ORIGINAL_ARTICLE
Significant roles played by interleukin-10 in outcome of pregnancy
Imbalanced immune responses against fetus alloantigens can lead to abnormality in pregnancy. Interleukin-10(IL-10) plays key roles in regulation of immune responses against self and foreign antigens to induce tolerance to these antigens. Therefore, alteration in expression of IL-10 during pregnancy may result in several pathologic conditions such as preterm labor. IL-10 leads to a normal pregnancy via several molecular mechanisms including development of tolerogenic dendritic cells, T regulatory lymphocytes and activation of the JAK1/STAT3 pathway in the target cells. This review has collected recent data regarding the status of IL-10 expression during term and preterm deliveries and also its molecular mechanisms that lead to a normal pregnancy.
https://ijbms.mums.ac.ir/article_6530_92c70d6e5b9ce0c1032c074d182dcede.pdf
2016-02-01
119
124
10.22038/ijbms.2016.6530
IL-10
Preterm delivery
Term delivery
Masoud
Mobini
masoudmobini@gmail.com
1
Immunology of Infectious Diseases Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Maryam
Mortazavi
m_mortazavi58@yahoo.com
2
Department of Gynecology and Obstetrics, Faculty of Medicine, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
LEAD_AUTHOR
Somayeh
Nadi
s.nadi@yahoo.com
3
Yadegar Emam Health Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Mohammad
Zare-Bidaki
h.yousefi31@yahoo.com
4
Immunology of Infectious Diseases Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Somayeh
Pourtalebi
spt782@gmail.com
5
Department of Microbiology, Faculty of Medicine, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Mohammad
Kazemi Arababadi
dr.kazemi@rums.ac.ir
6
Immunology of Infectious Diseases Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
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57
ORIGINAL_ARTICLE
Berberine suppresses migration of MCF-7 breast cancer cells through down-regulation of chemokine receptors
Objective(s): Berberine is one of the main alkaloids and it has been proven to have different pharmacological effects including inhibition of cell cycle and progression of apoptosis in various cancerous cells; however, its effects on cancer metastasis are not well known. Cancer cells obtain the ability to change their chemokine system and convert into metastatic cells. In this study, we examined the effect of berberine on breast cancer cell migration and its probable interaction with the chemokine system in cancer cells.
Materials and Methods: The MCF-7 breast cancer cell line was cultured, and then, treated with berberine (10, 20, 40 and 80 μg/ml) for 24 hr. MTT assay was used in order to determine the cytotoxic effect of berberine on MCF-7 breast cancer cells. Wound healing assay was applied to determine the inhibitory effect of berberine on cell migration. Moreover, real-time quantitative PCR analysis of selected chemokine receptors was performed to determine the probable molecular mechanism underlying the effect of berberine on breast cancer cell migration.
Results: The results of wound healing assay revealed that berberine decreases cell migration. Moreover, we found that the mRNA levels of some chemokine receptors were reduced after berberine treatment, and this may be the underlying mechanism for decreased cell migration.
Conclusion: Our results indicate that berberine might be a potential preventive biofactor for human breast cancer metastasis by targeting chemokine receptor genes.
https://ijbms.mums.ac.ir/article_6531_bae6c063592dffa39d2ce535b80d5cd9.pdf
2016-02-01
125
131
10.22038/ijbms.2016.6531
Anticancer agents
Breast Cancer
Berberine
Chemokine receptors
Metastasis
Naghmeh
Ahmadiankia
ahmadian@shmu.ac.ir
1
Shahroud University of Medical Sciences, Shahroud, Iran
LEAD_AUTHOR
Hamid
Kalalian Moghaddam
2
Shahroud University of Medical Sciences, Shahroud, Iran
AUTHOR
Mohammad Amir
Mishan
mo.am.mishan@gmail.com
3
Department of Biology, Ferdowsi University of Mashhad, Mashhad, Iran
AUTHOR
Ahmad Reza
Bahrami
ar-bahram@um.ac.ir
4
Department of Biology, Ferdowsi University of Mashhad, Mashhad, Iran
AUTHOR
Hojjat
Naderi-Meshkin
5
Stem Cell and Regenerative Medicine Research group, Iranian Academic Center for Education, Culture and Research (ACECR), Mashhad Branch, Mashhad, Iran
AUTHOR
Hamid Reza
Bidkhori
hbidkhori@gmail.com
6
Department of Biology, Ferdowsi University of Mashhad, Mashhad, Iran
AUTHOR
Maryam
Moghaddam
mmoghaddam2@gmail.com
7
Department of Biology, School of Basic Sciences, Islamic Azad University of Damghan, Damghan, Iran
AUTHOR
Seyed Jamal Aldin
Mirfeyzi
8
Department of Biology, School of Basic Sciences, Islamic Azad University of Damghan, Damghan, Iran
AUTHOR
1. Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin 2011;61:69-90.
1
2. Naderi-Meshkin H, Bahrami AR, Bidkhori HR, Mirahmadi M, Ahmadiankia N. Strategies to improve homing of mesenchymal stem cells for greater efficacy in stem cell therapy. Cell biol Int 2015;39:23-34.
2
3. Ben-Baruch A. Organ selectivity in metastasis: regulation by chemokines and their receptors. Clin Exp Metastasis 2008;25:345-356.
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4. Leelawat K, Leelawat S, Narong S, Hongeng S. Roles of the MEK1/2 and AKT pathways in CXCL12/CXCR4 induced cholangiocarcinoma cell invasion. World J Gastroenterol 2007;13:1561-1568.
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5. Sarvaiya PJ, Guo D, Ulasov I, Gabikian P, Lesniak MS. Chemokines in tumor progression and metastasis. Oncotarget 2013;4:2171-2185.
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6. Papatheodorou H, Papanastasiou AD, Sirinian C, Scopa C, Kalofonos HP, Leotsinidis M, et al. Expression patterns of SDF1/CXCR4 in human invasive breast carcinoma and adjacent normal stroma: Correlation with tumor clinicopathological parameters and patient survival. Pathol Res Pract 2014; 210:662-667
6
7. Wang CL, Sun BS, Tang Y, Zhuang HQ, Cao WZ. CCR1 knockdown suppresses human non-small cell lung cancer cell invasion. J Cancer Res Clin Oncol 2009;135:695-701.
7
8. Liu J, Ke F, Xu Z, Liu Z, Zhang L, Yan S, et al. CCR6 Is a Prognostic Marker for Overall Survival in Patients with Colorectal Cancer, and Its Overexpression Enhances Metastasis In vivo. PLoS One 2014;9:e101137.
8
9. Johnson EL, Singh R, Singh S, Johnson-Holiday CM, Grizzle WE, Partridge EE, et al. CCL25-CCR9 interaction modulates ovarian cancer cell migration, metalloproteinase expression, and invasion. World J Surg Oncol 2010;8:62.
9
10. Ginestier C, Liu S, Diebel ME, Korkaya H, Luo M, Brown M, et al. CXCR1 blockade selectively targets human breast cancer stem cells in vitro and in xenografts. J Clin Invest 2010;120:485-497.
10
11. Moghaddam HK, Baluchnejadmojarad T, Roghani M, Khaksari M, Norouzi P, Ahooie M, et al. Berberine ameliorate oxidative stress and astrogliosis in the hippocampus of STZ-induced diabetic rats. Mol Neurobiol 2014;49:820-826.
11
12. Refaat A, Abdelhamed S, Yagita H, Inoue H, Yokoyama S, Hayakawa Y, et al. Berberine enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in breast cancer. Oncol Lett 2013;6:840-844.
12
13. Jabbarzadeh Kaboli P, Rahmat A, Ismail P, Ling KH. Targets and mechanisms of berberine, a natural drug with potential to treat cancer with special focus on breast cancer. Eur J Pharmacol 2014;740:584-595. 14. Patil JB, Kim J, Jayaprakasha GK. Berberine induces apoptosis in breast cancer cells (MCF-7) through mitochondrial-dependent pathway. Eur J Pharmacol 2010;645:70-78.
13
15. Shibata T, Matsuo Y, Shamoto T, Hirokawa T, Tsuboi K, Takahashi H, et al. Girdin, a regulator of cell motility, is a potential prognostic marker for esophageal squamous cell carcinoma. Oncol Rep 2013;29:2127-2132.
14
16. Olson TS, Ley K. Chemokines and chemokine receptors in leukocyte trafficking. Am J Physiol Regul Integr Comp Physiol 2002;283:R7-R28.
15
17. Singh S, Singh UP, Stiles JK, Grizzle WE, Lillard JW, Jr. Expression and functional role of CCR9 in prostate cancer cell migration and invasion. Clin Cancer Res 2004;10:8743-8750.
16
18. Jiang QF, Wu TT, Yang JY, Dong CR, Wang N, Liu XH, et al. 17beta-estradiol promotes the invasion and migration of nuclear estrogen receptor-negative breast cancer cells through cross-talk between GPER1 and CXCR1. J Steroid Biochem Mol Biol 2013;138:314-324.
17
19. Varney ML, Singh S, Li A, Mayer-Ezell R, Bond R, Singh RK. Small molecule antagonists for CXCR2 and CXCR1 inhibit human colon cancer liver metastases. Cancer Lett 2011;300:180-188.
18
20. Zhang Z, Ni C, Chen W, Wu P, Wang Z, Yin J, et al. Expression of CXCR4 and breast cancer prognosis: a systematic review and meta-analysis. BMC Cancer 2014;14:49.
19
21. Ling X, Spaeth E, Chen Y, Shi Y, Zhang W, Schober W, et al. The CXCR4 antagonist AMD3465 regulates oncogenic signaling and invasiveness in vitro and prevents breast cancer growth and metastasis in vivo. PLoS One 2013;8:e58426.
20
22. Sun Y, Mao X, Fan C, Liu C, Guo A, Guan S, et al. CXCL12-CXCR4 axis promotes the natural selection of breast cancer cell metastasis. Tumour Biol 2014 35:7765-7773
21
23. Richmond A. Nf-kappa B, chemokine gene transcription and tumour growth. Nat Rev Immunol 2002;2:664-674.
22
24. Singh T, Vaid M, Katiyar N, Sharma S, Katiyar SK. Berberine, an isoquinoline alkaloid, inhibits melanoma cancer cell migration by reducing the expressions of cyclooxygenase-2, prostaglandin E(2) and prostaglandin E(2) receptors. Carcinogenesis 2011;32:86-92.
23
25. Tillhon M, Guaman Ortiz LM, Lombardi P, Scovassi AI. Berberine: new perspectives for old remedies. Biochem Pharmacol 2012;84:1260-1267.
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26. Courtney KD, Corcoran RB, Engelman JA. The PI3K pathway as drug target in human cancer. J Clin Oncol 2010;28:1075-1083.
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27. Mitchell B, Leone D, Feller K, Menon S, Bondzie P, Yang S, et al. Protein expression of the chemokine receptor CXCR4 and its ligand CXCL12 in primary cutaneous melanoma-biomarkers of potential utility? Hum Patho. 2014. 45:2094-3000.
26
28. Davis ME, Zuckerman JE, Choi CH, Seligson D, Tolcher A, Alabi CA, et al. Evidence of RNAi in humans from systemically administered siRNA via targeted nanoparticles. Natur. 2010;464:1067-1070.
27
ORIGINAL_ARTICLE
In vitro and in silico studies of the inhibitory effects of some novel kojic acid derivatives on tyrosinase enzyme
Objective(s): Tyrosinase is a key enzyme in pigment synthesis. Overproduction of melanin in parts of the skin results in hyperpigmentation diseases. This enzyme is also responsible for the enzymatic browning in fruits and vegetables. Thus, its inhibitors are of great importance in the medical, cosmetic and agricultural fields. Materials and Methods: A series of twelve kojic acid derivatives were designed to be evaluated as tyrosinase activity inhibitors. The potential inhibitory activity of these compounds was investigated in silico using molecular docking simulation method. Four compounds with a range of predicted tyrosinase inhibitory activities were prepared and their inhibitory effect on tyrosinase activity was evaluated. The antioxidant properties of these compounds were also investigated by in vitro DPPH (2,2-diphenyl-1-picrylhydrazyl) and hydrogen peroxide scavenging assays. Results: Compound IIId exhibited the highest tyrosinase inhibitory activity with an IC50 value of 0.216 ± 0.009 mM which was in accordance with the in silico ΔGbind results (-13.24 Kcal/mol).
Conclusion: Based on the docking studies, from the twelve compounds studied, one (IIId) appeared to have the highest inhibition on tyrosinase activity. This was confirmed by enzyme activity measurements. Compound IIId has an NO2 group which binds to both of Cu2+ ions located inside the active site of the enzyme. This compound appeared to be even stronger than kojic acid in inhibiting tyrosinase activity. The DPPH free radical scavenging ability of all the studied compounds was more than that of BHT. However, they were not as strong as BHT or gallic acid in scavenging hydrogen peroxide.
https://ijbms.mums.ac.ir/article_6533_bfc308ab77a54d39a6c686efb3cfa990.pdf
2016-02-01
132
144
10.22038/ijbms.2016.6533
Antioxidant activity
In silico studies
Kojic acid
Tyrosinase
Azizeh
Asadzadeh
az.asadzadeh@yahoo.com
1
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
AUTHOR
Hajar
Sirous
2
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Morteza
Pourfarzam
pourfarzam@pharm.mui.ac.ir
3
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Parichehreh
Yaghmaei
yaghmaei_p@srbiau.ac.ir
4
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
AUTHOR
Afshin
Fassihi
fassihi@pharm.mui.ac.ir
5
Department of Biochemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
LEAD_AUTHOR
1. Chang TS. An updated review of tyrosinase inhibitors. Int J Mol Sci 2009; 10:2440-2475.
1
2. Muñoz-Muñoz JL, García-Molina Mdel M, Garcia-Molina F, Berna J, Garcia-Ruiz PA, García-Moreno M, et al. Catalysis and inactivation of tyrosinase in its action on o-diphenols, o-aminophenols and o-phenylendiamines: Potential use in industrial applications. J Mol Catal B Enzym 2013; 91:17-24.
2
3. Therdphapiyanak N, Jaturanpinyo M, Waranuch N, Kongkaneramit L, Sarisuta N. Development and assessment of tyrosinase inhibitory activity of liposomes of Asparagus racemosus extracts. Asian J Pharm Sci2013; 8:134-142.
3
4. Li ZC, Chen LH, Yu XJ, Hu YH, Song KK, Zhou XW, et al. Inhibition kinetics of chlorobenzaldehyde thiosemicarbazones on mushroom tyrosinase. J Agric Food Chem 2010; 58:12537-12540.
4
5. Guerrero A, Rosell G. Biorational approaches for insect control by enzymatic inhibition. Curr Med Chem 2005; 12:461-469.
5
6. Loizzo MR, Tundis R, Menichini F. Natural and synthetic tyrosinase inhibitors as antibrowning agents: An update. Compr Rev Food Sci Food Saf 2012; 11:378-398.
6
7. Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F. Similar enzyme activation and catalysis in hemocyanins and tyrosinases. Gene 2007; 398:183–191.
7
8. De Faria RO, Moure VR, Lopes MA, Krieger N, Mitchell DA. The biotechnological potential of mushroom tyrosinases. Food Technol Biotech 2007; 45:287-294.
8
9. Aytemir MD, Karakaya G, Ekinci D. Kojic acid derivatives. In: Ekinci Deniz., editor. Medicinal Chemistry and Drug Design. 2012. pp. 1–26.
9
10. Noh JM, Kwak SY, Seo HS, Seo JH, Kim BG, Lee YS. Kojic acid–amino acid conjugates as tyrosinase inhibitors. Bioorg Med Chem Lett 2009; 19:5586-5589.
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18. Mohammadpour M, Sadeghi A, Fassihi A, Saghaei L, Movahedian A, Rostami M. Synthesis and antioxidant evaluation of some novel orthohydroxypyridine-4-one iron chelators. Res Pharm Sci 2012; 3:171-179
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19. Ahn SM, Rho HS, Baek HS, Joo YH, Hong YD, Shin SS,et al. Inhibitory activity of novel kojic acid derivative containing trolox moiety on melanogenesis. Bioorg Med Chem Lett 2011; 24:7466-7469.
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36. Chung KW, Jeong HO, Jang EJ, Choi YJ, Kim DH, Kim SR, et al. Characterization of a small molecule inhibitor of melanogenesis that inhibits tyrosinase activity and scavenges nitric oxide (NO). Biochim Biophys Acta 2013; 1830:4752–4761.
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41
ORIGINAL_ARTICLE
Growth suppression effect of human mesenchymal stem cells from bone marrow, adipose tissue, and Wharton's jelly of umbilical cord on PBMCs
Objective(s):Immunosuppressive property of mesenchymal stem cells (MSCs) has great attraction in regenerative medicine especially when dealing with tissue damage involving immune reactions. The most attractive tissue sources of human MSCs used in clinical applications are bone marrow (BM), adipose tissue (AT), and Wharton's jelly (WJ) of human umbilical cord. The current study has compared immunomodulatory properties of human BM, AT, and WJ-MSCs. Materials and Methods: Three different types of human MSCs were isolated, cultured, and characterized by flow cytometry and differentiation potentials. The MSCs were co-cultured with allogeneic phytohemagglutinin (PHA) activated peripheral blood mononuclear cells (PBMCs). The proliferation of PBMCs was assessed by flow cytometry of carboxyfluorescein succinimidyl ester (CFSE) stained cells and compared to each other and to the growth of PBMCs in the absence of MSCs, 3 days post co-culture. Additionally, the growth suppression was indirectly assessed by using the transwell culture system. Results: the proliferation of PBMCs reduced to 6.2, 7 and 15.4- fold in cultures with AT-MSCs, WJ-MSCs, and BM-MSCs, respectively, compared to the PHA-activated cells. When the growth suppression was indirectly assessed by using the transwell culture system, it was revealed that AT-MSCs, WJ-MSCs, and BM-MSCs caused growth reduction in PBMCs to 3, 8, and 8 -fold, respectively, compared to the PHA-activated cells. Conclusion:These data collectively conclude that the immunomodulatory effects of MSCs, which may mostly carry out through direct cell to cell contact, are different between various sources. Accordingly results of this study may contribute to the application of these cells in cell therapy and regenerative medicine.
https://ijbms.mums.ac.ir/article_6535_e1083312874779d139713c5d13fb0b8f.pdf
2016-02-01
145
153
10.22038/ijbms.2016.6535
Adipose tissue
bone marrow
Immunosuppression
Mesenchymal stem cell (MSC)
Regenerative medicine
Wharton's jelly
Maryam
Ayatollahi
ayatollmb@yahoo.com
1
Transplant Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Tahereh
Talaei-Khozani
talaeit@sums.ac.ir
2
Laboratory for Stem Cell Research, Department of Anatomy, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Mahboobeh
Razmkhah
mrazmkhah2@gmail.com
3
Shiraz Institute for Cancer Research, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
LEAD_AUTHOR
1. Chamberlain G, Fox J, Ashton B, Middleton J. Concise review: mesenchymal stem cells: their phenotype, differentiation capacity, immunological features, and potential for homing. Stem Cells 2007; 25: 2739-2749.
1
2. Mareschi K, Ferrero I, Rustichelli D, Aschero S, Gammaitoni L, Aglietta M, et al. Expansion of mesenchymal stem cells isolated from pediatric and adult donor bone marrow. J Cell Biochem 2006; 97:744-754.
2
3. Mitchell KE, Weiss ML, Mitchell BM, Martin P, Davis D, Morales L, et al. Matrix cells from Wharton’s jelly form neurons and glia. Stem Cells 2003; 21:50–60.
3
4. Friedenstein AJ, Gorskaja UF, Julagina NN. Fibroblast precursors in normal and irradiated mouse hematopoietic organs. Exp Hematol 1976; 4:267–274.
4
5. Ankrum J, Karp JM. Mesenchymal stem cell therapy: Two steps forward, one step back. Trends Mol Med 2010; 16:203–209.
5
6. Kassem M, Kristiansen M, Abdallah BM. Mesenchymal stem cells: cell biology and potential use in therapy. Basic Clin Pharmacol Toxicol 2004; 95:209–214.
6
7. Docheva D, Popov C, Mutschler W, Schieker M. Human mesenchymal stem cells in contact with their environment: surface characteristics and the integrin system. J Cell Mol Med 2007; 11:21-38.
7
8. Nardi NB, Meirelles SD. Mesenchymal stem cells: isolation, in vitro expansion and characterization. HEP 2006; 174:249–282.
8
9. Kim N, Cho SG. Clinical applications of mesenchymal stem cells. Korean J Intern Med 2013; 28:387-402.
9
10. Zappia E, Casazza S, Pedemonte E, Benvenuto F, Bonanni I, Gerdoni E, et al. Mesenchymal stem cells ameliorate experimental autoimmune encephalomyelitis inducing T-cell anerg. Blood 2005; 106:1755–1761.
10
11. Ortiz LA, Gambelli F, McBride C, Gaupp D, Baddoo M, Kaminski N, et al. Mesenchymal stem cell engraftment in lung is enhanced in response to bleomycin exposure and ameliorates its fibrotic effects. Proc Natl Acad Sci USA 2003; 100:8407–8411.
11
12. Polchert D, Sobinsky J, Douglas G, Kidd M, Moadsiri A, Reina E, et al. IFN-c activation of mesenchymal stem cells for treatment and prevention of graft versus host disease. Eur J Immunol 2008; 38:1745–1755.
12
13. Sakaguchi Y, Sekiya I, Yagishita K, Muneta T. Comparison of human stem cells derived from various mesenchymal tissues: superiority of synovium as a cell source. Arthritis Rheum 2005; 52:2521-2529.
13
14. Erices A, Conget P, Minguell JJ. Mesenchymal progenitor cells in human umbilical cord blood. Br J Haematol 2000; 109:235-242.
14
15. Musina RA, Bekchanova ES, Sukhikh GT. Comparison of mesenchymal stem cells obtained from different human tissues. Bull Exp Biol Med 2005; 139:504-509.
15
16. Jurgens WJ, Oedayrajsingh-Varma MJ, Helder MN, Zandiehdoulabi B, Schouten TE, Kuik DJ, et al. Effect of tissue-harvesting site on yield of stem cells derived from adipose tissue: implications for cell-based therapies. Cell Tissue Res 2008; 332:415–426.
16
17. Sarugaser R, Lickorish D, Baksh D, Hosseini MM, Davies JE. Human umbilical cord perivascular (HUCPV) cells: A source of mesenchymal progenitors. Stem Cells 2005; 23:220–229.
17
18. Wang HS, Hung SC, Peng ST, Huang CC, Wei HM, Guo YJ, et al. Mesenchymal stem cells in the Wharton’s jelly of the human umbilical cord. Stem Cells 2004; 22:1330–1337.
18
19. Ayatollahi M, Soleimani M, Geramizadeh B, Imanieh MH. Insulin-like growth factor1 (IGF-I) improves hepatic differentiation of human bone marrow-derived mesenchymal stem cells. Cell Biol Int 2011; 35:1169-1176.
19
20. Razmkhah M, Abedi N, Hosseini A, Imani MT, Talei AR, Ghaderi A. Induction of T regulatory subsets from Naïve CD4+ T cells after exposure to breast cancer adipose derived stem cells. Iran J Immunol 2015; 12:1-15.
20
21. Rezaeifard S, Razmkhah M, Robati M, Momtahan M, Ghaderi A. Adipose derived stem cells isolated from omentum: a novel source of chemokines for ovarian cancer growth. J Cancer Res Ther 2014; 10:159-164.
21
22. Sakai D, Mochida J, Yamamoto Y, Nomura T, Okuma M, Nishimura K, et al. Transplantation of mesenchymal stem cells embedded in Atelocollagen gel to the intervertebral disc: a potential therapeutic model for disc degeneration. Biomaterials 2003; 24:3531-3541.
22
23. Shang Q, Wang Z, Liu W, Shi Y, Cui L, Cao Y. Tissue-engineered bone repair of sheep cranial defects with autologous bone marrow stromal cells. J Craniofac Surg 2001; 12:586–593.
23
24. Shintani S, Murohara T, Ikeda H, Ueno T, Honma T, Katoh A, et al. Mobilization of endothelial progenitor cells in patients with acute myocardial infarction. Circulation 2001; 103:2776–2779.
24
25. Noort WA, Kruisselbrink AB, In’t Anker PS, Kruger M, van Bezooijen RL, de Paus RA, et al. Mesenchymal stem cells promote engraftment of human umbilical cord blood derived CD34(+) cells in NOD/SCID mice. Exp Hematol 2002; 30:870–878.
25
26. Le Blanc K, Rasmusson I, Sundberg B, Götherström C, Hassan M, Uzunel M, et al. Treatment of severe acute graft-versus-host disease with third party haploidentical mesenchymal stem cells. Lancet 2004; 363:1439-1441.
26
27. Erices A, Conget P, Minguell JJ. Mesenchymal progenitor cells in human umbilical cord blood. Br J Hematol 2000; 109:235–242.
27
28. Strioga M, Viswanathan S, Darinskas A, Slaby O, Michalek J. Same or not the same? Comparison of adipose tissue-derived versus bone marrow-derived mesenchymal stem and stromal cells. Stem Cells Dev 2012; 21:2724-2752.
28
29. Prasanna SJ, Gopalakrishnan D, Shankar SR, Vasandan AB. Pro-inflammatory cytokines, IFNgamma and TNFalpha, influence immune properties of human bone marrow and Wharton jelly mesenchymal stem cells differentially. PLoS One 2010; 5:e9016.
29
30. Amable PR, Teixeira MV, Carias RB, Granjeiro JM, Borojevic R. Protein synthesis and secretion in human mesenchymal cells derived from bone marrow, adipose tissue and Wharton's jelly. Stem Cell Res Ther 2014; 5:53.
30
31. Ribeiro A, Laranjeira P, Mendes S, Velada I, Leite C, Andrade P, et al. Mesenchymal stem cells from umbilical cord matrix, adipose tissue and bone marrow exhibit different capability to suppress peripheral blood B, natural killer and T cells. Stem Cell Res Ther 2013; 4:125.
31
32. Bochev I, Elmadjian G, Kyurkchiev D, Tzvetanov L, Altankova I, Tivchev P, et al. Mesenchymal stem cells from human bone marrow or adipose tissue differently modulate mitogen-stimulated B-cell immunoglobulin production in vitro. Cell Biol Int 2008; 32:384–393.
32
33. Ivanova-Todorova E, Bochev I, Mourdjeva M, Dimitrov R, Bukarev D, Kyurkchiev S, et al. Adipose tissue-derived mesenchymal stem cells are more potent suppressors of dendritic cells differentiation compared to bone marrow-derived mesenchymal stem cells. Immunol Lett 2009; 126:37–42.
33
34. Najar M, Raicevic G, Jebbawi F, De Bruyn C, Meuleman N, Bron D, et al. Characterization and functionality of the CD200-CD200R system during mesenchymal stromal cell interactions with T-lymphocytes. Immunol Lett 2012; 146:50-56.
34
ORIGINAL_ARTICLE
Evaluation of Δ9-tetrahydrocannabinol metabolites and oxidative stress in type 2 diabetic rats
Objective(s): The object of the study is to examine the effects of Δ9-tetrahydrocannabinol (THC) against oxidative stress in the blood and excretion of THC metabolites in urine of type 2 diabetic rats. Materials and Methods: The control (n=8), THC control (n=6), diabetes (n=8) and diabetes + THC (n=7) groups were created. Type 2 diabetes was induced by nicotinamide (NA, 85 mg/kg) + streptozotocin (STZ, 65 mg/kg). THC was administered intraperitoneally for seven days. The glutathione (GSH) level in erythrocytes and malondialdehyde (MDA) level, superoxide dismutase (SOD) and catalase (CAT) enzyme activities in plasma were measured. THC metabolites were analyzed in urine. Results: The results showed that the erythrocyte GSH levels were significantly increased (P<0.05), but plasma MDA levels were non-significantly decreased in diabetes group treated with THC when compared with the diabetes group. The CAT activity was non-significantly reduced and SOD was significantly increased (P<0.01) in the plasma of diabetes induced by THC in comparison with the diabetic group. The excretion of THC metabolites was higher in the urine of diabetes + THC rats as compared to the THC control rats. Conclusion: These findings highlight that THC treatment may attenuate slightly the oxidative stress in diabetic rats. The excretion rate of THC may vary in the type 2 diabetes mellitus status.
https://ijbms.mums.ac.ir/article_6536_cc5fbadd9ae6d42134e382bf4566c999.pdf
2016-02-01
154
158
10.22038/ijbms.2016.6536
Diabetes Mellitus
Metabolite
Oxidative stress
Type 2
Urine
Δ9-tetrahydrocannabinol
Zeynep
Coskun
zeynepminecoskun@gmail.com
1
Department of Molecular Biology and Genetics, Faculty of Arts and Sciences, Istanbul Bilim University, Istanbul, Turkey
LEAD_AUTHOR
Sema
Bolkent
bolkent@istanbul.edu.tr
2
Department of Medical Biology, Faculty of Cerrahpasa Medicine, Istanbul University, Istanbul, Turkey
AUTHOR
1. Hillig KW, Mahlberg PG. A chemotaxonomic analysis of cannabinoid variation in Cannabis (Cannabaceae). Am J Bot 2004; 91:961-975.
1
2. Kochanowski M, Kała M. Tetrahydrocannabinols in clinical and forensic toxicology. Przegl Lek 2005; 62:576-580.
2
3. Gieringer D, Rosenthal E, Carter GT. Marijuana medical handbook: Practical guide to the therapeutic uses of marijuana. Berkley, CA, USA: 2008.
3
4. ElSohly MA, Slade D. Chemical constituents of marijuana: The complex mixture of natural cannabinoids. Life Sci 2005; 78:539-548.
4
5. Borgelt LM, Franson KL, Nussbaum AM, Wang GS. The pharmacologic and clinical effects of medical cannabis. Pharmacotherapy 2013; 33:195-209.
5
6. Lutge EE, Gray A, Siegfried N. The medical use of cannabis for reducing morbidity and mortality in patients with HIV/AIDS. Cochrane Database Syst Rev 2013; 4:CD005175.
6
7. Reynolds TD, Osborn HL. The use of cannabinoids in chronic pain. BMJ Case Rep 2013; bcr2013010417.
7
8. Carroll CB, Zeissler ML, Hanemann CO, Zajicek JP. Δ⁹-tetrahydrocannabinol (Δ⁹-THC) exerts a direct neuroprotective effect in a human cell culture model of Parkinson's disease. Neuropathol Appl Neurobiol 2012; 38:535-547.
8
9. Chen J, Errico SL, Freed WJ. Reactive oxygen species and p38 phosphorylation regulate the protective effect of delta9-tetrahydrocannabinol in the apoptotic response to NMDA. Neurosci Lett 2005; 389:99-103.
9
10. Li X, Kaminski NE, Fischer LJ. Examination of the immunosuppressive effect of delta9-tetrahydro-cannabinol in streptozotocin-induced autoimmune diabetes. Int Immunopharmacol 2001; 1:699-712.
10
11. Moldzio R, Pacher T, Krewenka C, Kranner B, Novak J. Effects of cannabinoids Δ(9)-tetrahydrocannabinol, Δ(9)-tetrahydrocannabinolic acid and cannabidiol in MPP+ affected murine mesencephalic cultures. Phytomedicine 2012; 19:819-824.
11
12. Sagredo O, Pazos MR, Satta V, Ramos JA, Pertwee RG, Fernández-Ruiz J. Neuroprotective effects of phytocannabinoid-based medicines in experimental models of Huntington's disease. J Neurosci Res 2011; 89:1509-1518.
12
13. Shinde SN, Dhadke VN, Suryakar AN. Evaluation of oxidative stress in type 2 diabetes mellitus and follow-up along with vitamin E supplementation. Indian J Clin Biochem 2011; 26:74-77.
13
14. Kassab A, Piwowar A. Cell oxidant stress delivery and cell dysfunction onset in type 2 diabetes. Biochimie 2012; 94:1837-1848.
14
15. Chen L, Magliano DJ, Zimmet PZ. The worldwide epidemiology of type 2 diabetes mellitus-present and future perspectives. Nat Rev Endocrinol 2011; 8:228-236.
15
16. Wolfsdorf J, Glaser N, Sperling MA. Diabetic ketoacidosis in infants, children, and adolescents. Diabetes Care 2006; 29:1150-1159.
16
17. Masiello P, Broca C, Gross R, Roye M, Manteghetti M, Hillaire-Buys D, et al. Experimental NIDDM: development of a new model inadult rats administered streptozotocin and nicotinamide. Diabetes 1998; 47:224–229.
17
18. Murugan P, Pari L. Influence of tetrahydrocurcumin on hepatic and renal functional markers and protein levels in experimental type 2 diabetic rats. Basic Clin Pharmacol Toxicol 2007; 101:241-245.
18
19. Beutler E, Duron O, Kelly BM. Improved method for the determination of blood glutathione. J Lab Clin Med 1963; 51:882-888.
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20. Crosby WN, Munn JI, Furth FW. Standardizing a method for clinical hemoglobinometry. U S Armed Forces Med J 1954; 5:693- 703.
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21. Ledwozyw A, Michalak J, Stepień A, Kadziolka A. The relationship between plasma triglycerides, cholesterol, total lipids and lipid peroxidation products during human atherosclerosis. Clin Chim Acta 1986; 155:275-283.
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22. Sun Y, Oberley LW, Li Y. A simple method for clinical assay of superoxide dismutase. Clin Chem 1988; 34:497-500.
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23. Aebi H. Catalase in vitro. Methods Enzymol 1984; 105:121–126.
23
24. Coskun ZM, Bolkent S. Oxidative stress and cannabinoid receptor expression in type-2 diabetic rat pancreas following treatment with Δ(9) -THC. Cell Biochem Funct 2014; 32:612-619.
24
25. Chang YC, Chuang LM. The role of oxidative stress in the pathogenesis of type 2 diabetes: from molecular mechanism to clinical implication. Am J Transl Res 2010; 2:316-331.
25
26. Niedowicz DM, Daleke DL. The role of oxidative stress in diabetic complications. Cell Biochem Biophys 2005; 43:289-330.
26
27. Kopáni M, Celec P, Danisovic L, Michalka P, Biró C. Oxidative stress and electron spin resonance. Clin Chim Acta 2006; 364:61-66.
27
28. Koch JE. Delta (9)-THC stimulates food intake in Lewis rats: effects on chow, high-fat and sweet high-fat diets. Pharmacol Biochem Behav 2001; 68:539-543.
28
29. Robson P. Therapeutic aspects of cannabis and cannabinoids. Br J Psychiatry 2001; 178:107-115.
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30. Hampson AJ, Grilmaldi M, Axelrod J, Wink D. Cannabidiol and (-)Δ9-tetrahydrocannabinol are neuroprotective antioxidants. Proc Natl Acad Sci 1998; 95:8268-8273.
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31. Nicotera P, Orrenius S. Role of thiols in protection against biological reactive intermediates. Adv Exp Med Biol 1986; 197:41–49.
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32. Feillet-Coudray C, Rock E, Coudray C, Grzelkowska K, Azais-Braesco V, Dardavet D, et al. Lipid peroxidation and antioxidant status in experimental diabetes. Clin Chim Acta 1999; 284:31-43.
32
33. Coskun ZM, Sacan O, Karatug A, Turk N, Yanardag R, Bolkent S, et al. Regulation of oxidative stress and somatostatin, cholecystokinin, apelin gene expressions by ghrelin in stomach of newborn diabetic rats. Acta Histochem 2013; 115:740-747.
33
34. Abdel-Salam OME, Nada SA, Salem NA, El-Sayed El-Shamarka M, Omara E. Effect of Cannabis sativa on oxidative stress and organ damage after systemic endotoxin administration in mice. Comp Clin Pathol 2013; 23:1069-1085.
34
35. Lowe RH, Abraham TT, Darwin WD, Herning R, Cadet JL, Huestis MA. Extended urinary Delta9-tetrahydrocannabinol excretion in chronic cannabis users precludes use as a biomarker of new drug exposure. Drug Alcohol Depend 2009; 105:24-32.
35
36. Kreuz DS, Axelrod J. Delta-9-tetrahydrocannabinol: localization in body fat. Science 1973; 179:391-393.
36
ORIGINAL_ARTICLE
Essential oils chemical composition, antioxidant activities and total phenols of Astrodaucus persicus
Objective(s):Astrodaucus persicus, Apiaceae, is used as vegetable or food additive in some parts of Iran. The essential oils of different parts of Astrodaucus persicus from Kordestan province were analyzed for the first time and compared with other regions. In this study, antioxidant activities and total phenols determination of aerial parts essential oils and root fractions of A. persicus were investigated. Materials and Methods: The essential oils were obtained by hydro-distillation from flowers/fruits, leaves/stems, ripe fruits and roots of plant and analyzed by GC-MS. Crude root extract was fractionated with hexane, chloroform, ethyl acetate and methanol. Antioxidant activities by DPPH and FRAP methods and total phenols by Folin-ciocalteu assay were measured. Results: The abundant compounds of flowers/fruits blue essential oil were α-thujene, β-pinene and α-pinene. The predominant components of blue leaves/stems essential oil were α-thujene, α-pinene and α-fenchene. The major volatiles of ripe fruits blue essential oil were β-pinene, α-thujene and α-pinene. The chief compounds of root yellow essential oil were trans-caryophyllene, bicycogermacrene and germacrene-D. Total root extract and ethyl acetate fraction showed potent antioxidant activities and high amount of total phenols in comparison to other samples. Among volatile oils, the flowers/fruits essential oil showed potent reducing capacity. Conclusion: The major compounds of aerial parts essential oils were hydrocarbon monoterpenes while the chief percentage of roots essential oil constituents were hydrocarbon sesquiterpenes. α-Eudesmol and β-eudesmol were identified as responsible for creation of blue color in aerial parts essential oils. A. persicus was known as a potent antioxidant among Apiaceae.
https://ijbms.mums.ac.ir/article_6539_9b61f4b725a2ae13033e19721f7d7348.pdf
2016-02-01
159
165
10.22038/ijbms.2016.6539
Apiaceae
Blue volatile
Free radical scavenger
Oxidation-reduction
Root fractions
Saeid
Goodarzi
saeid.goodarzi@yahoo.com
1
Department of Pharmacognosy, Faculty of Pharmacy and Medicinal Plant Research Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Abbas
Hadjiakhoondi
abbhadji@tums.ac.ir
2
Department of Pharmacognosy, Faculty of Pharmacy and Medicinal Plant Research Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Narguess
Yassa
yasa@sina.tums.ac.ir
3
Department of Pharmacognosy, Faculty of Pharmacy and Medicinal Plant Research Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Mahnaz
Khanavi
4
Department of Pharmacognosy, Faculty of Pharmacy and Medicinal Plant Research Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Zahra
Tofighi
ztofighi@tums.ac.ir
5
Department of Pharmacognosy, Faculty of Pharmacy and Medicinal Plant Research Center, Tehran University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
1. Bazargani YT, Almasirad A, Amin G, Shafiee A. Chemical composition of the essential oils of Astrodaucus persicus (Boiss.) Drude root, stem/leaves and flowers/fruits. Flavour Fragr J 2006; 21:294-296.
1
2. Nazemiyeh H, Razavi SM, Delazar A, Asnaashari S, Khoi NS, Daniali S, et al. Distribution Profile of Volatile Constituents in Different Parts of Astrodaucus orientalis (L.) Drude. Rec Nat Prod 2009; 3:126-130.
2
3. Yildirim E, Dursun A, Turan M. Determination of the Nutrition Contents of the Wild Plants Used as Vegetables in Upper Coruh Valley. Turk J Bot 2001; 25:367-371.
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4. Bigdeli M, Rustaiyan A, Ameri N, Masoudi Sh. Essential Oil of Astrodaucus persicus (Boiss.) Drude. from Iran. J Essent Oil Res 2014; 16:420-421.
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5. Omidbaigi R, Bastan MR, Omidbaigi MA. Essential oil content and chemical composition of Astrodaucus persicus Boiss cultivated in Iran. J Essent Oil Bear Pl 2005; 8:334-336.
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6. Mirza M, Baher Nik Z, Dini M. Chemical composition of the essential oils of Astrodaucus orientalis (L.) Drude leaves and seeds. Flavour Fragr J 2003; 18:205–206.
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7. Mazloomifar H, Bigdeli M, Saber-Tehrani M, Rustaiyan A, Masoudi Sh. Essential oil of Astrodaucus orientalis (L.) Drude. J Essential Oil Res 2013; 15:254-256.
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8. Abdolmohammadi MH, Fouladdel Sh, Shafiee A, Amin Gh, Ghaffari SM, Azizi E. Anticancer effects and cell cycle analysis on human breast cancer T47D cells treated with extracts of Astrodaucus persicus (Boiss.) Drude in comparison to doxorubicin. Daru 2008; 16:112-118.
8
9. Azizi E, Abdolmohammadi MH, Fouladdel Sh, Shafiee A, Amin Gh, Ghaffari SM. Evaluation of p53 and Bcl-2 genes and proteins expression in human breast cancer T47D cells treated with extracts of Astrodaucus persicus (Boiss.) Drude in comparison to Tamoxifen, Immunocytochemistry. Daru 2009; 17:181-186.
9
10. Abdolmohammadi MH, Fouladdel S, Shafiee A, Amin G, Ghaffari SM, Azizi E. Antiproliferative and apoptotic effect of Astrodaucus orientalis (L.) drude on T47D human breast cancer cell line: Potential mechanisms of action. Afr J Biotechnol 2009; 8:4265-4276.
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11. Razavi SM, Imanzadeh G, Dolati S, Nejad-Ebrahimi S, Majrouhi AA, Zahri S, et al. Phytochemical prospection and biological activity of Astrodaucus orientalis (L.) Drude growing wild in Iran. Pharmacologia 2011; 2:299-303.
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12. Soltani J, Aliabadi A. Antibacterial effects of several plant extracts and essential oils on Xanthomonas arboricola pv. juglandis in vitro. J Essent Oil Bear Plant 2013; 16:461-468.
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13. Adams RP. Identification of essential oil components by gas chromatography/ quadrupole mass spectroscopy. Allured Publishing Co. Carol Stream Illinois USA: 2001.
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14. Massada Y. Analysis of essential oil by gas chromatography and spectrometry. Wiley, New York, USA: 1976.
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15. Yassa N, Razavi Bani H, Hadjiakhoondi A. Free radical scavenging and lipid peroxidation activity of Shahany black grape. Pak J Biol Sci 2008; 11:1-4.
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17. Jafari S, Moradi A, Salaritabar A, Hadjiakhoondi A, Khanavi M. Determination of total phenolic and flavonoid contents of Leonurus cardiaca L. in compare with antioxidant activity. Res J Biol Sci 2010; 5:484-487.
17
18. Noghogne LR, Gatsing1 D, Fotso, Kodjio N Sokoudjou JB, Kuiate JR. In vitro antisalmonellal and antioxidant properties of Mangifera indica L. stem bark crude extracts and fractions. Br J Pharm Res 2015; 5:29-41.
18
19. Plattner PLA, Magyar G. Zur Kenntnis der Sesquiterpene. Abbau des Dihydroguajols mit Chromsäure. Bereitung des 1,4,7-Trimethyl-azulens. Helv chim Acta 1942; 25:581-589.
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20. Beadle GW, Brauns FE, Deulofeu V, Doudoroff M, Fox DL, Geiger E, et al. Progress in the Chemistry of Organic Natural Products. Springer-Verlag, Vienna Austria: 1948.
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21. Coruh N, Sagdioglu Celep AG, Ozgokce F. Antioxidant properties of Prangos ferulacea (L.) Lindl., Chaerophyllum macropodum Boiss. and Heracleum persicum Desf. from Apiaceae family used as food in eastern Anatolia and their inhibitory effects on glutathione-s-transferase. Food Chem 2007; 100:1237-1242.
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22. Plazonic A, Mornar A, Males Z, Kujundzic N. Phenolic content and antioxidant activities of Burr Parsley (Caucalis platycarpos L.). Molecules 2013; 18:8666-8681.
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23. Saeed N, Khan MR, Shabbir M. Antioxidant activity, total phenolic and total flavonoid contents of whole plant extracts Torilis leptophylla L. BMC Complement Alt Med 2012; 12:221-233.
23
24. Cadiz-Gurrea M, Fernandez-Arroyo S, Joven J, Segura-Carretero A. Comprehensive characterization by UHPLC-ESI-Q-TOF-MS from an Eryngium bourgatii extract and their antioxidant and anti-inflammatory activities. Food Res Int 2013; 50:197-204.
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25. Surveswaran S, Cai YZ, Corke H, Sun M. Systematic evaluation of natural phenolic antioxidants from 133 Indian medicinal plants. Food Chem 2007; 102:938-953.
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26. Rebey IB, Zakhama N, Karoui IJ, Marzouk B. Polyphenol composition and antioxidant activity of Cumin (Cuminum Cyminum L.) seed extract under drought. J Food Sci 2012; 77:734-739.
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27. Maulidiani, Abas F, Khatib A, Shaari K, Lajis NH. Chemical characterization and antioxidant activity of three medicinal Apiaceae species. Ind Crops Prod 2014; 55:238-247.
27
ORIGINAL_ARTICLE
Effect of coating thickness of iron oxide nanoparticles on their relaxivity in the MRI
Objective(s):Iron oxide nanoparticles have found prevalent applications in various fields including drug delivery, cell separation and as contrast agents. Super paramagnetic iron oxide (SPIO) nanoparticles allow researchers and clinicians to enhance the tissue contrast of an area of interest by increasing the relaxation rate of water. In this study, we evaluate the dependency of hydrodynamic size of iron oxide nanoparticles coated with Polyethylene glycol (PEG) on their relativities with 3 Tesla clinical MRI. Materials and Methods: We used three groups of nanoparticles with nominal sizes 20, 50 and 100 nm with a core size of 8.86 nm, 8.69 nm and 10.4 nm that they were covered with PEG 300 and 600 Da. A clinical magnetic resonance scanner determines the T1 and T2 relaxation times for various concentrations of PEG-coated nanoparticles. Results: The size measurement by photon correlation spectroscopy showed the hydrodynamic sizes of MNPs with nominal 20, 50 and 100 nm with 70, 82 and 116 nm for particles with PEG 600 coating and 74, 93 and 100 nm for particles with PEG 300 coating, respectively. We foud that the relaxivity decreased with increasing overall particle size (via coating thickness). Magnetic resonance imaging showed that by increasing the size of the nanoparticles, r2/r1 increases linearly. Conclusion: According to the data obtained from this study it can be concluded that increments in coating thickness have more influence on relaxivities compared to the changes in core size of magnetic nanoparticles.
https://ijbms.mums.ac.ir/article_6540_42ab0689da4b798d9a9c6fbe4044d9bb.pdf
2016-02-01
166
171
10.22038/ijbms.2016.6540
Coating thickness Hydrodynamic size
Nanoparticles
Relaxivity
Farzaneh
Hajesmaeelzadeh
farzane.910814@gmail.com
1
Biomolecular Imaging Analysis Group, Research Center for Molecular and Cellular Imaging, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Saeed
Shanehsazzadeh
2
Radiation Application Research School, Nuclear Science and Technology Research Institute, Tehran, Iran
AUTHOR
Cordula
Grüttner
gruettner@micromod.de
3
Micromod Partikeltechnologie GmbH, Friedrich-Barnewitz-Str. 4, D-18119 Rostock, Germany
AUTHOR
Fariba
Johari Daha
fjohari@aeoi.org.ir
4
Radiation Application Research School, Nuclear Science and Technology Research Institute, Tehran, Iran
AUTHOR
Mohammad Ali
Oghabian
maoghabian@gmail.com
5
Biomolecular Imaging Analysis Group, Research Center for Molecular and Cellular Imaging, Tehran University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
1. Gamarra L, Pontuschka WM, Amaro E, Costa-Filho A, Brito G, Vieira E, et al. Kinetics of elimination and distribution in blood and liver of biocompatible ferrofluids based on Fe 3 O 4 nanoparticles: An EPR and XRF study. Mater Sci Eng C 2008;28:519-25.
1
2. Shanehsazzadeh S, Gruettner C, Lahooti A, Mahmoudi M, Allen BJ, Ghavami M, et al. Monoclonal antibody conjugated magnetic nanoparticles could target MUC‐1‐positive cells in vitro but not in vivo. Contrast Media Mol Imaging 2015; 10:225–36.
2
3. Zhao X, Zhao H, Chen Z, Lan M. Ultrasmall superparamagnetic iron oxide nanoparticles for magnetic resonance imaging contrast agent. J Nanosci Nanotechnol 2014; 14:210-20.
3
4. Shanehsazzadeh S, Oghabian MA, Allen BJ, Amanlou M, Masoudi A, Daha FJ. Evaluating the effect of ultrasmall superparamagnetic iron oxide nanoparticles for a long-term magnetic cell labeling. J Med Phys 2013; 38:34.
4
5. Shanehsazzadeh S, Oghabian MA, Lahooti A, Abdollahi M, Haeri SA, Amanlou M, et al. Estimated background doses of [67Ga]-DTPA-USPIO in normal Balb/c mice as a potential therapeutic agent for liver and spleen cancers. Nucl Med Commun 2013; 34:915-25.
5
6. Mahmoudi M, Sant S, Wang B, Laurent S, Sen T. Superparamagnetic iron oxide nanoparticles (SPIONs): development, surface modification and applications in chemotherapy. Adv Drug Deliv Rev 2011; 63:24-46.
6
7. Bagheri-abassi F, Alavi H, Mohammadipour A, Motejaded F. Ebrahimzadeh-bideskan, A., The effect of silver nanoparticles on apoptosis and dark neuron production in rat hippocampus. Iran J Basic Med Sci 2015,18, 644-648.
7
8. Mayelifar K, Taheri AR, Rajabi O, Sazgarnia A. Ultraviolet B efficacy in improving antileishmanial effects of silver nanoparticles. Iran J Basic Med Sci 2015, 18, 677-683.
8
9. Lind K, Kresse M, Debus NP, Müller RH. A novel formulation for superparamagnetic iron oxide (SPIO) particles enhancing MR lymphography: comparison of physicochemical properties and the in vivo behaviour. J Drug Target 2002;10:221-30.
9
10. Mahmoudi M, Simchi A, Imani M, Hafeli UO. Superparamagnetic iron oxide nanoparticles with rigid cross-linked polyethylene glycol fumarate coating for application in imaging and drug delivery. J Phys Chem C 2009; 113:8124-31.
10
11. Harris JM, Chess RB. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov 2003; 2:214-21.
11
12. Moghimi SM, Hunter AC, Murray JC. Long-circulating and target-specific nanoparticles: theory to practice. Pharmacol Rev 2001;53:283-318.
12
13. Carroll MC. The complement system in regulation of adaptive immunity. Nat Immunol 2004;5:981-6.
13
14. Ni F, Jiang L, Yang R, Chen Z, Qi X, Wang J. Effects of PEG length and iron oxide nanoparticles size on reduced protein adsorption and non-specific uptake by macrophage cells. J Nanosci Nanotechnol 2012;12:2094-100.
14
15. Ahmad T, Bae H, Rhee I, Chang Y, Lee J, Hong S. Particle size dependence of relaxivity for silica-coated iron oxide nanoparticles. Curr Appl Phys 2012;12:969-74.
15
16. Wang C, Chen J, Talavage T, Irudayaraj J. Gold Nanorod/Fe3O4 Nanoparticle “Nano‐Pearl‐Necklaces” for Simultaneous Targeting, Dual‐Mode Imaging, and Photothermal Ablation of Cancer Cells. Angew Chem 2009;121:2797-801.
16
17. LaConte LE, Nitin N, Zurkiya O, Caruntu D, O'Connor CJ, Hu X, et al. Coating thickness of magnetic iron oxide nanoparticles affects R2 relaxivity. J Magn Reson Imaging 2007;26:1634-41.
17
18. Tromsdorf UI, Bigall NC, Kaul MG, Bruns OT, Nikolic MS, Mollwitz B, et al. Size and surface effects on the MRI relaxivity of manganese ferrite nanoparticle contrast agents. Nano Lett 2007;7:2422-7.
18
19. Duan H, Kuang M, Wang X, Wang YA, Mao H, Nie S. Reexamining the effects of particle size and surface chemistry on the magnetic properties of iron oxide nanocrystals: new insights into spin disorder and proton relaxivity. J Phys Chem C 2008;112:8127-31.
19
20. Thanh NT. Magnetic nanoparticles: from fabrication to clinical applications: CRC press; 2012.
20
21. Khameneh B, Halimi V, Jaafari MR, Golmohammadzadeh S. Safranal-loaded solid lipid nanoparticles: evaluation of sunscreen and moisturizing potential for topical applications. Iran J Basic Med Sci 2015;18:58-63.
21
22. Lahooti A, Shanehsazzadeh S, Oghabian M A, Allen BJ. In Assessment of human effective absorbed dose of Tc-99m-USPIO based on biodistribution rat data. J Label Compd Rad 2013; S258-S258.
22
23. Jahanbakhsh R, Atyabi F, Shanehsazzadeh S, Sobhani Z, Adeli M, Dinarvand R. Modified Gadonanotubes as a promising novel MRI contrasting agent. Daru 2013;21:53-61.
23
24. Omid H, Oghabian MA, Ahmadi R, Shahbazi N, Hosseini HRM, Shanehsazzadeh S, et al. Synthesizing and staining manganese oxide nanoparticles for cytotoxicity and cellular uptake investigation. BBA-Gen Subjects 2014;1840:428-33.
24
25. Müller-Bierl B, Louis O, Fierens Y, Buls N, Luypaert R, de Mey J. Cylinders or walls? A new computational model to estimate the MR transverse relaxation rate dependence on trabecular bone architecture. Magn Reson Mater Phys Biol Med 2014;27:349-61.
25
26. Galassi F, Brujic D, Rea M, Lambert N, Desouza N, Ristic M. Fast and accurate localization of multiple RF markers for tracking in MRI-guided interventions. Magn Reson Mater Phys Biol Med 2015;28:33-48.
26
27. Marshall I, Jansen MA, Tao Y, Merrifield GD, Gray GA. Application of kt-BLAST acceleration to reduce cardiac MR imaging time in healthy and infarcted mice. Magn Reson Mater Phys Biol Med 2014;27:201-10.
27
28. Wang Y-XJ, Hussain SM, Krestin GP. Superparamagnetic iron oxide contrast agents: physicochemical characteristics and applications in MR imaging. Eur Radiol 2001;11:2319-31.
28
ORIGINAL_ARTICLE
Mucosal acidification increases hydrogen sulfide release through up-regulating gene and protein expressions of cystathionine gamma-lyase in the rat gastric mucosa
Objective(s): This study was performed to investigate the effects of mucosal acidification on mRNA expression and protein synthesis of cystathionine gamma lyase (CSE), cystathionine beta synthase (CBS), and mucosal release of H2S in gastric mucosa in rats.
Materials and Methods:Thirty-two rats were randomly assigned into 4 groups (8 in each), including: the control group, HCl (10 mM) treated group, HCl (100 mM) treated group, and one group to study the effect of Nω-Nitro-L-arginine methyl ester hydrochloride (L-NAME). Anesthetized rats underwent tracheostomy and midline laparotomy. Ninety min after the instillation of neutral or acidic solutions, animals were sacrificed and the gastric mucosa was collected to measure the H2S concentration by ELISA method and to quantify mRNA expression of CSE and CBS by quantitative real-time PCR (qRT-PCR). Protein synthesis was also detected by Western blot method.
Results:Mucosal acidification with 10 and 100 HCl, significantly increased mucosal levels of H2S (P<0.01 and P<0.001) and mRNA (P<0.01 and P<0.001) and protein expressions of CSE (P<0.01 and P<0.001). L-NAME treatment reversed H2S release to control level.
Conclusion:Our findings indicated that mucosal acidification with HCl increased mucosal release of H2S through upregulation of CSE gene and its protein expression. This effect is mainly mediated through the involvement of nitric oxide.
https://ijbms.mums.ac.ir/article_6541_b4126fd277fc89ec29878a38469156b7.pdf
2016-02-01
172
177
10.22038/ijbms.2016.6541
Cystathionine gamma lyase H2S
Mucosal acidification
Rat
Seyyed Ali
Mard
alimard77@gmail.com
1
Physiology Research Center, Research Center for Infectious Diseases of Digestive System, Department of Physiology, School of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
LEAD_AUTHOR
Ali
Veisi
ali_veisi1556@yahoo.com
2
Physiology Research Center, Department of Physiology, School of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
AUTHOR
Akram
Ahangarpour
mard-sa@ajums.ac.ir
3
Physiology Research Center, Department of Physiology, School of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
AUTHOR
Mohammad Kazem
Gharib-Naseri
4
Physiology Research Center, Department of Physiology, School of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
AUTHOR
Farrugia G, Szurszewski JH. Carbon monoxide, hydrogen sulfide, and nitric oxide as signaling molecules in the gastrointestinal tract. Gastroenterology 2014; 147:303-313.
1
2. Wallace JL. Hydrogen sulfide: a rescue molecule for mucosal defence and repair. Dig Dis Sci 2012; 57:1432-1434.
2
3. Magierowski M, Magierowska K, Kwiecien S, Brzozowski T. Gaseous mediators nitric oxide and-hydrogen sulfide inthe mechanism of gastrointestinal integrity, protection and ulcer healing. Molecules 2015; 20:9099-9123.
3
4. Ise F, Takasuka H, Hayashi S, Takahashi K, Koyama M, Aihara E, et al. Stimulation of duodenal HCO3− secretion by hydrogen sulphide in rats: Relation to prostaglandins, nitric oxide and sensory neurones. Acta Physiol 2011; 201:117-126.
4
5. Magierowski M, Jasnos K, Kwiecień S, Brzozowski T. [Role of hydrogen sulfide in the physiology of gastrointestinal tract and in the mechanism of gastroprotection]. Postepy Hig Med Dosw (Online) 2012; 67:150-156.
5
6. Mard SA, Askari H, Neisi N, Veisi A. Antisecretory effect of hydrogen sulfide on gastric acid secretion and the involvement of nitric oxide. Biomed Res Int 2014; 2014:480921.
6
7. Yonezawa D, Sekiguchi F, Miyamoto M, Taniguchi E, Honjo M, Masuko T, et al. A protective role of hydrogen sulfide against oxidative stress in rat gastric mucosal epithelium. Toxicology 2007; 241:11-18.
7
8. Mard SA, Neisi N, Solgi G, Hassanpour M, Darbor M, Maleki M. Gastroprotective effect of NaHS against mucosal lesions induced by ischemia–reperfusion injury in rat. Dig Dis Sci 2012; 57:1496-1503.
8
9. Medeiros JV, Bezerra VH, Gomes AS, Barbosa AL, Lima-Júnior RC, Soares PM, et al. Hydrogen sulfide prevents ethanol-induced gastric damage in mice: role of ATP-sensitive potassium channels and capsaicin-sensitive primary afferent neurons. J Pharmacol Exp Ther 2009; 330:764-770.
9
10. Fiorucci S, Antonelli E, Distrutti E, Rizzo G, Mencarelli A, Orlandi S, et al. Inhibition of hydrogen sulfide generation contributes to gastric injury caused by anti-inflammatory nonsteroidal drugs. Gastroenterology 2005; 129:1210-1224.
10
11. Lou LX, Geng B, Du JB, Tang CS. Hydrogen sulphide-induced hypothermia attenuates stress-related ulceration in rats. Clin Exp Pharmacol Physiol 2008; 35:223-228.
11
12. Takeuchi K, Aihara E, Kimura M, Dogishi K, Hara T, Hayashi S. Gas mediators involved in modulating duodenal HCO3-secretion. Cur Med Chem 2012; 19:43-54.
12
13. Takeuchi K, Ise F, Takahashi K, Aihara E, Hayashi S. H2S-induced HCO3 (-) secretion in the rat stomach-Involvement of nitric oxide, prostaglandins, and capsaicin-sensitive sensory neurons. Nitric Oxide 2015 30; 46:157-64
13
14. Mard SA, Veisi A, Ahangarpour A, Gharib-Naseri MK. Gastric acid induces mucosal H2S release in rats by upregulating mRNA and protein expression of cystathionine gamma lyase. J Physiol Sci 2015; 65:545-554.
14
15. Medeiros JV, Soares PM, Castro Brito GA, Souza MH. Immunohistochemical approach reveals localization of cystathionine-gamma-lyase and cystathionine-beta-synthetase in ethanol-induced gastric mucosa damage in mice. Arq Gastroenterol 2013; 50:157-160.
15
16. Tarnawski A, Hollander D, Stachura J, Krause WJ, Gergely H. Prostaglandin protection of the gastric mucosa against alcohol injury—a dynamic time-related process: role of the mucosal proliferative zone. Gastroenterology 1985; 88:334–352.
16
ORIGINAL_ARTICLE
The role of ISCOMATRIX bilayer composition to induce a cell mediated immunity and protection against leishmaniasis in BALB/c mice
Objective(s):Development of new generation of vaccines against leishmaniasis is possible because long-term protection is usually seen after recovery from cutaneous leishmaniasis. ISCOMATRIX is particulate antigen delivery system composed of antigen, cholesterol, phospholipid and saponin. In this study, the role of ISCOMATRIX bilayer composition made by different phase transition temperature (Tc) to induce a type of immune response and protection against leishmaniasis was assessed.
Materials and Methods:ISCOMATRIX formulations with different bilayer compositions consisting of EPC (Tc <0 ◦C), DMPC (Tc 23 ◦C) and DSPC (Tc 54 ◦C) were prepared. Different ISCOMATRIX formulations were mixed with soluble Leishmania antigens (SLA). BALB/c mice were immunized subcutaneously, three times with 2-week intervals. As criteria for protection, footpads swelling, parasite burden, determination of IgG isotypes and the level of IFN-γ and IL-4 were assessed.
Results: Although the groups of mice immunized with ISCOMATRIX DMPC or ISCOMATRIX DSPC showed the smallest footpad swelling and least parasite burden compared with the buffer group, the difference was not significant. Moreover, the highest level of IFN- γ and IL-4 was observed in the splenocytes of mice immunized with ISCOMATRIX DMPC or ISCOMATRIX DSPC, respectively. After challenge, the mice immunized with ISCOMATRIX DSPC showed the highest elevation of IgG, IgG1 and IgG2a antibodies (P<0.01) compared with control group. However, our results indicated that ISCOMATRIX EPC, DMPC or DSPC generated a mixed Th1/Th2 response that was not protective.
Conclusion: Our results showed that the adjuvanticity of prepared ISCOMATRIX doesn’t influence with different phospholipids at least in our mice model.
https://ijbms.mums.ac.ir/article_6542_1dd12b3e8774326a110ea15e2e6af91b.pdf
2016-02-01
178
186
10.22038/ijbms.2016.6542
Immune response
ISCOMATRIX
Leishmania major
Transition temperature
Ahmad
Mehravaran
ahmadmehravaran55@gmail.com
1
Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Mahmoud Reza
Jaafari
jafarimr@mums.ac.ir
2
Biotechnology Research Center, Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Seyed Amir
Jalali
jalalia@sbmu.ac.ir
3
Immunology Department, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
Ali
Khamesipour
4
Center for Research and Training in Skin Diseases and Leprosy, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Reza
Ranjbar
dabir120@yahoo.com
5
Molecular Biology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Mansure
Hojatizade
6
Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Ali
Badiee
badieea@mums.ac.ir
7
Nanotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
LEAD_AUTHOR
1. World Health Organization. Control of the leishmaniases. World Health Organ. Tech Rep Ser 2010; 1- 186.
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2. World Health Organization. Control of the Leishmaniases. Report of a WHO expert committee. Technical report series 1990; No. 793.
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3. Alvar J, Croft S, Kaye P, Khamesipour A, Sundar S, Reed SG. Case study for a vaccine against leishmaniasis.Vaccine 2013; 31: 244-249.
3
4. Thakur CP, Kumar K. Post Kala-azar dermal leishmaniasis: a neglected aspect of kala-azar control programmes. Ann Trop Med Parasitol 1992; 86:355-359.
4
5. Bryceson A. A policy for leishmaniasis with respect to the prevention and control of drug resistance. Trop Med Int Health 2001; 6:928–934.
5
6. Croft SL, Coombs GH. Leishmaniasis current chemotherapy and recent advances in the search for novel drugs. Trends Parasitol 2003; 19:502–508.
6
7. Hadighi R, Mohebali M, Boucher P, Hajjaran H, Khamesipour A, Ouellette M. Unresponsiveness to glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites. Plos Med 2006; 3:659–667.
7
8. Sacks D, Noben-Trauth N. The immunology of susceptibility and resistance to Leishmania major in mice. Nat Rev Immunol 2002; 2:845–858.
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9. Grencis RK. Th2-mediated host protective immunity to intestinal nematode infections. Philos Trans R Soc Lond B Biol Sci.1997; 352:1377–1384.
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10. Modabber F. Vaccines against leishmaniasis. Ann Trop Med Parasitol 1995; 89: 83–88.
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11. Khamesipour A, Dowlati Y, Asilian A, Hashemi-Fesharki R, Javadi A, Noazin S, et al. Leishmanization: use of an old method for evaluation of candidate vaccines against leishmaniasis. Vaccine 2005; 23: 3642–3648.
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12. Modabber F, Coler R, Reed SG. Vaccines against Leishmania. In: Modabber, F. (Ed.), New Generation Vaccines. E-Publishing Inc, New York 2009; 273–283.
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13. Mutiso JM, Macharia JC, Mutisya RM, Taracha E. Subcutaneous immunization against Leishmania major infection in mice. Efficacy of formalin-killed promastigotes combined with adjuvants. Rev. Inst. Med. Trop. Sao Paulo 2012; 52: 95–100.
13
14. Copland MJ, Rades T, Davies NM, Baird MA. Lipid based particulate formulations for the delivery of antigen. Immunol Cell Bio 2005; 83:97–105.
14
15. Badiee A, Heravi SV, Khamesipour A, Jaafari MR. Micro/nanoparticle adjuvants for anti leishmanial vaccines: present and future trends. Vaccine 2013; 31: 735-749.
15
16. Hong-Xiang S, Yong X, Yi-Ping Y. ISCOMs and ISCOMATRIX TM . Vaccine 2009; 27: 4388–4401.
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17. Rimmelzwaan GF, Osterhaus ADME. A novel generation of viral vaccines based on ISCOM matrix. In Vaccine Design, the Subunit and Adjuvant Approach (M. F. Powell and M. J. Newman, eds.), New York: Plenum 1995; 543–558.
17
18. Lövgren K, Morein B, Osterhaus A. ISCOM technology-based Matrix M™ adjuvant: success in future vaccines relies on formulation. Expert Rev Vaccines 2011; 10: 401-403.
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19. Sanders MT, Brown LE, Deliyannis G, Pearse MJ. ISCOM-based vaccines: the Second decade. Immunol Cell Biol 2005; 83:119–128.
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20. Sjölander A, Drane D, Maraskovsky E, Scheerlinck JP, Suhrbier A, Tennent A, et al. Immune responses to ISCOM formulations in animal and primate models. Vaccine 2001; 19:2661–2665.
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21. Barr IG, Sjolander A, Cox JC. ISCOMs and other saponin based adjuvants. Adv Drug Del Rev 1998; 32: 247-271.
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22. Sjolander A, Cox JC, Barr IG. ISCOMs: an adjuvant with multiple functions. J leukoc Biol 1998; 64:713-723.
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23. Cox JC. Drane D, Suhrbier A. Immunogenic complex and methods relating thereto 2000; PCT/AU00/00110.
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24. Behboudi S, Morein B, Vilacres-Eriksson M. In vitro activation of antigen-presenting cells (APC) by defined composition of Quillaja saponaria Molina triterpenoids. Clin Exp Immunol 1996; 105:26-30.
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25. Khamesipour A, Rafati S, Davoudi N, Maboudi F, Modabber F. Leishmaniasis vaccine candidates for development: a global overview. IJMR 2006; 123: 423–438.
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34. Golali E, Jaafari MR, Khamesipour A, Abbasi A, Saberi Z, Badiee A. Comparison of in vivo Adjuvanticity of Liposomal PO CpG ODN with Liposomal PS CpG ODN: Soluble Leishmania Antigens as a Model. Iran J Basic Med Sci 2012; 15:1032-1045.
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44
ORIGINAL_ARTICLE
Down-regulation of HSP40 gene family following OCT4B1 suppression in human tumor cell lines
Objective(s): The OCT4B1, as one of OCT4 variants, is expressed in cancer cell lines and tissues more than other variants and plays an important role in apoptosis and stress (heat shock protein) pathways. The present study was designed to determine the effects of OCT4B1 silencing on expressional profile of HSP40 gene family expression in three different human tumor cell lines. Materials and Methods: The OCT4B1 expression was suppressed by specific siRNA transfection in AGS (gastric adenocarcinoma), 5637 (bladder tumor) and U-87MG (brain tumor) cell lines employing Lipofectamine reagent. Real-time PCR array technique was employed for RNA qualification. The fold changes were calculated using RT2 Profiler PCR array data analysis software version 3.5. Results: Our results indicated that fifteen genes (from 36 studied genes) were down-regulated and two genes (DNAJC11 and DNAJC5B) were up-regulated in all three studied tumor cell lines by approximately more than two folds. The result of other studied genes (19 genes) showed different expressional pattern (up or down-expression) based on tumor cell lines. Conclusion: According to the findings of the present study, we may suggest that there is a direct correlation between OCT4B1 expression in tumor cell lines (and tissues) and HSP40 family gene expressions to escape from apoptosis and cancer expansion.
https://ijbms.mums.ac.ir/article_6543_ac3bb0f4091f6e48a1cc65e0a416562e.pdf
2016-02-01
187
193
10.22038/ijbms.2016.6543
HSP40 gene family
OCT4B1
siRNA
Tumor cell lines
Mohammad Reza
Mirzaei
mirzaeemr@gmail.com
1
Molecular Medicine Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
LEAD_AUTHOR
MalekHosein
Asadi
2
Departments of Biotechnology, Institute of Science and High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran
AUTHOR
Seyed Javad
Mowla
s_ mowla@gmail.com
3
Departments of Molecular Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
AUTHOR
Gholamhossin
Hassanshahi
4
Molecular Medicine Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Zahra
Ahmadi
zahra.ahmadi83@yahoo.com
5
Molecular Medicine Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
1. Sanchez Y, Parsell DA, Taulien J, Vogel JL, Craig EA, Lindquist S. Genetic evidence for a functional relationship between Hsp104 and Hsp70. J Bacteriol 1993; 175:6484-6491.
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2. Parcellier A, Gurbuxani S, Schmitt E, Solary E, Garrido C. Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways. Biochem Biophys Res Commun 2003; 304:505-512.
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3
4. Alexiou GA, Vartholomatos G, Stefanaki K, Patereli A, Dova L, Karamoutsios A, et al. Expression of heat shock proteins in medulloblastoma. J Neurosurg Pediatr 2013; 12:452-457.
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5. Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J Leukoc Biol 2007; 81:15-27.
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6. Lanneau D, Brunet M, Frisan E, Solary E, Fontenay M, Garrido C. Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med 2008; 12:743-761.
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13. Scholer HR, Ruppert S, Suzuki N, Chowdhury K, Gruss P. New type of POU domain in germ line-specific protein Oct-4. Nature 1990; 344:435-439.
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14. Lee J, Kim HK, Rho JY, Han YM, Kim J. The human OCT-4 isoforms differ in their ability to confer self-renewal. J Biol Chemi 2006; 281:33554-3365.
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15. Prud'homme GJ. Cancer stem cells and novel targets for antitumor strategies. Curr Pharm Des 2012; 18:2838-2849.
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16. Yasuda H, Tanaka K, Okita Y, Araki T, Saigusa S, Toiyama Y, et al. CD133, OCT4, and NANOG in ulcerative colitis-associated colorectal cancer. Oncol Lett 2011; 2:1065-1071.
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17. Ricci MS, Zong WX. Chemotherapeutic approaches for targeting cell death pathways. Oncologist 2006; 11:342-357.
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18. Gao Y, Wang X, Han J, Xiao Z, Chen B, Su G, et al. The novel OCT4 spliced variant OCT4B1 can generate three protein isoforms by alternative splicing into OCT4B. J Genet Genomics 2010; 37:461-465.
18
19. Cheng L, Sung MT, Cossu-Rocca P, Jones TD, MacLennan GT, De Jong J, et al. OCT4: biological functions and clinical applications as a marker of germ cell neoplasia. J Pathol 2007; 211:1-9.
19
20. Rijlaarsdam MA, van Herk HA, Gillis AJ, Stoop H, Jenster G, Martens J, et al. Specific detection of OCT3/4 isoform A/B/B1 expression in solid (germ cell) tumours and cell lines: confirmation of OCT3/4 specificity for germ cell tumours. Br J Cancer 2011; 105:854-863.
20
21. Atlasi Y, Mowla SJ, Ziaee SA, Gokhale PJ, Andrews PW. OCT4 spliced variants are differentially expressed in human pluripotent and nonpluripotent cells. Stem Cells 2008; 26:3068-3074.
21
22. Asadi MH, Mowla SJ, Fathi F, Aleyasin A, Asadzadeh J, Atlasi Y. OCT4B1, a novel spliced variant of OCT4, is highly expressed in gastric cancer and acts as an antiapoptotic factor. Int J Cancer 2011; 128:2645-2652.
22
23. Farashahi Yazd E, Rafiee MR, Soleimani M, Tavallaei M, Salmani MK, Mowla SJ. OCT4B1, a novel spliced variant of OCT4, generates a stable truncated protein with a potential role in stress response. Cancer Lett 2011; 309:170-175.
23
24. Mirzaei MR, Najafi A, Arababadi MK, Asadi MH, Mowla SJ. Altered expression of apoptotic genes in response to OCT4B1 suppression in human tumor cell lines. Tumour Biol 2014 ; 35:9999-10009.
24
25. Asadzadeh J, Asadi MH, Shakhssalim N, Rafiee MR, Kalhor HR, Tavallaei M, et al. A plausible anti-apoptotic role of up-regulated OCT4B1 in bladder tumors. Urol J 2012; 9:574-580.
25
26. Momeni M, Reza Mirzaei M, Zainodini N, Hassanshahi G, Arababadi MK. MiR-143 induces expression of AIM2 and ASC in jurkat cell line. Iran J Immunol 2013; 10:103-109.
26
27. Li D, Yang ZK, Bu JY, Xu CY, Sun H, Tang JB, et al. OCT4B modulates OCT4A expression as ceRNA in tumor cells. Oncol Rep 2015; 33:2622-2630.
27
28. Sterrenberg JN, Blatch GL, Edkins AL. Human DNAJ in cancer and stem cells. Cancer Lett 2011; 312:129-142.
28
29. He HL, Lee YE, Chen HP, Hsing CH, Chang IW, Shiue YL, et al. Overexpression of DNAJC12 predicts poor response to neoadjuvant concurrent chemoradiotherapy in patients with rectal cancer. Exp Mol Pathol 2015; 98:338-345.
29
30. Morita R, Nishizawa S, Torigoe T, Takahashi A, Tamura Y, Tsukahara T, et al. Heat shock protein DNAJB8 is a novel target for immunotherapy of colon cancer-initiating cells. Cancer Sci 2014; 105:389-395.
30
ORIGINAL_ARTICLE
Association of -77T>C and Arg194trp polymorphisms of XRCC1 with risk of coronary artery diseases in Iranian population
Objective(s): Coronary artery disease (CAD) is the leading cause of death in both male and female worldwide. The main cause of CAD is the atherosclerosis of coronary arteries, which is, mostly caused by genetic alteration. 50% of such cases occur in mitotic cells where single-strand breaks occur spontaneously or due to ionizing radiation. X-ray repair cross-complementing protein 1 (XRCC1) as a key element, participate in the base excision repair (BER) and Single-strand Break Repair (SSBR) pathways. It has been suggested that XRCC1 functions as a scaffold protein able to coordinate and facilitate the various steps of DNA repair pathways. Two Single Nucleotide Polymorphisms (SNPs) (Arg194Trp and -77T>C) were reported to affect the function and expression of XRCC1, respectively. Materials and Methods:A case-control study was performed to investigate the relation between these polymorphisms and the CAD development. A population of 406 individuals was screened for SNPs by Restriction Fragment Length Polymorphisms (RFLP) method. Results: XRCC1 Arg194Trp polymorphism was associated with increased risk of CAD in examined population under a dominant model (Odds-ratio=2.604, P-value=0.001). Also the SNP of -77T>C revealed a protective role in the population under a dominant model (Odds-ratio=0.618, P-value=0.032). Conclusion:Our findings demonstrated a contributory role of these two SNPs in CAD. Furthermore, our results support the role of DNA damages and the malfunctions of DNA repair system in cardiovascular disease development in Iranian patients.
https://ijbms.mums.ac.ir/article_6545_eb6cfa51b74b8d95e6c597282b8acb3c.pdf
2016-02-01
194
200
10.22038/ijbms.2016.6545
Atherosclerosis
CAD
DNA damage
DNA repair
Single nucleotide poly-morphism
X-ray repair cross comple-menting protein
Saghar
Pahlavanneshan
saghar.pahlavanneshan@yahoo.com
1
Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
AUTHOR
Amirhossein
Ahmadi
amirhossein_pharma@yahoo.com
2
Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
AUTHOR
Mohammadali
Boroumand
borumand@sina.tums.ac.ir
3
Tehran Heart Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Saeed
Sadeghian
ssdeghian@tums.ac.ir
4
Tehran Heart Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Mehrdad
Behmanesh
behmanesh@modares.ac.ir
5
Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
LEAD_AUTHOR
1. Weber C, Noels H. Atherosclerosis: current pathogenesis and therapeutic options. Nat Med 2011; 17: 1410-1422.
1
2. Grech ED. ABC of interventional cardiology: Pathophysiology and investigation of coronary artery disease. BMJ 2003; 326: 1027.
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3. Saade S,Cazier J-B,Ghassibe-Sabbagh M,Youhanna S,Badro D A,Kamatani Y, et al. Large scale association analysis identifies three susceptibility loci for coronary artery disease. PloS one 2011; 6: e29427.
3
4. Thaker AM, Frishman WH. Sortilin The Mechanistic Link Between Genes, Cholesterol, and Coronary Artery Disease. Cardiol Rev 2014; 22: 91-96.
4
5. Woestijne AP, Graaf Y, Bakker PI, Asselbergs FW, Borst GJ, Algra A, et al. LDL-c-linked SNPs are associated with LDL-c and myocardial infarction despite lipid-lowering therapy in patients with established vascular disease. Eur J Clin Invest 2014; 44: 184-191.
5
6. Martinelli N, Girelli D, Lunghi B, Pinotti M, Marchetti G, Malerba G, et al. Polymorphisms at LDLR locus may be associated with coronary artery disease through modulation of coagulation factor VIII activity and independently from lipid profile. Blood 2010; 116: 5688-5697.
6
7. Yoshino S, Cilluffo R, Best PJ, Atkinson EJ, Aoki T, Cunningham JM, et al. Single nucleotide polymorphisms associated with abnormal coronary microvascular function. Coron Artery Dis 2014; 25: 281-289.
7
8. Ziaee S, Kalayinia S, Boroumand MA, Pourgholi L, Cheraghi S, Anvari MS, et al. Association between the atrial natriuretic peptide rs5065 gene polymorphism and the presence and severity of coronary artery disease in an Iranian population. Coron Artery Dis 2014; 25: 242-246.
8
9. Guven M, Guven G S, Oz E, Ozaydin A, Batar B, Ulutin T, et al. DNA repair gene XRCC1 and XPD polymorphisms and their association with coronary artery disease risks and micronucleus frequency. Heart Vessels 2007; 22:355-360.
9
10. Mahmoudi M, Mercer J, Bennett M. DNA damage and repair in atherosclerosis. Cardiovasc Res 2006: 71: 259-68.
10
11. Gray K, Bennett M. Role of DNA damage in atherosclerosis--bystander or participant? Biochem Pharmacol 2011; 82: 693-700.
11
12. Botto N, Rizza A, Colombo M, Mazzone A, Manfredi S, Masetti S, et al. Evidence for DNA damage in patients with coronary artery disease. Mutat Res 2001 493: 23-30.
12
13. Cooke MS, Evans MD, Dizdaroglu M, Lunec J. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 2003; 17: 1195-1214.
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14. Mondal NK, Sorensen E, Hiivala N, Feller E, Griffith B, Wu ZJ. Oxidative stress, DNA damage and repair in heart failure patients after implantation of continuous flow left ventricular assist devices. Int J Med Sci 2013; 10: 883-893.
14
15. Martinet W, Knaapen MWM, De Meyer GRY, Herman AG, Kockx MM. Elevated Levels of Oxidative DNA Damage and DNA Repair Enzymes in Human Atherosclerotic Plaques. Circulation 2002; 106: 927-932.
15
16. Mohazzab K, Kaminski PM, Wolin MS. NADH oxidoreductase is a major source of superoxide anion in bovine coronary artery endothelium. Am J Physiol 1994; 266: H2568-H2572.
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17. Griendling KK, Minieri CA, Ollerenshaw JD, Alexander RW. Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ Res 1994; 74: 1141-1148.
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18. Williams GM, Jeffrey AM. Oxidative DNA damage: endogenous and chemically induced. Regul Toxicol Pharmacol 2000; 32: 283-292.
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19. Behmanesh m, Sakumi K, Abolhassani N, Toyokuni S., Oka S, Ohnishi YN, Tsuchimoto D, Nakabeppu Y. ITPase-deficient mice show growth retardation and die before weaning. Cell death Differ 2009; 16: 1315-1322.
19
20. Michalik V, Maurizot M, SCharlier M. Calculation of hydroxyl radical attack on different forms of DNA. J Biomol Struct Dyn 1994; 13: 565-575.
20
21. Ahmadi A, Behmanesh M, Boroumand MA, Tavallaei M. Up-regulation of MSH2, XRCC1 and ATM genes in patients with type 2 diabetes and coronary artery disease. Diabetes Res Clin Pract 2015; 109: 500-506.
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22. Wood RD, Mitchell M, Sgouros J, Lindahl T. Human DNA repair genes. Science 2001; 291: 1284-1299.
22
23. Nazarkina ZK, Khodyreva SN, Marsin S, Lavrik OI, Radicella JP. XRCC1 interactions with base excision repair DNA intermediates. DNA Repair 2007; 6: 254-264.
23
24. Brem R, Hall J. XRCC1 is required for DNA single-strand break repair in human cells. Nucleic Acids Res 2005; 33: 2512-2520.
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25. Tebbs RS, Flannery ML, Meneses JJ, Hartmann A, Tucker JD, Thompson LH, et al. Requirement for the Xrcc1 DNA Base Excision Repair Gene during Early Mouse Development. Dev Biol 1999; 208: 513-529.
25
26. Mohamadynejad P, Saadat M. Genetic polymorphisms of XRCC1 (at codons 194 and 399) in Shiraz population (Fars province, southern Iran). Mol Biol Rep 2008; 35: 669-672.
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27. Hao B, Miao X, Li Y, Zhang X, Sun T, Liang G, et al.A novel T-77C polymorphism in DNA repair gene XRCC1 contributes to diminished promoter activity and increased risk of non-small cell lung cancer. Oncogene 2006; 25: 3613-3620.
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28. Stephens M, Smith NJ, Donnelly P. A new statistical method for haplotype reconstruction from population data. Am J Hum Genet 2001; 68: 978-989.
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29. Stephens M, Scheet P. Accounting for decay of linkage disequilibrium in haplotype inference and missing-data imputation. Am J Hum Genet 2005; 76: 449-462.
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30. Andreassi M, Botto N, Colombo M, Biagini A, Clerico A. Genetic instability and atherosclerosis: can somatic mutations account for the development of cardiovascular diseases? Environ Mol Mutage 2000; 35: 265-269.
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31. Andreassi MG. Coronary atherosclerosis and somatic mutations: an overview of the contributive factors for oxidative DNA damage. Mutat Res 2003; 543: 67-86.
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32. Tousoulis D, Kampoli AM, Stefanadis C. Diabetes mellitus and vascular endothelial dysfunction: current perspectives. Curr Vas Pharmacol 2012; 10: 19-32.
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33. Paschalaki KE, Starke RD, Hu Y, Mercado N, Margariti A, Gorgoulis VG, et al. Dysfunction of endothelial progenitor cells from smokers and chronic obstructive pulmonary disease patients due to increased DNA damage and senescence. Stem Cells 2013; 31: 2813-2826.
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34. Kaya Y, Ari E, Demir H, Soylemez N, Cebi A, Alp H, et al. Accelerated atherosclerosis in haemodialysis patients; correlation of endothelial function with oxidative DNA damage. Nephrol Dial Transplant 2012; 27: 1164-1169.
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35. Morrell CN. Reactive oxygen species: finding the right balance. Circ Res 2008; 103: 571-572.
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36. Banerjee M,Vats P. Reactive metabolites and antioxidant gene polymorphisms in Type 2 diabetes mellitus. Redox Biol 2014; 2: 170-177.
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37. Thompson LH, West MG. XRCC1 keeps DNA from getting stranded. Mutat Res 2000; 459: 1-18.
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38. Audebert M, Salles B, Calsou P. Involvement of poly (ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. JBC 2004; 279: 55117-55126.
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39. Hu Z, Ma H, Chen F, Wei Q, Shen H. XRCC1 polymorphisms and cancer risk: a meta-analysis of 38 case-control studies. Cancer Epidemiol Biomarkers Prev 2005; 14: 1810-1818.
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40. Zhang Y, Wang Y, Wu J, Li LJ. XRCC1 Arg194Trp polymorphism is associated with oral cancer risk: evidence from a meta-analysis. Tumour Biol 2013; 34: 2321-2327.
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41. Fang Z, Chen F, Wang X, Yi S, Chen W, Ye G. XRCC1 Arg194Trp and Arg280His polymorphisms increase bladder cancer risk in asian population: evidence from a meta-analysis. PloS one 2013; 8: e64001.
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42. Ünal M, Güven M, Batar B, Özaydın A, Sarici A, Devranoğlu K. Polymorphisms of DNA repair genes XPD and XRCC1 and risk of cataract development. Exp Eye Res 2007; 85: 328-334.
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43. Ladiges W, Wiley J, MacAuley A. Polymorphisms in the DNA repair gene XRCC1 and age-related disease. Mech Ageing Dev 2003; 124: 27-32.
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44. Vodicka P, Stetina R, Polakova V, Tulupova E, Naccarati A, Vodickova L, et al. Association of DNA repair polymorphisms with DNA repair functional outcomes in healthy human subjects. Carcinogenesis 2007; 28: 657-664.
44
45. Bazo AP, Salvadori JrD, Salvadori RA, Sodré LP, da Silva GN, de Camargo EA, et al. DNA repair gene polymorphism is associated with the genetic basis of atherosclerotic coronary artery disease. Cardiovas Pathol 2011; 20: e9-e15.
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46. Yu X, Liu J, Zhu H, Xia Y, Gao L, Dong Y, et al. Synergistic association of DNA repair relevant gene polymorphisms with the risk of coronary artery disease in northeastern Han Chinese. Thromb Res 2014; 133: 229-234.
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47. Dvornyk V, Long JR, Xiong DH, Liu PY, Zhao LJ, Shen H, et al. Current limitations of SNP data from the public domain for studies of complex disorders: a test for ten candidate genes for obesity and osteoporosis. BMC genetics 2004; 5: 4.
47
48. Saber MM, Boroumand MA, Behmanesh M. Investigation of CYP2C19 allele and genotype frequencies in Iranian population using experimental and computational approaches. Thromb Res, 2014; 133:272-275.
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49. Huang G, Cai S, Wang W, Zhang Q, Liu A. Association between XRCC1 and XRCC3 Polymorphisms with Lung Cancer Risk: A Meta-Analysis from Case-Control Studies. PloS one 2013; 8: e68457.
49
50. Brem R, Cox DG, Chapot B, Moullan N, Romestaing P, Gerard JP, et al. The XRCC1− 77T→ C variant: haplotypes, breast cancer risk, response to radiotherapy and the cellular response to DNA damage. Carcinogenesis 2006; 27: 2469-2474.
50
ORIGINAL_ARTICLE
α-Terpineol attenuates morphine-induced physical dependence and tolerance in mice: role of nitric oxide
Objective(s):Dependence and tolerance to opioid analgesics are major problems limiting their clinical application. a-Terpineol is a monoterpenoid alcohol with neuroprotective effects which is found in several medicinal plants such as Myrtus communis, Laurus nobilis, and Stachys byzantina. It has been shown that some of these medicinal plants such as S. byzantina attenuate dependence and tolerance to morphine. Since a-terpineol is one of the bioactive phytochemical constituent of these medicinal plants, the present study was conducted to investigate the effects of a-terpineol on morphine-induced dependence and tolerance in mice. Materials and Methods: The mice were rendered dependent or tolerant to morphine by a 3-day administration schedule. The hot-plate test and naloxone-induced withdrawal syndrome were used to evaluate tolerance and dependence on morphine, respectively. To investigate a possible role for nitric oxide (NO) in the protective effect of a-terpineol, the NO synthase inhibitor, L-N(G)-nitroarginine methyl ester (L-NAME) and NO precursor, L-arginine, were used. Results: Administration of a-terpineol (5, 10, and 20 mg/kg, IP) significantly decreased the number of jumps in morphine dependent animals. Moreover, a-terpineol (20 and 40 mg/kg, IP) attenuated tolerance to the analgesic effect of morphine. The inhibitory effects of a-terpineol on morphine-induced dependence and tolerance were enhanced by pretreatment with L-NAME (10 mg/kg, IP). However, L-arginine (300 mg/kg, IP) antagonized the protective effects of a-terpineol on dependence and tolerance to morphine. Conclusion: These findings indicate that a-terpineol prevents the development of dependence and tolerance to morphine probably through the influence on NO production.
https://ijbms.mums.ac.ir/article_6546_64083fa7fd5e543f236a120c7aa694d0.pdf
2016-02-01
201
208
10.22038/ijbms.2016.6546
α-Terpineol
Dependence
Monoterpenoid
Morphine
Nitric oxide
Tolerance
Siavash
Parvardeh
parvardehs@sbmu.ac.ir
1
Department of Pharmacology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Mahsa
Moghimi
mahsa_764314@yahoo.com
2
Department of Pharmacology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
Pegah
Eslami
pegahslm@gmail.com
3
School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
Alireza
Masoudi
ar.masoudi90@sbmu.ac.ir
4
Department of Pharmacology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
AUTHOR
1. Alldredge BK, Corelli RL, Ernst ME, Guglielmo BJ, Jacobson PA, Kradjan WA, et al. Koda-Kimble and Young’s Applied Therapeutics: The Clinical Use of Drugs. 10th ed. Philadelphia: Lippincott Williams and Wilkins; 2013.
1
2. Tabatabai SM, Dashti S, Doosti F, Hosseinzadeh H. Phytotherapy of opioid dependence and withdrawal syndrome: a review. Phytother Res 2014; 28:811-830.
2
3. Shokraviyan M, Miladi-Gorji H, Vaezi GH. Voluntary and forced exercises prevent the development of tolerance to analgesic effects of morphine in rats. Iran J Basic Med Sci 2014;17:271-277.
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17. Salehi Surmaghi MH, Amin G, Shakibafar A, Azadi B. Unexpected volatile compounds of myrtus communis L. fruit rind growing in Iran. Int J Biol Pharm Res 2014; 5:428-431.
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18. Khan M, Al-Mansour MA, Mousa AA, Alkhathlan HZ. Compositional characteristics of the essential oil of Myrtus communis grown in the central part of Saudi Arabia. J Essent Oil Res 2014; 26:13-18.
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19. Abu-Dahab R, Kasabri V, Afifi FU. Evaluation of the volatile oil composition and antiproliferative activity of Laurus nobilis L. (Lauraceae) on breast cancer cell line models. Rec Nat Prod 2014; 8:136-147.
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20. Mostafavi H, Mousavi SH, Zalaghi A, Delsouzi R. Chemical composition of essential oil of Stachys byzantina from North-West Iran. J Essent Oil Bear Plant 2013; 16:334-337.
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21. Hosseinzadeh H, Dowlati S, Etemad L. Effects of Stachys byzantina C. Koch aerial parts aqueous extract on morphine dependence and tolerance in mice. Pharmacologyonline 2008; 2:614-617.
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22. Özek M, Üresin Y, Güngör M. Comparison of the effects of specific and nonspecific inhibition of nitric oxide synthase on morphine analgesia, tolerance and dependence in mice. Life Sci 2003;72:1943-1951.
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24. Abdel-Zaher AO, Abdel-Rahman MS, ELwasei FM. Blockade of nitric oxide over-production and oxidative stress by Nigella sativa oil attenuates morphine-induced tolerance and dependence in mice. Neurochem Res 2010; 35:1557-1565.
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27. Parvardeh S, Hosseinzadeh H. Hypnotic and muscle relaxant activity of thymoquinone, the major active constituent of Nigella sativa seeds, and its effects on locomotor activity and motor coordination in mice. J Med Plant 2003; 4:17-26.
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29. Kandel ER, Schwartz JH. Principles of Neural Science. 5th ed. McGraw-Hill; 2013.
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31. Abdel-Zaher AO, Hamdy MM, Aly SA, Abdel-Hady RH, Abdel-Rahman S. Attenuation of morphine tolerance and dependence by aminoguanidine in mice. Eur J Pharmacol 2006; 540:60-66.
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32. Abdel-Zaher AO, Mostafa MG, Farghly HM, Hamdy MM, Omran GA, Al-Shaibani NK. Inhibition of brain oxidative stress and inducible nitric oxide synthase expression by thymoquinone attenuates the development of morphine tolerance and dependence in mice. Eur J Pharmacol 2013; 702:62-70.
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33. Majeed NH, Przewłocka B, Machelska H, Przewłocki R. Inhibition of nitric oxide synthase attenuates the development of morphine tolerance and dependence in mice. Neuropharmacology 1994; 33:189-192.
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34. Cappendijk SL, de Vries R, Dzoljic MR. Inhibitory effect of nitric oxide (NO) synthase inhibitors on naloxone-precipitated withdrawal syndrome in morphine-dependent mice. Neurosci Lett 1993; 162:97-100.
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35. Özek M, Üresin Y, Güngör M. Comparison of the effects of specific and nonspecific inhibition of nitric oxide synthase on morphine analgesia, tolerance and dependence in mice. Life Sci 2003; 72:1943-1951.
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36. Homayoun H, Khavandgar S, Namiranian K, Dehpour AR. The effect of cyclosporin A on morphine tolerance and dependence: involvement of L-arginine/nitric oxide pathway. Eur J Pharmacol 2002; 452:67-75.
36
37. Vuong QV, Hirun S, Chuen TL, Goldsmith CD, Munro B, Bowyer MC, et al. Physicochemical, antioxidant and anti-cancer activity of a Eucalyptus robusta (Sm.) leaf aqueous extract. Indust Crop Prod 2015;64:167-174.
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38. Al-Sayed E, El-Naga RN. Protective role of ellagitannins from Eucalyptus citriodora against ethanol-induced gastric ulcer in rats: Impact on oxidative stress, inflammation and calcitonin-gene related peptide. Phytomedicine 2015; 22:5-15.
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39. Goudjil MB, Ladjel S, Bencheikh SE, Zighmi S, Hamada D. Study of the chemical composition, antibacterial and antioxidant activities of the essential oil extracted from the leaves of Algerian Laurus nobilis Lauraceae. J Chem Pharm Res 2015; 7:379-385.
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40. Cherrat, L, Espina, L, Bakkali, M, García‐Gonzalo, D, Pagán, R, Laglaoui, A. Chemical composition and antioxidant properties of Laurus nobilis L. and Myrtus communis L. essential oils from Morocco and evaluation of their antimicrobial activity acting alone or in combined processes for food preservation. J Sci Food Agric 2014; 94:1197-1204.
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41. El SN, Karagozlu N, Karakaya S, Sahın S. Antioxidant and antimicrobial activities of essential oils extracted from Laurus nobilis L. leaves by using solvent-free microwave and hydrodistillation. Food Nutr Sci 2014; 5:97-106.
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42. Asnaashari S, Delazar A, Alipour SS, Nahar L, Williams AS, Pasdaran A, et al. Chemical composition, free-radical-scavenging and insecticidal activities of the aerial parts of Stachys byzantina. Arch Biol Sci 2010; 62:653-662.
42
ORIGINAL_ARTICLE
Assessment of expressions of Bcl-XL, b-FGF, Bmp-2, Caspase-3, PDGFR-α, Smad1 and TGF-β1 genes in a rat model of lung ischemia/reperfusion
Objective(s):Ischemia is described as organs and tissues are destitute of oxygen due to decreased arterial or venous blood flow. Many mechanisms play role in cell death happened as a consequence of a new blood flow is needed for both cell regeneration and to clean toxic metabolites during ischemia and later. Lung damage induced by ischemia/reperfusion (I/R) is a frequent problem in lung transplantation. Apoptosis (programmed cell death) is known as cell suicide, and plays a key role in embryonic developmental and in maintain adult tissue’s life.
Materials and Methods:It is investigated expressions of Smad1, Bmp-2, Bcl-XL, b-FGF, Caspase-3, TGF-β1, PDGFR-α genes for molecular changes in lung tissues, after I/R is formed, in this study. For this, we included 40 Wistar albino rats to this study and divided 4 groups (n=10). The Groups were determined as Control (C), Group 1= 1 hr ischemia (I), Group 2= 1 hr ischemia+2 hr reperfusion (I+2R), Group 3= 1 hr ischemia+4 hr reperfusion (I+4R). Besides, molecular analysis and histopathologic examinations of tissues were performed, and the results were evaluated by normalization and statistics analysis.
Results: We have found a significant increase in expression of Bcl-XL (P=0.046) and Caspase-3 (P=0.026) genes of group 1, and it was not monitored any significant difference in Group 2 and Group 3. In all groups, the changes in b-FGF (P=0.087), Bmp-2 (P=0.457), TGF-β1 (P=0.201) and PDGFR-α (P=0.116) were not significant compared to control group. We did not see any mRNA expression of Smad1 gene in all groups include control.
Conclusion: These findings suggest that I/R injury may trigger apoptotic mechanism in lung.
https://ijbms.mums.ac.ir/article_6547_77d673394b582525b7ead558e2775b86.pdf
2016-02-01
209
214
10.22038/ijbms.2016.6547
Apoptosis
Growth factors
Ischemia/Reperfusion
Lung
Hasan
Şimşek
hasansimsek47@hotmail.com
1
Dumlupınar University, Department of Physiology, Faculty of Medicine, Kütahya, Turkey
AUTHOR
Şeniz
Demiryürek
sdemiryurek@gantep.edu.tr
2
Gaziantep University, Department of Physiology, Faculty of Medicine, Gaziantep, Turkey
LEAD_AUTHOR
Tuncer
Demir
drtuncer2003@yahoo.com
3
Gaziantep University, Department of Physiology, Faculty of Medicine, Gaziantep, Turkey
AUTHOR
Hüsne
Didem Atabay
4
Gaziantep University, Department of Physiology, Faculty of Medicine, Gaziantep, Turkey
AUTHOR
Ali Osman
Çeribasi
5
Fırat University, Department of Pathology, Faculty of Veterinary Science, Elazığ, Turkey
AUTHOR
Recep
Bayraktar
rbyrktr@gmail.com
6
Gaziantep University, Department of Medical Biology, Faculty of Medicine, Gaziantep, Turkey
AUTHOR
Davut
Sinan Kaplan
7
Gaziantep University, Department of Physiology, Faculty of Medicine, Gaziantep, Turkey
AUTHOR
Serdar
Öztuzcu
oztuzcu@gantep.edu.tr
8
Gaziantep University, Department of Medical Biology, Faculty of Medicine, Gaziantep, Turkey
AUTHOR
Beyhan
Cengiz
beyhancengiz@hotmail.com
9
Gazi University, Department of Medical Genetic, Faculty of Medicine, Ankara, Turkey
AUTHOR
1. Torres RL, Beló-Klein A, Andrade CF, Cardoso PF. Effect of systemically administered low potassium dextran solution on oxidative stress in a rat model of lung ischemia. Interact Cardiovasc Thorac Surg 2009; 8:3-6.
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2. Wilhelm J. Metabolic aspects of membrane lipid peroxidation. Acta Univ Carol Med Monogr 1990; 137:1-53
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3. Ng CS, Wan S, Yim AP. Pulmonary ischaemia-reperfusion injury: role of apoptosis. Eur Respir J 2005; 25 :356-363.
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4. Delbin MA, Antunes E, Zanesco A. Role of exercise training on pulmonary ischemia/reperfusion and inflammatory response. Rev Bras Cir Cardiovasc 2009; 24:552-561.
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5. Ryter SW, Choi AM. Autophagy in the lung. Proc Am Thorac Soc 2010; 7:13-21.
5
6. den Hengst WA, den Hengst WA. Lung ischemia-reperfusion injury: a molecular and clinical view on a complex pathophysiological process. Am J Physiol Heart Circ Physiol 2010; 299:H1283-1299.
6
7. Hotchkiss RS, Strasser A, McDunn JE, Swanson PE. Cell death. N Engl J Med 2009; 361:1570-1583.
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8. Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26:239-257.
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9. Connolly PF, Jäger R, Fearnhead HO. New roles for old enzymes: killer caspases as the engine of cell behavior changes. Front Physiol 2014; 5:149.
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10. Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, Korsmeyer SJ. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 2001; 8:705-711.
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11. Chipuk JE, Moldoveanu T, Llambi F, Parsons MJ, Green DR. The BCL-2 family reunion. Mol Cell 2010; 37:299-310.
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12. Gacche RN, Meshram RJ. Angiogenic factors as potential drug target: Efficacy and limitations of anti-angiogenic therapy. Biochim Biophys Acta 2014; 1846:161-179.
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13. Li HH, Huo LJ, Gao ZY, Zhao F, Zeng JW. Regulation of scleral fibroblast differentiation by bone morphogenetic protein-2. Int J Ophthalmol 2014; 7:152-156.
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14. Herhaus L, Sapkota GP. The emerging roles of deubiquitylating enzymes (DUBs) in the TGFbeta and BMP pathways. Cell Signal 2014; 26:2186-2192.
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15. Schul D, Schmitt A, Regneri J, Schartl M, Wagner TU. Burst BMP triggered receptor kinase activity drives Smad1 mediated long-term target gene oscillation in C2C12 cells. PloS One 2013; 8:e59442.
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16. Heldin CH. Targeting the PDGF signaling pathway in tumor treatment. Cell Commun Signal 2013; 11:97.
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17. Takhtfooladi H, Takhtfooladi M, Moayer F, Mobarakeh S. Melatonin attenuates lung injury in a hind limb ischemia-reperfusion rat model. Rev Port Pneumol 2015; 21:30-35.
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18. Forgiarini LF, Forgiarini LA Jr, da Rosa DP, Silva MB, Mariano R, Paludo Ade O,et al. N-acetylcysteine administration confers lung protection in different phases of lung ischaemia-reperfusion injury. Interact Cardiovasc Thorac Surg 2014; 19:894-899.
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19. Porter AG, Janicke RU. Emerging roles of caspase-3 in apoptosis. Cell Death Differ 1999; 6:99-104.
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20. Zhang Z, Shen H, Qin HD, Xu Y, Ma Mz, Bao L, Wang H. [Protective effect of N-acetylcysteine against pneumocyte apoptosis during ischemia/reperfusion injury of lung in rats]. Zhongguo wei zhong bing ji jiu yi xue = Chinese critical care medicine = Zhongguo weizhongbing jijiuyixue 2012; 24:111-115.
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21. Zhang C, Guo Z, Lio H, Shi Y, Ge S. Influence of levosimendan postconditioning on apoptosis of rat lung cells in a model of ischemia-reperfusion injury. PloS One 2015; 10:e0114963.
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22. Gao X, Cao Y, Staloch DA, Gonzales MA, Aronson JF. Bone morphogenetic protein signaling protects against cerulein-induced pancreatic fibrosis. PloS One 2014; 9:e89114.
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23. Langenfeld EM, Kong Y, Langenfeld J. Bone morphogenetic protein 2 stimulation of tumor growth involves the activation of Smad-1/5. Oncogene 2006; 25:685-692.
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24. Goumans MJ, Mummery C. Functional analysis of the TGFbeta receptor/Smad pathway through gene ablation in mice. Int J Dev Biol 2000; 44:253-265.
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25. Fu XB, Yang YH, Sun TZ, Gu XM, Jiang LX, Sun XQ, Sheng ZY. Effect of intestinal ischemia-reperfusion on expressions of endogenous basic fibroblast growth factor and transforming growth factor betain lung and its relation with lung repair. World J Gastroenterol 2000; 6:353-355
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26. Florkiewicz RZ, Ahluwalia A, Sandor Z, Szabo S, Tarnawski AS. Gastric mucosal injury activates bFGF gene expression and triggers preferential translation of high molecular weight bFGF isoforms through CUG-initiated, non-canonical codons. Biochem Biophys Res Commun 2011; 409:494-499.
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27. Sage E, Mercier O, Van den Eyden F, de Perrot M, Barlier-Mur AM, Dartevelle P, Eddahibi S. Endothelial cell apoptosis in chronically obstructed and reperfused pulmonary artery. Respir Res 2008; 9:19.
27
ORIGINAL_ARTICLE
Opium induces apoptosis in Jurkat cells via promotion of pro-apoptotic and inhibition of anti-apoptotic molecules
Objective(s): The aim of this study was to determine the important molecules involved in apoptosis induction by opium in Jurkat cell line.
Materials and Methods: Jurkat cells were incubated 48 hrs with2.86×10-5 g/ml concentration of opium and apoptosis as well as expression levels of related molecules weremeasured.
Results: Our results demonstrated that 50.3±0.2 percent of opium treated Jurkat cells were revealed apoptotic features. The levels of mRNA of several pro-apoptotic and anti-apoptotic molecules were increased and decreased, respectively, in the opium treated cells. The results also demonstrated that expression levels of BCL2, DFFA and NOL3 as anti-apoptotic molecules were increased in the opium treated cells.
Conclusion: It seems that opium induces apoptosis in Jurkat cells via both intrinsic and extrinsic pathways. Although opium induces apoptosis in the cells but increased expression of some anti-apoptotic molecules may be a normal resistance of the cell for death.
https://ijbms.mums.ac.ir/article_6548_d86a2aff9940d220b1630eac8b0f50a6.pdf
2016-02-01
215
220
10.22038/ijbms.2016.6548
Apoptosis
Jurkat cells
PCR array
Mohammad
Kazemi Arababadi
dr.kazemi@rums.ac.ir
1
Department of Laboratoty Sciences, Faculty of Paramedicine, Rafsanjan University of Medical Sciences, Rafsanjan, Iran
AUTHOR
Gholamreza
Asadikaram
immuno.paper@yahoo.com
2
Endocrinology and Metabolism Research Center, Institute of Basic and Clinical Physiology Sciences and Department of Biochemistry, School of Medicine, Kerman University of Medical Sciences, Kerman, Iran
LEAD_AUTHOR
1. Takata A, Terauchi M, Hiramitsu S, Uno M, Wakana K, Kubota T. Dkk-3 induces apoptosis through mitochondrial and fas death receptor pathways in human mucinous ovarian cancer cells. Int J Gynecol Cancer 2014; 25:372-379.
1
2. Paganelli R, Giovannetti A, Pierdominici M, Iorio A, Cianci R, Murdaca G, et al. Apoptosis in the homeostasis of the immune system and in human immune mediated diseases. Curr Pharm Des. 2008; 14:253-268.
2
3. Khalil H, Rosenblatt N, Liaudet L, Widmann C. The role of endogenous and exogenous RasGAP-derived fragment N in protecting cardiomyocytes from peroxynitrite-induced apoptosis. Free Radic Biol Med 2012; 53:926-935.
3
4. Mirzaei MR, Najafi A, Arababadi MK, Asadi MH, Mowla SJ. Altered expression of apoptotic genes in response to OCT4B1 suppression in human tumor cell lines. Tumor Biol 2014; 35:9999-10009.
4
5. Aydin AF, Ersahin ME, Dereli RK, Sarikaya HZ, Ozturk I. Long-term anaerobic treatability studies on opium alkaloids industry effluents. J Environ Sci Health A Tox Hazard Subst Environ Eng 2010; 45:192-200.
5
6. Buchbauer G, Nikiforov A, Remberg B. Headspace constituents of opium. Planta Med 1994; 60:181-183.
6
7. Asiabanha M, Asadikaram G, Rahnema A, Mahmoodi M, Hasanshahi G, Hashemi M, et al. Chronic opium treatment can differentially induce brain and liver cells apoptosis in diabetic and non-diabetic male and female rats. Korean J Physiol Pharmacol 2011; 15:327-332.
7
8. Igder S, Asadikaram GR, Sheykholeslam F, Sayadi AR, Mahmoodi M, Arababadi MK, et al. Opium induces apoptosis in Jurkat cells. Addict Health 2013; 5:27.
8
9. Asadikaram G, Sirati-Sabet M, Asiabanha M, Shahrokhi N, Jafarzadeh A, Khaksari M. Hematological changes in opium addicted diabetic rats. Int J High Risk Behav Addict 2013; 1:141-148.
9
10. Ghazavi A, Solhi H, Moazzeni SM, Rafiei M, Mosayebi G. Cytokine profiles in long-term smokers of opium (Taryak). J Addict Med 2013; 7:200-203.
10
11. Nabati S, Asadikaram G, Arababadi MK, Shahabinejad G, Rezaeian M, Mahmoodi M, et al. The plasma levels of the cytokines in opium-addicts and the effects of opium on the cytokines secretion by their lymphocytes. Immunol Lett 2013; 152:42-46.
11
12. Momeni M, Mirzaei MR, Zainodini N, Hassanshahi G, Arababadi MK. MiR-143 induces expression of AIM2 and ASC in Jurkat cell line. Iran J Immunol 2013; 10:103.
12
13. Momeni M, Zainodini N, Bidaki R, Hassanshahi G, Daneshvar H, Khaleghinia M, et al. Decreased expression of toll like receptor signaling molecules in chronic HBV infected patients. Hum Immun 2014; 75:15-19.
13
14. Wang JY. The capable ABL: what is its biological function? Mol Cell Biol 2014; 34:1188-1197.
14
15. Fernández-Velasco M, Prieto P, Terrón V, Benito G, Flores JM, Delgado C, et al. NOD1 activation induces cardiac dysfunction and modulates cardiac fibrosis and cardiomyocyte apoptosis. PloS One 2012; 7:e45260.
15
16. Etemadi N, Holien JK, Chau D, Dewson G, Murphy JM, Alexander WS, et al. Lymphotoxin α induces apoptosis, necroptosis and inflammatory signals with the same potency as tumour necrosis factor. FEBS J 2013; 280:5283-5297.
16
17. Kuai J, Nickbarg E, Wooters J, Qiu Y, Wang J, Lin L-L. Endogenous association of TRAF2, TRAF3, cIAP1, and Smac with lymphotoxin β receptor reveals a novel mechanism of apoptosis. J Biol Chem 2003; 278:14363-14369.
17
18. D'Osualdo A, Ferlito F, Prigione I, Obici L, Meini A, Zulian F, et al. Neutrophils from patients with TNFRSF1A mutations display resistance to tumor necrosis factor–induced apoptosis: pathogenetic and clinical implications. Arthritis Rheum 2006; 54:998-1008.
18
19. Yao H, Mi S, Gong W, Lin J, Xu N, Perrett S, et al. Anti-apoptosis proteins Mcl-1 and Bcl-xL have different p53-binding profiles. Biochemistry 2013; 52:6324-6334.
19
20. Ju H, Lee KA, Yang M, Kim HJ, Kang CP, Sohn TS, et al. TP53BP2 locus is associated with gastric cancer susceptibility. Int J Cancer 2005; 117:957-960.
20
21. Li C, Chang L, Guo L, Zhao D, Liu H, Wang Q, et al. β-elemene induces caspase-dependent apoptosis in human glioma cells in vitro through the upregulation of bax and fas/fasL and downregulation of Bcl-2. Asian Pac J Cancer Prev 2013; 15:10407-10412.
21
22. Koekemoer AL, Chong NW, Goodall AH, Samani NJ. Myocyte stress 1 plays an important role in cellular hypertrophy and protection against apoptosis. FEBS Lett 2009; 583:2964-2967.
22
ORIGINAL_ARTICLE
Cardioprotective effect of royal jelly on paclitaxel-induced cardio-toxicity in rats
Objective(s):Paclitaxel is a potent chemotherapy agent with severe side effects, including allergic reactions, cardiovascular problems, complete hair loss, joint and muscle pain, which may limit its use and lower its efficiency. The cardioprotective effect of royal jelly was investigated on paclitaxel-induced damages. Materials and Methods:Adult male Wistar rats were divided into control and test groups (n=8). The test group was assigned into five subgroups; 4 groups, along with paclitaxel administration (7.5 mg/kg BW, weekly), received various doses of royal jelly (50, 100, and 150 mg/kg BW) for 28 consecutive days. The last group received only royal jelly at 100 mg/kg. In addition to oxidative and nitrosative stress biomarkers, the creatine kinase (CK-BM) level was also determined. To show the cardioprotective effect of royal jelly on paclitaxel-induced damages, histopathological examinations were conducted. Results:Royal jelly lowered the paclitaxel-elevated malondialdehyde and nitric oxide levels in the heart. Royal jelly could also remarkably reduce the paclitaxel-induced cardiac biomarker of creatine kinase (CK-BM) level and pathological injuries such as diffused edema, hemorrhage, congestion, hyaline exudates, and necrosis. Moreover, royal jelly administration in a dose-dependent manner resulted in a significant (P<0.05) increase in the paclitaxel-reduced total antioxidant capacity. Conclusion:Our data suggest that the paclitaxel-induced histopathological and biochemical alterations could be protected by the royal jelly administration. The cardioprotective effect of royal jelly may be related to the suppression of oxidative and nitrosative stress.
https://ijbms.mums.ac.ir/article_6549_b806ccbe30c4386db77d83ef572af84b.pdf
2016-02-01
221
227
10.22038/ijbms.2016.6549
Antioxidant
Cardioprotective effect
Paclitaxel
Royal jelly
Hassan
Malekinejad
hassanmalekinejad@yahoo.com
1
Department of Pharmacology and Toxicology, Faculty of Pharmacy, Urmia University of Medical Sciences, Urmia, Iran
LEAD_AUTHOR
Sima
Ahsan
2
Department of Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Urmia, Iran
AUTHOR
Fatemeh
Delkhosh-Kasmaie
3
Department of Pathology, Faculty of Veterinary Medicine, University of Urmia, Iran
AUTHOR
Hadi
Cheraghi
cheraghi_hadi@yahoo.com
4
Department of Clinical Pathology, Faculty of Veterinary Medicine, Tehran University, Tehran, Iran
AUTHOR
Ali
Rezaei-Golmisheh
a_rezaei82@yahoo.com
5
Department of Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Urmia, Iran
AUTHOR
Hamed
Janbaz-Acyabar
6
Department of Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Urmia, Iran
AUTHOR
1. Rowinsky EK, Donehower RC. The clinical pharmacology and use of antimicrotubule agents in cancer chemotherapeutics. Pharmacol Ther 1991; 52:35-84.
1
2. Needleman DJ, Ojeda-Lopez MA, Raviv U, Ewert K, Miller HP, Wilson L, et al. Radial compression of microtubules and the mechanism of action of taxol and associated proteins. Biophys J 2005; 89:3410–3423.
2
3. Onetto N, Canetta R, Winograd B, Catane R, Dougan M, Grechko J, et al. Overview of Taxol safety. J Natl Cancer Inst Monogr 1993; 15:131–139.
3
4. Nagai T, Inoue R. Preparation and functional properties of water extract and alkaline extract of royal jelly. Food Chem 2004; 84:181–186.
4
5. Caparica-Santos C, Marcucci MC. Quantitative determination of trans-10- hydroxy-2-decenoic acid (10-HDA) in Brazilian royal jelly and commercial products containing royal jelly. J Apicultural Res 2007; 46:149–153.
5
6. Matsui T, Doi YA, Sugimoto S, Yamada H, Matsumoto HK. Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR. J Nutr Biochem 2002; 13:80–86.
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