentiation but not proliferation in early embryonic cortex of the rat: the possible roles of androgen and estrogen receptors. Neurosci Lett 2000; 231:57–60.
16
17. Kang JH, Lee CK, Kim JR, Yu SJ, Jo JH, Do BR, Kim HK, Kang SG.Estrogen stimulates the neuronal differentiation of human umbilical cord blood mesenchymal stem cells (CD34-). Neuroreport. 2007; 18: 35-38.
17
18. Rehman J, Traktuev D, Li J, Merfeld-Clauss S, Temm-Grove CJ, Bovenkerk JE, Pell CL, Johnstone BH, Considine RV, March KL. Secretion of angiogenic and antiapoptotic factors by human adipose stromal cells. Circulation 2004; 109: 1292–1298.
18
19. Okada M, Murase K, Makino A, Nakajima M, Kaku T, Furukawa S, Furukawa Y. Effects of estrogens on proliferation and differentiation of neural stem/progenitor cells. Biomed Res. 2008; 29:163-70.
19
20. Razavi S, Razavi MR, Zarkesh Esfahani H, Kazemi M, Mostafavi FS Comparing brain-derived neurotrophic factor and ciliary neurotrophic factor secretion of induced neurotrophic factor secreting cells from human adipose and bone marrow-derived stem cells. Dev Growth Differ. 2013; 55: 648-55.
20
21. Wei X, Zhao L, Zhong J, Gu H, Feng D, Johnstone BH, March KL, Farlow MR, Du Y. Adipose stromal cells-secreted neuroprotective media against neuronal apoptosis. Neurosci Lett.2009; 462: 76–79.
21
22. Razavi S, Mardani M, Kazemi M, Esfandiari E, Narimani M, Esmaeili A, Ahmadi N. Effect of leukemia inhibitory factor on the myelinogenic ability of Schwann-like cells induced from human adipose-derived stem cells.Cell Mol Neurobiol. 2013; 33: 283-289.
22
23. Razavi S, Razavi MR, Kheirollahi-Kouhestani M, Mardani M, Mostafavi FS. Co-culture with neurotrophic factor secreting cells induced from adipose-derived stem cells: promotes neurogenic differentiation.Biochem Biophys Res Commun. 2013 25; 440:381-387.
23
24. Su JD, Qiu J, Zhong YP, Li XY, Wang JW, Chen YZ. Expression of estrogen receptor (ER)-alpha and -beta immunoreactivity in hippocampal cell cultures with special attention to GABAergic neurons. J Neurosci Res 2001; 65:396-402.
24
25. Pilgrim C, Hutchison JB. Developmental regulation of sex differences in the brain: Can the role of gonadal steroids be redefined? Neuroscience 1994; 60: 843–855.
25
26. McEwen BS, Alves SE, Bulloch K, Weiland NG. Ovarian steroids and the brain: Implications for cognition and aging. Neurology 1997; 48: S8–15.
26
27. Lafferty FW, Fiske ME. Postmenopausal estrogen replacement: A long-term cohort study. Am J Med 1994; 97: 66–77.
27
28. Hurn PD, Macrae IM. Estrogen as a neuroprotectant in stroke. J Cereb Blood Flow Metab. 2000; 20: 631- 652.
28
29. Evans RM. The steroid and thyroid hormone receptor superfamily. Science 1988; 240: 889-895.
29
30. Paech K, Webb P, Kuiper GG, Nilsson S, Gustafsson J, Kushner PJ, Scanlan TS. Differential ligand activation of estrogen receptors ERα and ERβ at AP1 sites.Science1997; 277: 1508–1510.
30
31. Patrone C, Pollio G, Vegeto E, Enmark E, de Curtis I, Gustafsson JA, Maggi A. Estradiol induces differential neuronal phenotypes by activating estrogen receptor alpha or beta. Endocrinology 2000; 141: 1839–1845.
31
32. Nilsson S, Mäkelä S, Treuter E, Tujague M, Thomsen J, Andersson G, Enmark E, Pettersson K, Warner M, Gustafsson JA. Mechanisms of estrogen action. Physiol Rev 2001; 81: 1535– 1565.
32
33. Patrone C, Andersson S, Korhonen L, Lindholm D. Estrogen receptor-dependent regulation of sensory neuron survival in developing dorsal root ganglion. Proc Natl Acad Sci U S A. 1999; 96: 10905–10910.
33
34. Almeida RD, Manadas BJ, Melo CV, Gomes JR, Mendes CS, Grãos MM, Carvalho RF, Carvalho AP, Duarte CB. Neuroprotection by BDNF against glutamate induced apoptotic cell death is mediated by ERK and PI3-kinase pathways. Cell Death Differ 2005; 12: 1329–1343.
34
35. Hong SH, Nah HY, Lee YJ, Lee JW, Park JH, Kim SJ, Lee JB, Yoon HS, Kim CH.Expression of estrogen receptor- alpha and –beta, glucocorticoid receptor, and progesterone receptor genes in human embryonic stem cells and embryoid bodies. Mol Cells 2004; 18: 320–325.
35
36. Wong JK, Le HH, Zsarnovszky A, Belcher SM. Estrogens and ICI182, 780 (Faslodex) modulate mitosis and cell death in immature cerebellar neurons via rapid activation of p44/p42 mitogen-activated protein kinase.J Neurosci. 2003; 23: 4984-4995.
36
37. Hamada H, Kim MK, Iwakura A, Ii M, Thorne T, Qin G, Asai J, Tsutsumi Y, Sekiguchi H, Silver M, Wecker A, Bord E, Zhu Y, Kishore R, Losordo DW. Estrogen receptors alpha and beta mediate contribution of bone marrow-derived endothelial progenitor cells to functional recovery after myocardial infarction. Circulation 2006, 114: 2261–2270.
37
ORIGINAL_ARTICLE
Chronic effects of aerobic exercise on gene expression of LOX-1 receptor in the heart of rats fed with high fat diet
Objective(s):Lectin-like low density lipoprotein receptor (LOX-1) has pivot role in vascular complications, which is upregulated in numerous pathological conditions. Since exercise has beneficial effects in prevention of hyperlipidemic complications, present study examined protective effects of aerobic exercise through reduction of LOX-1 expression in heart during dyslipidemia.
Materials and Methods: Four groups of rats were used (N=25): Normal, Normal and exercise, High fat and High fat and exercise. High fat diet (HFD) was made by adding 10% animal oil, 2% cholesterol and 0.5% colic acid to standard rodent chow. Exercise protocol consisted of swimming 1 hr/day, and 5 days/week for 8 weeks. Plasma lipids were evaluated at the end of experiment, 48 hr after final session of exercise. At the end, rats were sacrificed and heart was removed for determination of malondialdehyde (MDA) content, and LOX-1 expression.
Results:HFD meaningfully changed lipid profile (>50%), but chronic exercise had no significant effects on lipid profile. LOX-1 expression was significantly increased in heart of rats fed with HFD, while swimming exercise considerably reduced gene expression of LOX-1. MDA content was significantly enhanced in rats fed with HFD (4.37±0.6 nmol/mg, P<0.01) compared to normal group (1.56±0.48 nmol/mg), whereas swimming exercise decreased MDA level of heart in rats fed with HFD (2.28±0.32, P<0.01).
Conclusion:Findings indicated that swimming exercise is able to diminish heart expression of LOX-1 receptor concomitant reduction of oxidative stress. Since these parameters are involved in generation of dyslipidemic complications, swimming exercise is a good candidate to reduce these complications.
https://ijbms.mums.ac.ir/article_4732_18e65787957c4a41b93c471b7e7b5797.pdf
2015-08-01
805
812
10.22038/ijbms.2015.4732
Dyslipidemia
LOX-1 receptor
Oxidative stress
Swimming exercise
Simin
Riahi
riahy_simin@yahoo.com
1
Exercise Physiology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Mohammad Taghi
Mohammadi
mohammadi.mohammadt@yahoo.com
2
Department of Physiology and Biophysics, Faculty of Medicine, Baqiyatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Vahid
Sobhani
sobhani.v@yahoo.com
3
Exercise Physiology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Mansureh
Soleimany
4
Department of Anatomy, Faculty of Medicine, Iran University of Medical Sciences, Tehran, Iran
AUTHOR
1. Kelley GA, Kelley KS. Efficacy of aerobic exercise on coronary heart disease risk factors. Prev Cardiol 2008; 11:71-75.
1
2. Tuzcu EM, Kapadia SR, Tutar E, Ziada KM, Hobbs RE, McCarthy PM, et al. High prevalence of coronary atherosclerosis in asymptomatic teenagers and young adults evidence from intravascular ultrasound. Circulation 2001; 103:2705-2710.
2
3. Lahoz C, Mostaza J, Tranche S, Martin-Jadraque R, Mantilla M, López-Rodriguez I, et al. Atherogenic dyslipidemia in patients with established coronary artery disease. Nutr Metab Cardiovasc Dis 2012; 22:103-108.
3
4. Rubenfire M, Brook RD, Rosenson RS. Treating mixed hyperlipidemia and the atherogenic lipid phenotype for prevention of cardiovascular events. Am J Med 2010; 123:892-898.
4
5. Nejat A, Mirbolouk M, Mohebi R, Hasheminia M, Tohidi M, Saadat N, et al. Changes in lipid measures and incident coronary heart disease: Tehran Lipid & Glucose Study. Clin Biochem 2014; 47:1239-1244.
5
6. Rizzo M, Kotur-Stevuljevic J, Berneis K, Spinas G, Rini GB, Jelic-Ivanovic Z, et al. Atherogenic dyslipidemia and oxidative stress: a new look. Transl Res 2009; 153:217-223.
6
7. Jakus V. The role of free radicals, oxidative stress and antioxidant systems in diabetic vascular disease. Bratisl Lek Listy 2000; 101:541–551.
7
8. Yan M, Mehta JL, Zhang W, Hu C. LOX-1, oxidative stress and inflammation: a novel mechanism for diabetic cardiovascular complications. Cardiovasc Drugs Ther 2011; 25:451-459.
8
9. Adameova A, Xu Y, Duhamel T, Tappia P, Shan L, Dhalla N. Anti-atherosclerotic molecules targeting oxidative stress and inflammation. Curr Pharm Des 2009; 15:3094-3107.
9
10. Dominguez JH, Mehta JL, Li D, Wu P, Kelly KJ, Packer CS, et al. Anti-LOX-1 therapy in rats with diabetes and dyslipidemia: ablation of renal vascular and epithelial manifestations. Am J Physiol Renal Physiol 2008; 294:F110-9.
10
11. Akhmedov A, Rozenberg I, Paneni F, Camici GG, Shi Y, Doerries C, et al. Endothelial overexpression of LOX-1 increases plaque formation and promotes atherosclerosis in vivo. Eur Heart J 2014; 35:2839-2848.
11
12. Trejo-Gutierrez JF, Fletcher G. Impact of exercise on blood lipids and lipoproteins. J Clin Lipidol 2007; 1:175-181.
12
13. Joseph B. Physical activity in prevention and treatment of coronary disease: the battle line is in exercise vascular cell biology. Med Sci Sports Exerc 2004; 36:352-62.
13
14. Brochu M, Poehlman ET, Savage P, Fragnoli-Munn K, Ross S, Ades PA. Modest effects of exercise training alone on coronary risk factors and body composition in coronary patients. J Cardiopulm Rehabil 2000; 20:180-188.
14
15. Kannan U, Vasudevan K, Balasubramaniam K, Yerrabelli D, Shanmugavel K, John NA. Effect of Exercise Intensity on Lipid Profile in Sedentary Obese Adults. Journal of J Clin Diagn Res 2014; 8:8-10.
15
16. Koivula RW, Tornberg AB, Franks PW. Exercise and diabetes-related cardiovascular disease: systematic review of published evidence from observational studies and clinical trials. Curr Diab Rep 2013; 13:372-380.
16
17. Blair SN, Kampert JB, Kohl HW, Barlow CE, Macera CA, Paffenbarger RS, et al. Influences of cardiorespiratory fitness and other precursors on cardiovascular disease and all-cause mortality in men and women. JAMA 1996; 276:205-210.
17
18. Iemitsu M, Fujie S, Murakami H, Sanada K, Kawano H, Gando Y, et al. Higher cardiorespiratory fitness attenuates the risk of atherosclerosis associated with ADRB3 Trp64Arg polymorphism. Eur J Appl Physiol 2014: 114:1-8.
18
19. Ramachandran S, Penumetcha M, Merchant NK, Santanam N, Rong R, Parthasarathy S. Exercise reduces preexisting atherosclerotic lesions in LDL receptor knock out mice. Atherosclerosis 2005; 178:33-38.
19
20. Shimada K, Kishimoto C, Okabe TA, Hattori M, Murayama T, Yokode M, et al. Exercise training reduces severity of atherosclerosis in apolipoprotein E knockout mice via nitric oxide. Circ J 2007; 71:1147-1151.
20
21. Okabe TA, Shimada K, Hattori M, Murayama T, Yokode M, Kita T, et al. Swimming reduces the severity of atherosclerosis in apolipoprotein E deficient mice by antioxidant effects. Cardiovasc Res 2007; 74:537-545.
21
22. Mann S, Beedie C, Jimenez A. Differential effects on cholesterol and lipid profile of physical activity, aerobic exercise, resistance training and combined exercise modalities: A review and synthesis. Sports Med 2014; 44:211-221.
22
23. Heidarian E, Jafari-Dehkordi E, Seidkhani-Nahal A. Effect of garlic on liver phosphatidate phosphohydrolase and plasma lipid levels in hyperlipidemic rats. Food Chem Toxicol 2011; 49:1110-1114.
23
24. Thomas TR, Pellechia J, Rector RS, Sun GY, Sturek MS, Laughlin MH. Exercise training does not reduce hyperlipidemia in pigs fed a high-fat diet. Metabolism 2002; 51:1587-1595.
24
25. Teerapornpuntakit J, Dorkkam N, Wongdee K, Krishnamra N, Charoenphandhu N. Endurance swimming stimulates transepithelial calcium transport and alters the expression of genes related to calcium absorption in the intestine of rats. Am J Physiol Endocrinol Metab 2009; 296:775-786.
25
26. Ishino S, Mukai T, Kume N, Asano D, Ogawa M, Kuge Y, et al. Lectin-like oxidized LDL receptor-1 (LOX-1) expression is associated with atherosclerotic plaque instability--analysis in hypercholesterolemic rabbits. Atherosclerosis 2007; 195:48-56.
26
27. Kataoka H, Kume N, Miyamoto S, Minami M, Moriwaki H, Murase T, et al. Expression of lectinlike oxidized low-density lipoprotein receptor-1 in human atherosclerotic lesions. Circulation 1999; 99:3110-3117.
27
28. Chen H, Li D, Sawamura T, Inoue K, Mehta JL. Upregulation of LOX-1 expression in aorta of hypercholesterolemic rabbits: modulation by losartan. Biochem Biophys Res Commun 2000; 276:1100-1104.
28
29. Nagase M, Ando K, Nagase T, Kaname S, Sawamura T, Fujita T. Redox-Sensitive Regulation of LOX-1 Gene Expression in Vascular Endothelium. Biochem Biophys Res Commun 2001; 281:720–725.
29
30. Mehta JL, Chen J, Hermonat PL, Romeo F, Novelli G. Lectin-like, oxidized low-density lipoprotein receptor-1 (LOX-1): a critical player in the development of atherosclerosis and related disorders. Cardiovasc Res 2006; 69:36-45.
30
31. Szostak J, Laurant P. The forgotten face of regular physical exercise: a natural anti-atherogenic activity. Clin Sci 2011; 121:91-106.
31
32. Hardman AE. Interaction of physical activity and diet: implications for lipoprotein metabolism. Public Health Nutr 1999; 2:369-376.
32
33. Kraus WE, Houmard JA, Duscha BD, Knetzger KJ, Wharton MB, McCartney JS, et al. Effects of the amount and intensity of exercise on plasma lipoproteins. N Engl J Med 2002; 347:1483-1492.
33
34. Karabulut AB, Kafkas ME, Kafkas AS, Onal Y, Kiran TR. The effect of regular exercise and massage on oxidant and antioxidant parameters. Indian J Physiol Pharmacol 2013; 57:378-383.
34
35. Wang JS, Chow SE, Chen JK, Wong MK. Effect of exercise training on oxidized LDL-mediated platelet function in rats. Thromb Haemost 2000;83:503-508.
35
36. Niebauer J, Maxwell AJ, Lin PS, Tsao PS, Kosek J, Bernstein D, et al. Impaired aerobic capacity in hypercholesterolemic mice: partial reversal by exercise training. Am J Physiol 1999; 276:1346-1354.
36
37. Kojda G, Harrison D. Interactions between NO and reactive oxygen species: pathophysiological importance in atherosclerosis, hypertension, diabetes and heart failure. Cardiovasc Res 1999; 43:652-671.
37
38. Raij L. Nitric oxide in the pathogenesis of cardiac disease. J Clin Hypertens 2006; 8:30-39.
38
39. Thompson MA, Henderson KK, Woodman CR, Turk JR, Rush JW, Price E, et al. Exercise preserves endothelium-dependent relaxation in coronary arteries of hypercholesterolemic male pigs. J Appl Physiol 2004; 96:1114-1126.
39
ORIGINAL_ARTICLE
Sphingosine 1-phosphate interacts with Survivin pathway to enhance tumorigenesis in cancer cells
Objective(s):Degradation of sphingosine 1-phosphate (S1P), as a bioactive lipid, or deregulation of its production involves in tumor progression, metastasis and chemoresistance. Since the tumor progression effects of S1P and its mechanism in chronic lymphoblastic leukemia and non-small cell lung cancer is not fully understood, we investigated the role and one of the mechanisms of S1P in tumor progression of SKW3 and H1299 cells.
Materials and Methods: The effects of S1P on proliferation, invasion and migration was studied using MTT assay, soft-agar colony forming assay and trans-well migration assay, respectively. In order to find out the mechanisms of S1P action, the role of S1P on expression of Survivin gene was assessed by real-time RT-PCR.
Results:Our results demonstrated that although invasion was shown only in H1299 cells, low concentration of S1P, especially at 1 μM, mediated proliferation and migration in both cell lines. In addition, these effects of S1P in tumor progression are S1P receptor-dependent, and Survivin plays a key role in S1P tumorigenesis.
Conclusion:Our results confirmed the involvement of S1P and its receptors in tumor progression of SKW3 and H1299. We also investigated another mechanism of S1P involved in cell survival, tumor progression, and Survivin signaling. In conclusion, data demonstrated the importance of this molecule as a target for designing new anticancer drugs such as anti-S1P monoclonal antibody for inhibiting major downstream signaling, which plays significant role in tumorigenesis.
https://ijbms.mums.ac.ir/article_4733_15de9ec9b961d45477872019fdb65bdf.pdf
2015-08-01
813
821
10.22038/ijbms.2015.4733
Invasion
Migration
Proliferation
Survivin
S1P
Maryam
Tabasinezhad
tabasinezhad.m@gmail.com
1
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran Student Research Center Committee, Tabriz university of Medical Sciences, Tabriz, Iran
AUTHOR
Hamid
Ghaedi
h.qaedi@sbmu.ac.ir
2
Medical Genetics Department, Faculty of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
Parisa
Qanbari
p.qanbari@gmail.com
3
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Mahsa
Mohseni
mohseni.mahsa66@gmail.com
4
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Mehdi
Sabzichi
mehdi.radi@yahoo.com
5
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Nasser
Samadi
nassersmd12345@yahoo.com
6
Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz, Iran Department of Medical Biotechnology, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
LEAD_AUTHOR
1. Chalfant CE, Spiegel S. Sphingosine 1-phosphate and ceramide 1-phosphate: expanding roles in cell signaling. J Cell Sci 2005; 118:4605-4612.
1
2. Hannun YA, Obeid LM. Principles of bioactive lipid signaling: lessons from sphingolipids. Nat Rev Mol Cell Biol 2008; 9:139-150.
2
3. Goparaju SK, Jolly PS, Watterson KR, Bektas M, Alvarez S, Sarkar S, et al. The S1P2 receptor negatively regulates platelet-derived growth factor-induced motility and proliferation. Mol Cell Biol 2005; 25:4237-4249.
3
4. Hla T, Brinkmann V. Sphingosine 1-phosphate (S1P) Physiology and the effects of S1P receptor modulation. Neurology 2011; 76:S3-S8.
4
5. Jung B and Hla T. Sphingosin 1-phosphate (S1P) receptors. In: Chun J, Hla T, Spiegel s, Moolenaar W, editors. Lysophospholipid Receptors: Signaling and Biochemistry. 1st ed. John Wiley & Sons Inc; 2013.p.41-60.
5
6. Tabasinezhad M, Samadi N, Ghanbari P, Mohseni M, Saei AA, Sharifi S, et al. Sphingosin 1-phosphate contributes in tumor progression. J Cancer Res Ther 2013; 9:556-563.
6
7. Windh RT, Lee MJ, Hla T, An S, Barr AJ, Manning DR. Differential coupling of the sphingosine 1-phosphate receptors Edg-1, Edg-3, and H218/Edg-5 to the Gi, Gq, and G12 families of heterotrimeric G proteins. J Bio Chem 1999; 274:27351-27358.
7
8. Gangoiti P, Camacho L, Arana L, Ouro A, Granado MH, Brizuela L, et al. Control of metabolism and signaling of simple bioactive sphingolipids: Implications in disease. Prog Lipid Res 2010; 49:316-334.
8
9. Alvarez S.E, Milstien S, Spiegel S. Autocrine and paracrine roles of sphingosine-1-phosphate. Trends Endocrinol Metab 2007; 18:300-307.
9
10. Maceyka M, Harikumar KB, Milstien S, Spiegel S. Sphingosine-1-phosphate signaling and its role in disease. Trends Cell Biol 2012; 22:50-60.
10
11. Oskeritzian CA, Milstien S, Spiegel S. Sphingosine-1-phosphate in allergic responses, asthma and anaphylaxis. Pharmacol Ther 2007; 115:390-399.
11
12. Salas A, Ponnusamy S, Senkal CE, Meyers-Needham M, Selvam SP, Saddoughi SA, et al. Sphingosine kinase-1 and sphingosine 1-phosphate receptor 2 mediate Bcr-Abl1 stability and drug resistance by modulation of protein phosphatase 2A. Blood 2011; 117:5941-5952.
12
13. Ambrosini G, Adida C, Altieri DC. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3:917-921.
13
14. Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, et al. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs. Cancer Res 1998; 58:5315-5320.
14
15. Li S, Chai L, Cai Z, Jin L, Chen Y, Wu H, et al. Expression of Survivin and Caspase 3 in Oral Squamous Cell Carcinoma and Peritumoral Tissue. Asian Pac J Cancer Prev 2012; 13:5027-5031.
15
16. Zhang1 M, Sun YF, Luo S. Ani-survivin DNAzymes inhibit cell proliferation and migration in Breast Cancer Cell Line MCF-7. Asian Pac J Cancer Prev 2012; 13: 6233-37.
16
17. Srivastava AK, Singh PK, Srivastava K, Singh D, Dalela D, Rath SK, et al. Diagnostic role of survivin in urinary bladder cancer. Asian Pac J Cancer Prev 2013; 14: 81-85.
17
18. Cho GS, Ahn TS, Jeong D, Kim JJ, Kim CJ, Cho HD, et al. Expression of the survivin-2B splice variant related to the progression of colorectal carcinoma. J Korean Surg Soc 2011; 80:404-411.
18
19. Brinkmann V. Sphingosine 1-phosphate receptors in health and disease: mechanistic insights from gene deletion studies and reverse pharmacology. Pharmacol Ther 2007; 115:84-105.
19
20. Novgorodov AS, El-Alwani M, Bielawski J, Obeid LM, Gudz TI. Activation of sphingosine-1-phosphate receptor S1P5 inhibits oligodendrocyte progenitor migration. FASEB J 2007; 21:1503-1514.
20
21. Rosen H, Sanna MG, Cahalan SM, Gonzalez-Cabrera PJ. Tipping the gatekeeper: S1P regulation of endothelial barrier function. Trends Immunol 2007; 28:102-107.
21
22. Kluk MJ, Hla T. Signaling of sphingosine-1-phosphate via the S1P/EDG-family of G-protein-coupled receptors. Biochim Biophys Acta 2002; 1582:72-80.
22
23. Takuwa Y. Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors. Biochim Biophys Acta 2002; 1582:112-120.
23
24. Okajima F, Tomura H, Sho K, Nochi H, Tamoto K, Kondo Y. Involvement of pertussis toxin-sensitive GTP-binding proteins in sphingosine 1-phosphate-induced activation of phospholipase Cî—¸ Ca< sup> 2+</sup> system in HL60 leukemia cells. FEBS lett 1996; 379:260-264.
24
25. Yoshida Y, Nakada M, Sugimoto N, Harada T, Hayashi Y, Kita D, et al. Sphingosine‐1‐phosphate receptor type 1 regulates glioma cell proliferation and correlates with patient survival. Int J Cancer 2010; 126:2341-2352.
25
26. Huang YL, Huang WP, Lee H. Roles of sphingosine 1-phosphate on tumorigenesis. World J Biol Chem 2011; 2:25-34.
26
27. Yamashita H, Kitayama J, Shida D, Yamaguchi H, Mori K, Osada M, et al, Sphingosine 1-phosphate receptor expression profile in human gastric cancer cells: differential regulation on the migration and proliferation. J Surg Res 2006; 130:80-87.
27
28. Kluk MJ, Ryan KP, Wang B, Zhang G, Rodig SJ, Sanchez T. Sphingosine-1-phosphate receptor 1 in classical Hodgkin lymphoma: assessment of expression and role in cell migration. Lab Invest 2013; 93:462-471.
28
29. Park KS, Kim MK, Lee HY, Kim SD, Lee SY, Kim JM, et al. S1P stimulates chemotactic migration and invasion in OVCAR3 ovarian cancer cells. Biochem Biophys Res Commun 2007; 356:239-44.
29
30. Gandy KAO, Adada M, Canals D, Carroll B, Roddy P, Hannun YA, et al. Epidermal growth factor-induced cellular invasion requires sphingosine-1-phosphate/sphingosine-1-phosphate 2 receptor-mediated ezrin activation. FASEB J 2013; 27:3155-3166.
30
31. Van Brocklyn JR. Regulation of cancer cell migration and invasion by sphingosine-1-phosphate. World J Biol Chem 2010; 1:307.
31
32. Maceyka M, Payne SG, Milstien S, Spiegel S. Sphingosine kinase, sphingosine-1-phosphate, and apoptosis. Biochim Biophys Acta 2002; 1585:193-201.
32
33. Cuvillier O, Levade T. Sphingosine 1-phosphate antagonizes apoptosis of human leukemia cells by inhibiting release of cytochrome c and Smac/DIABLO from mitochondria. Blood 2001; 98:2828-2836.
33
34. Pyne NJ, Pyne S. Sphingosine 1-phosphate and cancer. Nat Rev Cancer 2010; 10:489-503.
34
35. McNeish I, Lopes R, Bell S, McKay T, Fernandez M, Lockley M, et al. Survivin interacts with Smac/DIABLO in ovarian carcinoma cells but is redundant in Smac-mediated apoptosis. Exp Cell Res 2005; 302:69-82.
35
36. Ling X, Bernacki RJ, Brattain MG, Li F. Induction of survivin expression by taxol (paclitaxel) is an early event, which is independent of taxol-mediated G2/M arrest. J Biol Chem 2004; 279:15196-15203.
36
37. Zhao P, Meng Q, Liu L-Z, You Y-P, Liu N, Jiang B-H. Regulation of survivin by PI3K/Akt/p70S6K1 pathway. Biochem Biophys Res Commun 2010; 395:219-224.
37
38. Shi M, Zhang H, Li M, Xue J, Fu Y, Yan L, et al. Normal endometrial stromal cells regulate survival and apoptosis signaling through PI3K/AKt/Survivin pathway in endometrial adenocarcinoma cells< i> in vitro</i>. Gynecol Oncol 2011; 123:387-392.
38
ORIGINAL_ARTICLE
Propofol differentially inhibits the release of glutamate, γ-aminobutyric acid and glycine in the spinal dorsal horn of rats
Objective(s): Propofol (2, 6-diisopropylphenol) is an intravenous anesthetic that is commonly used for the general anesthesia. It is well known that the spinal cord is one of the working targets of general anesthesia including propofol. However, there is a lack of investigation of the effects of propofol on spinal dorsal horn which is important for the sensory transmission of nociceptive signals. The objective of this study was to investigate the effects of increasing dosage of propofol on the release of glutamate (Glu), γ-aminobutyric acid (GABA) and glycine (Gly) in the spinal dorsal horn. Materials and Methods: The efflux of Glu, GABA or Gly in the spinal dorsal horn of rats was detected using transverse spinal microdialysis under an awake condition and various depths of propofol anesthesia. The infusion rates of propofol were, in order, 400 µg/(kg·min), 600 µg/(kg·min) and 800 µg/(kg·min), with a 20 min infusion period being maintained at each infusion rate. Results: Propofol decreased the glutamate efflux within spinal dorsal horn in a dose-dependent manner, and the maximum decrease was 56.8 ± 6.0% at high-dose propofol infusion producing immobility. The inhibitory GABA and Gly efflux was also decreased about 15–20% at low-dose propofol infusion only producing sedation, but did not continue to drop with higher doses of propofol. Conclusion: Propofol decreased both excitatory and inhibitory amino acids efflux in spinal dorsal horn, and the preferential suppression of the excitatory amino acid might be associated with the analgesic effect of propofol.
https://ijbms.mums.ac.ir/article_4734_79831e3acba25f55d136a830506e3d28.pdf
2015-08-01
822
826
10.22038/ijbms.2015.4734
Amino acids
Anesthetics
Dorsal horn
Microdialysis
Propofol
Jing
Yang
523526931@qq.com
1
Department of Anesthesiology, Chinese People Liberation Army (PLA) General Hospital, Beijing 100853, China
AUTHOR
Wei
Wang
wangwei1982@hotmail.com
2
Department of Orthopedics, Chinese People Liberation Army (PLA) General Hospital, Beijing 100853, China
AUTHOR
Zheng
Yong
3
Department of Pharmacology, Institution of Pharmacology and Toxicology, 100039, China
AUTHOR
Weidong
Mi
weidongmi96@126.com
4
Department of Anesthesiology, Chinese People Liberation Army (PLA) General Hospital, Beijing 100853, China
LEAD_AUTHOR
Hong
Zhang
pengruiwec@163.com
5
Department of Anesthesiology, Chinese People Liberation Army (PLA) General Hospital, Beijing 100853, China
AUTHOR
1.Collins JG, Kendig JJ, Mason P. Anesthetic actions within the spinal cord: Contributions to the state of general anesthesia. Trends Neurosci 1995; 18: 549 -553.
1
2.Kungys G, Kim J, Jinks SL, Atherley RJ, Antognini JF. Propofol produces immobility via action in the ventral horn of the spinal cord by a GABAergic mechanism. Anesth Analg 2009; 108: 1531-1537.
2
3.Willis WD, Westlund KN. Neuroanatomy of the pain system and of the pathways that modulate pain. J Clin Neurophysiol 1997; 14: 2-31.
3
4.Takasusuki T1, Yamaguchi S, Hamaguchi S, Yaksh TL. Effects of general anesthetics on substance P
4
release and c-Fos expression in the spinal dorsal horn. Anesthesiology. 2013; 119: 433-442.
5
5.Antognini JF, Wang XkW, Piercy M, Carstens E. Propofol directly depresses lumbar dorsal horn neuronal responses to noxious stimulation in goats. Can J Anaesth 2000; 47: 273-279.
6
6.Takechi K, Carstens MI, Klein AH, Carstens E. The antinociceptive and antihyperalgesic effects of topical propofol on dorsal horn neurons in the rat. Anesth Analg 2013; 116: 932-938.
7
7.Skilling SR, Smullin DH, Beitz AJ, Larson AA. Extracellular amino acid concentrations in the dorsal spinal cord of freely moving rats following veratridine and nociceptive stimulation. J Neuroehem 1988; 51: 127-132.
8
8.Sluka KA,Westlund KN. (1992). An experimental arthritis model in rats: dorsal horn aspartate and glutamate increases. Neurosci Lett 145: 141-144.
9
9.Valtschanoff JG, Phend KD, Bernardi PS, Weinherg RJ, Rustioni A. Amino acid immunocytochemistry of primary afferent terminals in the rat dorsal horn. J Comp Neurol 1994; 346: 237–252.
10
10.Ataka T1, Kumamoto E, Shimoji K, Yoshimura M. Baclofen inhibits more effectively C-afferent than Adelta-afferent glutamatergic transmission in substantia gelatinosa neurons of adult rat spinal cord slices. Pain 2000, 86: 273-282.
11
11.Engelman HS, MacDermott AB. Presynaptic ionotropic receptors and control of transmitter release. Nat Rev Neurosci 2004; 5: 135-145.
12
12.Ishikawa, T, Marsala, M, Sakabe, T, Yaksh TLl. Characterization of spinal amino acid release and touch-evoked allodynia produced by spinal glycine or GABA (A) receptor antagonist. Neuroscience 2000; 95: 781-786.
13
13.Kleschevnikov AM, Belichenko PV, Gall J, George L, Noshenv MT. Increased efficiency of the GABAA and GABAB receptor-mediated neurotransmission in the Ts65Dn mouse model of Down syndrome. Neurobiol Dis 2012; 45: 683-691.
14
14.Manuel NA, Davies CH. Pharmacological modulation of GABA (A) receptor-mediated postsynaptic potentials in the CA1 region of the rat hippocampus. Br J Pharmacol 1998; 125: 1529-1542.
15
15.Shimizu M, Yamakura T, Tobita T, Okamoto M, Ataka T, et al. Propofol enhances GABAA receptor-mediated presynaptic inhibition in human spinal cord. Neuroreport 2002; 13: 357-360.
16
16.Yamakura T, Bertaccini E, Trudell JR, Harris RA. Anesthetics and ion channels: molecular models and sites of action. Annu Rev Pharmacol Toxicol. 2001; 41:23–51.
17
17.Lü N, Han M, Yang ZL, Wang YQ, Wu GC, Zhang YQ. Nociceptin/Orphanin FQ in PAG modulates the release of amino acids, serotonin and norepinephrine in the rostral ventromedial medulla and spinal cord in rats. Pain 2010; 148: 414-425.
18
ORIGINAL_ARTICLE
Squid ink polysaccharide reduces cyclophosphamide-induced testicular damage via Nrf2/ARE activation pathway in mice
Objective(s):Cyclophosphamide (CP) toxicity on testis was hampered by squid ink polysaccharide (SIP) via restoration of antioxidant ability in our previous investigations. This study investigated roles of Nrf2/ARE signal pathway in testis of treated mice.
Materials and Methods: Male Kunming mice were employed to undergo treatment with SIP and/or CP. Protein levels of Nrf2, keap-1, histone deacetylase 2 (HDAC2), quinone oxidoreductase 1 (NQO-1), and heme oxygenase 1 (HO-1) and phosphorylation level of protein kinase C (PKC) in testis were evaluated by Western blotting.
Results: Data showed that SIP elevated expressions of NQO-1 and HO-1 genes, two downstream target molecules of Nrf2, via activating Nrf2 to play preventive roles on CP-treated testis, and further discovered that upstream regulators of Nrf2, keap-1, HDAC2, and PKC, were concerned with the regulation of Nrf2.
Conclusion: These results suggest that SIP could effectively weaken CP-associated testicular damage via Nrf2/ARE signal pathway.
https://ijbms.mums.ac.ir/article_4735_5a96f407139a35695918cf1ae0eb4bd0.pdf
2015-08-01
827
831
10.22038/ijbms.2015.4735
Cyclophosphamide
Mice
Nrf2/ARE
Squid Ink Polysaccharides
Testis
Xiaoyan
Le
2509913188@qq.com
1
College of Science, Guangdong Ocean University, Zhanjiang, China
AUTHOR
Ping
Luo
352719451@qq.com
2
College of Science, Guangdong Ocean University, Zhanjiang, China
AUTHOR
Yipeng
Gu
951448865@qq.com
3
College of Science, Guangdong Ocean University, Zhanjiang, China
AUTHOR
Yexing
Tao
846653553@qq.com
4
College of Science, Guangdong Ocean University, Zhanjiang, China
AUTHOR
Huazhong
Liu
liuhzbs@163.com
5
College of Science, Guangdong Ocean University, Zhanjiang, China
LEAD_AUTHOR
1. Emadi A, Jones RJ, Brodsky RA. Cyclophosphamide and cancer: golden anniversary. Nat Rev Clin Oncol 2009; 6:638-647.
1
2. Pryzant RM, Meistrich ML, Wislon G, Brown B, McLaughlinP. Long-term reduction in sperm count after chemotherapy with and without radiation therapy for non-hodgkin’s lymphomas. J Clin Oncol 1993; 11:239–247.
2
3. Elangovan N, Chiou TJ, Tzeng WF, Chu ST. Cyclophosphamide treatment causes impairment of sperm and its fertilizing ability in mice. Toxicology 2006; 222:60-70.
3
4. Takaya Y, Uchisawa H, Narumi F, Matsue H. Illexins A, B, and C from squid ink shoule have a branched structure. Biochem Biophys Res Commun 1996; 226:335-338.
4
5. Chen S, Xu J, Xue C, Dong P, Sheng W, Yu G, Chai W. Sequence determination of a non-sulfated glycosaminoglycan-like polysaccharide from melanin-free ink of the squid Ommastrephes bartrami by negative-ion electrospray tandemmass spectrometry and NMR spectroscopy. Glycoconjugate J 2008; 25:481-492.
5
6. Le XY, Luo P, Gu YP, Tao YX, Liu HZ. Interventional effects of squid ink polysaccharides on cyclophosphamide-associated testicular damage in mice. Bratisl Lek Listy 2015; 116: 334-339.
6
7. Tang Q, Zuo T, Lu S, Wu J, Wang J, Zheng R, Chen S, Xue C. Dietary squid ink polysaccharides ameliorated the intestinal microflora dysfunction in mice undergoing chemotherapy. Food Funct 2014; 5: 2529-2535.
7
8. Zuo T, Cao L, Xue C, Tang QJ. Dietary squid ink polysaccharide induces goblet cells to protect small intestine from chemotherapy induced injury. Food Funct 2015; 6: 981-986.
8
9. Zuo T, Cao L, Li X, Zhang Q, Xue C, Tang QJ. The Squid Ink Polysaccharides Protect Tight Junctions and Adherens Junctions from Chemotherapeutic Injury in the Small Intestinal Epithelium of Mice. Nutr Cancer 2015; 67: 364–371.
9
10. Luo P, Liu HZ. Antioxidant ability of squid ink polysaccharides as well as their protective effects on DNA damage in vitro. Afr J Pharm Pharmacol 2013; 7:1382-1388.
10
11. Li Y, Paonessa JD, Zhang Y. Mechanism of chemical activation of Nrf2. Plos One 2012; 7: e35122.
11
12. Tripathi DN, Jena GB. Astaxanthin inhibits cytotoxic and genotoxic effects of cyclophosphamide. Toxicology 2008; 248:96-103.
12
13. Balogun E, Hoque M, Gong P, Killeen E, Green CJ, Foresti R, et al. Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element. Biochem J 2003; 371:887-895.
13
14. Garg R, Gupta S, Maru GB. Dietary curcumin modulates transcriptional regulators of phaseⅠand phaseⅡenzymes in benzo[a]pyrene-treated mice: mechanism of its anti-initiating action. Carcinogenesis 2008; 29:1022-1032.
14
15. Liu F, Li XL, Lin T, He DW, Wei GH, Liu JH, et al. The cyclophosphamide metabolite, acrolein, induces cytoskeletal changes and oxidative stress in Sertoli cells. Mol Biol Rep 2012; 39: 493-500.
15
16. Miao W, Hu L, Scrivens PJ, Batist G. Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway direct cross talk between phaseⅠand phaseⅡ drug-metabolizing enzymes. J Biol Chem 2005; 280:20340-20348.
16
17. Stepkowski TM, Kruszewski MK. Molecular cross-talk between the Nrf2/KEAP1 signaling pathway, autophagy, and apoptosis. Free Radic Biol Med 2011; 50:1186-1195.
17
18. Tripathi DN, Jena GB. Astaxanthin intervention ameliorates cyclophosphamide-induced oxidative stress, DNA damage and early hepatocarcinogenesis in rat: role of Nrf2, p53, p38 and phase-Ⅱ enzymes. Mutat Res 2010; 696:69-80.
18
19. Huang HC, Nguyen T, Pickett CB. Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. J Biol Chem 2002; 277:42769-42774.
19
20. Niture SK, Jain AK, Jaiswal AK. Antioxidant-induced modification of INrf2 cysteine 151 and PKC-δ-mediated phosphorylation of Nrf2 serine 40 are both required for stabilization and nuclear translocation of Nrf2 and increased drug resistance. J Cell Sci 2009; 122:4452-4464.
20
21. Keum YS, Yu S, Chang PP, Yuan X, Kim JH, Xu C, et al. Mechanism of action of sulforaphane: inhibition of p38 mitogen-activated protein kinase isoforms contributing to the induction of antioxidant response element–mediated heme oxygenase-1 in human hepatoma hepG2 cells. Cancer Res 2006; 66:8804-8813.
21
22. Velichkova M,Hasson T. Keap1 regulates the oxidation-sensitive shuttling of Nrf2 into and out of the nucleus via a Crm1-dependent nuclear export mechanism. Mol Cell Biol 2005; 25:4501-4513.
22
23. Sun Z, Chin YE, Zhang DD. Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response. Mol Cell Biol 2009; 29:2658-2672.
23
24. Mercado N, Thimmulappa R, Thomas CM, Fenwick PS, Chana KK, Donnelly LE, Biswal S, Ito K, Barnes PJ. Decreased histone deacetylase 2 impairs Nrf2 activation by oxidative stress. Biochem Biophys Res Commun 2011; 406:292-298.
24
25. Forney GB, Morre DJ, Morre DM. Oxidative stress reduced by a green tea concentrate and capsicum combination: synergistic effects. J Diet Suppl 2013; 10:318-324.
25
26. Li B, Cui W, Tan Y, Luo P, Chen Q, Zhang C, et al. Zinc is essential for the transcription function of Nrf2 in human renal tubule cells in vitro and mouse kidney in vivo under the diabetic condition. J Cell Mol Med 2014; 18:895-906.
26
27. Kobayashi M, Yamamoto M. Nrf2–Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Adv Enzyme Regul 2006; 46:113-140.
27
28. Yang JH, Shin BY, Han JY, Kim MG, Wi JE, Kim YW, et al. Isorhamnetin protects against oxidative stress by activating Nrf2 and inducing the expression of its target genes. Toxicol Appl Pharm 2013; 274:293-301.
28
29. Zhang C, Su ZY, Khor TO, Shu L, Kong AN. Sulforaphane enhances Nrf2 expression in prostate cancer TRAMP C1 cells through epigenetic regulation. Biochem Pharmacol 2013; 85: 1398-1404.
29
ORIGINAL_ARTICLE
Effect of pioglitazone, quercetin and hydroxy citric acid on extracellular matrix components in experimentally induced non-alcoholic steatohepatitis
Objective(s):Non-alcoholic steatohepatitis (NASH), is an important component of Non-alcoholic fatty liver disease (NAFLD) spectrum, which progresses to the end stage liver disease, if not diagnosed and treated properly. The disproportionate production of pro- and anti-inflammatory adipokines secreted from fat contributes to the pathogenesis of NASH. In this study, the comparative effect of pioglitazone, quercetin and hydroxy citric acid on extracellular matrix (ECM) component levels were studied in experimentally induced NASH.
Materials and Methods: The experimental protocol consists of using 48 male Wister rats, which were divided into 8 groups. The levels of hyaluronic acid, leptin and adiponectin were monitored in experimental NASH.
Results:The experimental NASH rats treated with pioglitazone showed significant decrease in the levels of hyaluronic acid and significant increase in adiponectin levels when compared to experimentally induced NASH group, but did not show any effect on the levels of leptin. Contrary to these two drugs, viz. pioglitazone and hydroxy citric acid, the group treated with quercetin showedsignificant decrease in the levels of hyaluronic acid and leptin and significant decrease in adiponectin levels compared with that of experimentally induced NASH NASH group, offering maximum protection against NASH. Conclusion: Considering our findings, it could be concluded that quercetin may offer maximum protection against NASH by significantly increasing the levels of adiponectin, when compared to pioglitazone and hydroxy citric acid.
https://ijbms.mums.ac.ir/article_4736_d2252cb456f634ba7cb0817900c9aa24.pdf
2015-08-01
832
836
10.22038/ijbms.2015.4736
Adiponectin
Hyaluronic acid
Hydroxy citric acid
Leptin
Non-alcoholic fatty liver – disease (NAFLD)
Non-alcoholic–steatohepatitis (NASH)
Pioglitazone
Quercetin
Surapaneni
Krishna Mohan
krishnamohan.surapaneni@gmail.com
1
Department of Biochemistry, Saveetha Medical College and Hospital, Faculty of Medicine, Saveetha University, Saveetha Nagar, Thandalam, Chennai – 602 105, Tamilnadu, India
LEAD_AUTHOR
Vishnu Priya
Veeraraghavan
2
Department of Biochemistry, Saveetha Dental College and Hospital, Saveetha University, 162, P.H.Road, Chennai – 600 077, Tamilnadu, India
AUTHOR
Mallika
Jainu
3
Department of Biomedical Engineering, SSN Engineering College, OMR, Klavakkam, Chennai – 603 110, Tamilnadu, India
AUTHOR
1. Ludwig J, Viggiano TR, McGill DB, Oh BJ. Nonalcoholic steatohepatitis: Mayo Clinic experiences with a hitherto unnamed disease. Mayo Clin Proc 1980; 55:434–438.
1
2. Ahmed MH, Byrne CD. Non-alcoholic steatohepatitis. In Byrne CD, D Wild S, editors. Metabolic syndrome. Chichester: John Wiley & Sons; 2005. p. 279-305.
2
3. Liou I, Kowdley KV. Natural history of nonalcoholic-steatohepatitis. J Clin Gastroenterol 2006; 40: S11–16.
3
4. Charlton M. Nonalcoholic fatty liver disease: a review of current understanding and future impact. Clin Gastroenterol Hepatol 2004; 2:1048–1058.
4
5. Wei Y, Clark SE, Thyfault JP, Uptergrove GM, Li W, Whaley-Connell AT, et al. Oxidative stress-mediated mitochondrial dysfunction contributes to angiotensin II-induced nonalcoholic fatty liver disease in transgenic Ren2 rats. Am J Pathol 2009; 174:1329–1337.
5
6. Tilg H, Diehl AM. Cytokines in alcoholic and nonalcoholic steatohepatitis. N Engl J Med 2000; 343:1467–1476.
6
7. Loffreda S, Yang SQ, Lin HZ, Karp CL, Brengman ML, Wang DJ, et al. Leptin regulates proinflammatory immune responses. FASEB J 1998; 12:57–65.
7
8. Bouloumie A, Marumo T, Lafontan M, Busse R. Leptin induces oxidative stress in human endothelial cells. FASEB J 1999; 13:1231–1238.
8
9. Chitturi S, Farrell G, Frost L, Kriketos A, Lin R, Fung C, et al. Serum leptin in NASH correlates with hepatic steatosis but not fibrosis: a manifestation of lipotoxicity? Hepatology 2002; 36:403–409.
9
10. Tilg H, Hotamisligil GS. Nonalcoholic fatty liver disease: Cytokine- adipokine interplay and regulation of insulin resistance. Gastroenterology 2006; 131:934-945.
10
11. Spiegelman BM, Flier JS. Obesity and the regulation of energy balance. Cell 2001; 104:531-143.
11
12. Friedman JM, Halaas JL. Leptin and the regulation of body weight in mammals. Nature 1998; 395:6763-6770.
12
13. Zhang Y, Proenca R, Maffei M, Barone M, Leopold L, Friedman JM. Positional cloning of the mouse obese gene and its human homologue. Nature 1994; 372:6425-6532.
13
14. Halaas JL, Friedman JM. Leptin and its receptor. J Endocrinol 1997: 155:215-156.
14
15. Surapaneni KM, Jainu M. Pioglitazone, quercetin and hydroxy citric acid effect on hepatic biomarkers in Non Alcoholic Steatohepatitis. Pharmacogn Res 2014; 6:153-162.
15
16. Surapaneni KM, Jainu M. Effect of pioglitazone, quercetin, and hydroxy citric acid on the lipid profile and lipoproteins in experimentally induced non-alcoholicsteatohepatitis (NASH). Indian J Pharm Educ Res 2014; 48:32-38.
16
17. Surapaneni KM, Priya VV, Mallika J. Pioglitazone, quercetin and hydroxy citric acid effect on cytochrome P450 2E1 (CYP2E1) enzyme levels in experimentally induced non alcoholic steatohepatitis (NASH). Eur Rev Med Pharmacol Sci 2014; 18:2736-2741.
17
18. Surapaneni KM, Jainu M. Comparative effect of pioglitazone, quercetin and hydroxy citric acid on the status of lipid peroxidation and antioxidants in experimental non-alcoholic steatohepatitis. J Phyiol Pharmacol 2014; 65:67-74.
18
19. Surapaneni KM, Saraswathi P, Jainu M. Non alcoholic steatohepatitis (NASH) experimental model induction in rats. Int J Pharm Bio Sci 2012; 3:1085 – 1090.
19
20. Surapaneni KM, Sarswathi P, Jainu M. Role of pioglitazone, quercetin and hydroxy citric acid against non alcoholic steatohepatitis (NASH) - histological and scanning electron microscopy (SEM) studies in an experimental model of NASH. Asian J Pharm Clin Res 2012; 5:244-247.
20
21. Stryer L, Biochemistry. 3 rd ed. New York: W. H. Freedman and Company. 1988.p.275 - 277.
21
22. Maffei M, Halaas J, Ravussin E, Pratley RE, Lee GH, Zhang Y, et al. Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects. Nat Med 1995; 1:1151-1161.
22
23. Tsao TS, Murrey HE, Hug C, Lee DH, Lodish HF. Oligomerization state-dependent activation of NF-kappa B signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30). J Biol Chem 2002; 277:29359-29362.
23
24. Suzuki A, Angulo P, Lymp J, Li D, Satomura S, Lindor K. Hyaluronic acid, an accurate serum marker for severe hepatic fibrosis in patients with non-alcoholic fatty liver disease. Liver Int 2005; 25:779–786.
24
25. Oh MK, Winn J,Poordad F. Review article: diagnosis and treatment of non-alcoholic fatty liver disease. Aliment Pharmacol Ther 2008; 28:503–522.
25
26. Miele L, Forgione A, La Torre G, Vero V, Cefalo C, Racco S, et al. Serum levels of HA and tissue metalloproteinase inhibitor-1 combined with age predict the presence of nonalcoholic steatohepatitis in a pilot cohort of subjects with nonalcoholic fatty liver disease. Transl Res 2009; 154:194-201.
26
27. Haukeland JW, Dam°as JK, Konopski Z, Løberg EM, Haaland T, Goverud I, et al. Systemic inflammation in nonalcoholic fatty liver disease is characterized by elevated levels of CCl2. J Hepatol 2006; 44:1167–1174.
27
28. Kamada Y, Takehara T, Hayashi N. Adipocytokines and liver disease. J Gastroenterol 2008; 43:811-822.
28
29. Huang XD, Fan Y, Zhang H, Gifford-Moore D, Huang XD, Christie D, et al. Serum leptin and soluble leptin receptor in non-alcoholic fatty liver disease. World J Gastroenterol 2008; 14:2888- 2893.
29
30. Tsochatzis EA, Manolakopoulos S, Papatheodo-ridis GV, Archimandritis AJ. Insulin resistance and metabolic syndrome in chronic liver diseases: old entities with new implications. Scand J Gastroenterol 2009; 44:6–14.
30
31. Pellme F, Smith U, Funahashi T, Matsuzawa Y, Brekke H, Wiklund O, et al. Circulating adiponectin levels are reduced in nonobese but insulin-resistant first-degree relatives of type 2 diabetic patients. Diabetes 2003; 52:1182–1186.
31
32. Fruebis J, Tsao TS, Javorschi S, Ebbets-Reed D, Erickson MR, Yen FT, et al. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein (Acrp30) increases fatty acid oxidation in muscle and causes weight loss in mice. Proc Natl Acad Sci U S A 2001; 98:2005–2010.
32
33. Berg AH, Combs TP, Scherer PE. ACRP30/adiponectin: an adipokine regulating glucose and lipid metabolism. Trends Endocrinol Metab 2002; 13:84–89.
33
34. Yokota, T, Oritani K, Takahashi I, Ishikawa J, Matsuyama A, Ouchi N et al. Adiponectin new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood 2000; 96: 1723-1732.
34
35. Gastaldelli A, Harrison S, Belfort-Aguiar R, Hardies J, Balas B, Schenker S, et al. Pioglitazone in the treatment of NASH: the role of adiponectin. Aliment Pharmacol Ther 2010; 32:769-775.
35
36. Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med 2001; 7:941–946.
36
37. Wellen KE, Uysal KT, Wiesbrock S, Yang Q, Chen H, Hotamisligil GS. Interaction of tumor necrosis factor-alpha- and thiazolidinedione-regulated pathways. Endocrinology 2004; 145:2214–2220.
37
38. Kubota N, Terauchi Y, Yamauchi T, Kubota T, Moroi M, Matsui J, et al. Disruption of adiponectin causes insulin resistance and neointimal formation. Biol Chem 2002; 277:25863–25866.
38
39. Xu A, Wang Y, Keshaw H, Xu LY, Lam KSL, Cooper GJS. The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver diseases in mice. Clin Invest 2003; 112:91–100.
39
40. Masaki T, Chiba S, Tatsukawa H, Yasuda T, Noguchi H, Seike M, et al. Adiponectin protects LPS- induced liver injury through modulation of TNF- alpha in KK-Ay obese mice. Hepatology 2004; 40:177-184.
40