ORIGINAL_ARTICLE
Pathogenic interactions between Helicobacter pylori adhesion protein HopQ and human cell surface adhesion molecules CEACAMs in gastric epithelial cells
Objective(s): The present paper aims to review the studies describing the interactions between HopQ and CEACAMs along with possible mechanisms responsible for pathogenicity of Helicobacter pylori.Materials and Methods: The literature was searched on “PubMed” using different key words including Helicobacter pylori, CEACAM and gastric.Results: HopQ is one of the outer membrane proteins of H. pylori and belongs to the family of adhesin proteins. In contrast to other adhesins, HopQ interacts with host cell surface molecules in a glycan independent manner. Human CEACAMs are the cell surface adhesion molecules mainly present on the epithelial cells, endothelial cells and leukocytes. The overexpression of these molecules may contribute to cancer progression and relapse. Recent studies have shown that HopQ may interact with human CEACAMs, particularly CEACAM1, CEACAM3, CEACAM5 and CEACAM6, but not CEACAM8. HopQ interacts with GFCC’C” interaction surface of IgV domain of N- terminal region of CEACAM1. Moreover, binding of HopQ to CEACAM1 prevent its trans-dimerization and stabilizes it in monomeric form. H. pylori may use these HopQ-CEACAM interactions to transfer its CagA oncoprotein into host gastric epithelial cells, which is followed by its phosphorylation and release of interleukin-8. HopQ-CEACAM interactions may also utilize T4SS, instead of CagA, to activate NF-κB signaling and trigger inflammation. Conclusion: HopQ of H. pylori may interact with CEACAMs of the human gastric cells to induce the development of gastric ulcers and cancers by transferring CagA oncoprotein or inducing activation of T4SS to initiate and maintain inflammatory reactions.
https://ijbms.mums.ac.ir/article_13103_04d7aa9dec353d698a15e7aa16fbc699.pdf
2019-07-01
710
715
10.22038/ijbms.2019.34237.8136
CEACAM
Gastric epithelial cells Helicobacter pylori
Interleukin 8
NF-kB
Ran
Xia
zhangorange638@aliyun.com
1
Geriatrics Department, the Affiliated Hospital to Changchun University of Chinese Medicine, Changchun, China
AUTHOR
Bo
Zhang
begoniazhang01@sina.com
2
Geriatrics Department, the Affiliated Hospital to Changchun University of Chinese Medicine, Changchun, China
AUTHOR
Xinxin
Wang
rainwang22@163.com
3
Medical Record Room, the Affiliated Hospital to Changchun University of Chinese Medicine, Changchun, China
AUTHOR
Qiuying
Jia
qy_jia@yahoo.com
4
Geriatrics Department, the Affiliated Hospital to Changchun University of Chinese Medicine, Changchun, China
LEAD_AUTHOR
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48
ORIGINAL_ARTICLE
Four main therapeutic keys for Parkinson’s disease: A mini review
Objective(s): Parkinson’s disease (PD) is characterized by motor and cognitive dysfunctions. The progressive degeneration of dopamine-producing neurons that are present in the substantia nigra pars compacta (SNpc) has been the main focus of study and PD therapies since ages.Materials and Methods: In this manuscript, a systematic revision of experimental and clinical evidence of PD-associated cell process was conducted. Results: Classically, the damage in the dopaminergic neuronal circuits of SNpc is favored by reactive oxidative/nitrosative stress, leading to cell death. Interestingly, the therapy for PD has only focused on avoiding the symptom progression but not in finding a complete reversion of the disease. Recent evidence suggests that the renin-angiotensin system imbalance and neuroinflammation are the main keys in the progression of experimental PD. Conclusion: The progression of neurodegeneration in SNpc is due to the complex interaction of multiple processes. In this review, we analyzed the main contribution of four cellular processes and discussed in the perspective of novel experimental approaches.
https://ijbms.mums.ac.ir/article_13010_e438c485cb63dcfc82e423bb96ab8375.pdf
2019-07-01
716
721
10.22038/ijbms.2019.33659.8025
Cell death
Dopaminergic neurons
Inflammation
Survival
Therapeutics
Daniel
Hernandez-Baltazar
dan.hernandez.baltazar@gmail.com
1
CONACYT-Instituto de Neuroetologia, Universidad Veracruzana, Xalapa, Veracruz, Mexico
LEAD_AUTHOR
Rasajna
Nadella
rasagna.s@gmail.com
2
IIIT Srikakulam, Rajiv Gandhi University of Knowledge Technologies (RGUKT); International collaboration ID:1840; India
AUTHOR
Laura Mireya
Zavala Flores
laura5utr@gmail.com
3
Centro de Investigacion Biomedica del Noreste. IMSS. Monterrey, Nuevo Leon. Mexico
AUTHOR
Christian de Jesus
Rosas-Jarquin
diesel9108@gmail.com
4
Instituto de Neuroetologia, Universidad Veracruzana. Xalapa, Veracruz, Mexico
AUTHOR
Maria de Jesus
Rovirosa-Hernandez
mrovirosa@yahoo.com
5
Instituto de Neuroetologia, Universidad Veracruzana. Xalapa, Veracruz, Mexico
AUTHOR
Arnulfo
Villanueva-Olivo
fitofagos@gmail.com
6
Facultad de Medicina. Universidad Autonoma de Nuevo Leon. Monterrey, Nuevo Leon, Mexico
AUTHOR
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63. Chao J, Yang L, Buch S, Gao L. Angiotensin II increased neuronal stem cell proliferation: role of AT2R. PLoS One 2013; 8:e63488.
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65. Garrido-Gil P, Rodriguez-Pallares J, Dominguez-Meijide A, Guerra MJ, Labandeira-Garcia JL. Brain angiotensin regulates iron homeostasis in dopaminergic neurons and microglial cells. Exp Neurol 2013; 250:384-396.
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66. Labandeira-Garcia JL, Rodriguez-Pallares J, Rodriguez-Perez AI, Garrido-Gil P, Villar-Cheda B, Valenzuela R, et al. Brain angiotensin and dopaminergic degeneration: relevance to Parkinson’s disease. Am J Neurodegener Dis 2012; 1:226-244.
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67. Munoz A, Garrido-Gil P, Dominguez-Meijide A, Labandeira-Garcia JL. Angiotensin type 1 receptor blockage reduces l-dopa-induced dyskinesia in the 6-OHDA model of Parkinson’s disease. Involvement of vascular endothelial growth factor and interleukin-1beta. Exp Neurol 2014; 261:720-732.
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68. Rocha NP, Scalzo PL, Barbosa IG, de Campos-Carli SM, Tavares LD, de Souza MS, et al. Peripheral levels of angiotensins are associated with depressive symptoms in Parkinson’s disease. J Neurol Sci 2016; 368:235-239.
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69. Villar-Cheda B, Costa-Besada MA, Valenzuela R, Perez-Costas E, Melendez-Ferro M, Labandeira-Garcia JL. The intracellular angiotensin system buffers deleterious effects of the extracellular paracrine system. Cell Death Dis 2017; 8:e3044.
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71. Stallcup WB. The NG2 proteoglycan: past insights and future prospects. J Neurocytol 2002; 31:423-435.
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73. Chung SH, Guo F, Jiang P, Pleasure DE, Deng W. Olig2/Plp-positive progenitor cells give rise to Bergmann glia in the cerebellum. Cell Death Dis 2013; 4:e546.
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75. Chari DM, Blakemore WF. Efficient recolonisation of progenitor-depleted areas of the CNS by adult oligodendrocyte progenitor cells. Glia 2002; 37:307-313.
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76. Magnus T, Carmen J, Deleon J, Xue H, Pardo AC, Lepore AC, et al. Adult glial precursor proliferation in mutant SOD1G93A mice. Glia 2008; 56:200-208.
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77. Nait-Oumesmar B, Decker L, Lachapelle F, Avellana-Adalid V, Bachelin C, Baron-Van Evercooren A. Progenitor cells of the adult mouse subventricular zone proliferate, migrate and differentiate into oligodendrocytes after demyelination. Eur J Neurosci 1999; 11:4357-4366.
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78. Tamura Y, Kataoka Y, Cui Y, Takamori Y, Watanabe Y, Yamada H. Multi-directional differentiation of doublecortin- and NG2-immunopositive progenitor cells in the adult rat neocortex in vivo. Eur J Neurosci 2007; 25:3489-3498.
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79. Charvin D, Medori R, Hauser RA, Rascol O. Therapeutic strategies for Parkinson disease: beyond dopaminergic drugs. Nat Rev Drug Discov 2018; 17:804-822
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81. Sanchez-Barcelo EJ, Rueda N, Mediavilla MD, Martinez-Cue C, Reiter RJ. Clinical Uses of Melatonin in Neurological Diseases and Mental and Behavioural Disorders. Curr Med Chem 2017; 24:3851-3878.
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82. Martinez B, Peplow PV. Neuroprotection by immunomodulatory agents in animal models of Parkinson’s disease. Neural Regen Res 2018; 13:1493-1506.
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83. Wang YL, Ju B, Zhang YZ, Yin HL, Liu YJ, Wang SS, et al. Protective effect of curcumin against oxidative stress-induced injury in rats with Parkinson’s disease through the Wnt/ beta-catenin signaling pathway. Cell Physiol Biochem 2017; 43:2226-2241.
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86. Kirik D, Cederfjall E, Halliday G, Petersen A. Gene therapy for Parkinson’s disease: Disease modification by GDNF family of ligands. Neurobiol Dis 2017; 97:179-188.
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87. Pignataro D, Sucunza D, Rico AJ, Dopeso-Reyes IG, Roda E, Rodriguez-Perez AI, et al. Gene therapy approaches in the non-human primate model of Parkinson’s disease. J Neural Transm (Vienna) 2018; 125:575-589.
87
ORIGINAL_ARTICLE
Irisin protect the Dopaminergic neurons of the Substantia nigra in the rat model of Parkinson’s disease
Objective(s): Exercise ameliorates the quality of life and reduces the risk of neurological derangements such as Alzheimer’s (AD) and Parkinson’s disease (PD). Irisin is a product of the physical activity and is a circulating hormone that regulates the energy metabolism in the body. In the nervous system, Irisin influences neurogenesis and neural differentiation in mice. We previously demonstrated that co-treatment of bone marrow stem cells (BMSCs) with a neurotrophic factor reduce Parkinson’s symptoms. Our goal in this project was to evaluate whether Irisin with BMSCs can protect the dopaminergic (DA) neurons in PD. Materials and Methods: 35 adult male Wistar rat weighing (200-250 g) were chosen. They were separated into five experimental groups (n=7). To create a Parkinson’s model, intranasal (IN) administration of the MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) was used. The BMSCs (2×106) and Irisin (50 nm/ml) was used for 7 days for treatment after creation of the PD model. After completion of the tests (4 weeks), their brains were used for the TUNEL and immunohistochemical (IHC) assays.Results: One of the important results of this study was that the Irisin induce BMSCs transport into the injured area of the brain. Co-treatment of the Irisin with BMSCs increased tyrosine hydroxylase-positive neurons (TH+) in substantia nigra (SN) and striatum of the PD mice brain. In this group, the number of TUNEL-positive cells significantly decreased. Behavioral symptoms were better in the combination group and Irisin simultaneously. Conclusion: Co- treatment of Irisin with BMSCs protects the DA neurons from degeneration and apoptotic process after MPTP injection.
https://ijbms.mums.ac.ir/article_13161_3e009c1bcb9a1c73405ec0829cade405.pdf
2019-07-01
722
728
10.22038/ijbms.2019.33444.7987
Irisin
Mesenchymal stem cells
Parkinson’s disease
Substantia nigra
Tunel
Sam
Zarbakhsh
szarbakhsh@yahoo.com
1
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
Manouchehr
Safari
kh_safari@yahoo.com
2
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
LEAD_AUTHOR
Mohammad Reza
Aldaghi
mald222@yahoo.com
3
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
Hamidreza
Sameni
hrsameni@gmail.com
4
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
Laya
Ghahari
laya_gh@yahoo.com
5
Department of Anatomy, AJA University of Medical Sciences, Tehran, Iran
AUTHOR
Younes
Khaleghi Lagmouj
ykhaleghi@gmail.com
6
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
Khojasteh
Rahimi Jaberi
khojasterahimi@gmail.com
7
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
Houman
Parsaie
houman70parsaie@gmail.com
8
Research Center of Nervous System Stem Cells, Department of Anatomy, Semnan University of Medical Sciences, Semnan , Iran
AUTHOR
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13. Dun SL, Lyu RM, Chen YH, Chang JK, Luo JJ, Dun NJ. Irisin-immunoreactivity in neural and non-neural cells of the rodent. Neuroscience 2013; 240:155-162.
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15. Wrann CD. FNDC5/irisin - their role in the nervous system and as a mediator for beneficial effects of exercise on the brain. Brain Plast 2015; 1:55-61.
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17. Greenberg ME, Xu B, Lu B, Hempstead BL. New insights in the biology of BDNF synthesis and release: implications in CNS function. J Neurosci 2009; 29:12764-12767.
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19. Hastings TG. The role of dopamine oxidation in mitochondrial dysfunction: implications for Parkinson’s disease. J Bioenerg Biomembr 2009; 41:469-472.
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20. Prediger RD, Batista LC, Medeiros R, Pandolfo P, Florio JC, Takahashi RN. The risk is in the air: Intranasal administration of MPTP to rats reproducing clinical features of Parkinson’s disease. Exp Neurol 2006; 202:391-403.
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22. Zhang W, He H, Song H, Zhao J, Li T, Wu L, et al. Neuroprotective effects of salidroside in the MPTP mouse model of Parkinson’s disease: Involvement of the PI3K/Akt/GSK3β Pathway. Parkinsons Dis 2016; 2016:9450137.
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23. Jadidi M, Biat SM, Sameni HR, Safari M, Vafaei AA, Ghahari L. Mesenchymal stem cells that located in the electromagnetic fields improves rat model of Parkinson’s disease. Iran J Basic Med Sci 2016; 19:741-748.
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24. Zarbakhsh S, Goudarzi N, Shirmohammadi M, Safari M. Histological study of bone marrow and umbilical cord stromal cell transplantation in regenerating rat peripheral nerve. Cell journal 2016; 17:668-677.
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25. Tatton NA, Kish SJ. In situ detection of apoptotic nuclei in the substantia nigra compacta of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-treated mice using terminal deoxynucleotidyl transferase labelling and acridine orange staining. Neuroscience 1997; 77:1037-1048.
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26. Grygiel-Górniak B, Puszczewicz M. A review on irisin, a new protagonist that mediates muscle-adipose-bone-neuron connectivity. Eur Rev Med Pharmacol Sci 2017; 21:4687-4693.
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38
ORIGINAL_ARTICLE
GYY4137 a H2S donor, attenuates ipsilateral epididymis injury in experimentally varicocele-induced rats via activation of the PI3K/Akt pathway
Objective(s): The current study was aimed to investigate the effect of morpholin-4-ium 4 methoxyphenyl (morpholino) phosphinodithioate (GYY4137) on ipsilateral epididymis injury in a rat model of experimental varicocele (VC).Materials and Methods: Sixty Wistar rats were randomly assigned to sham, sham plus GYY4137, VC and VC plus GYY4137 groups. Sperm quality parameters, including sperm count, motility and viability were evaluated after 4 weeks. Histological changes were measured by hematoxylin and eosin staining between the groups. The oxidative stress levels were estimated by determining epididymal superoxide dismutase (SOD) and malondialdehyde (MDA). The apoptosis status and the expression of phosphatidylinositol 3′-OH kinase (PI3K)/Akt were analyzed by immunohistochemical analysis, western blot and RT-qPCR. Results: VC resulted in the decrease of sperm parameters, significant histological damage and higher levels of oxidative stress and apoptosis. Compared to the VC group, GYY4137 markedly ameliorated these observed changes. In addition, treatment with GYY4137 obviously reduced the levels of caspase-3 and Bax and increased the levels of the phosphorylation of PI3K p85 and Akt. Conclusion: Our data demonstrated that GYY4137 may alleviate the sperm damage and epididymis injury in experimentally VC-induced rats by activation of the PI3K/Akt pathway.
https://ijbms.mums.ac.ir/article_12180_82051b57b7ef6125b38ca0a7e47f7913.pdf
2019-07-01
729
735
10.22038/ijbms.2019.30588.7372
Apoptosis
Epididymis
GYY4137
Reactive Oxygen Species
Varicocele
Yu-qi
Xia
xiayuqi1994@qq.com
1
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Jin-zhuo
Ning
1315816132@qq.com
2
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Fan
Cheng
urology1969@aliyun.com
3
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
LEAD_AUTHOR
Wei-min
Yu
416202996@qq.com
4
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Ting
Rao
chenfan_93@126.com
5
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Yuan
Ruan
yuanruan@126.com
6
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Run
Yuan
805258017@qq.com
7
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
Yang
Du
phoenixneo@126.com
8
Department of Urology, Renmin Hospital of Wuhan University, Wuhan, Hubei 430060, P.R. China
AUTHOR
1. Damsgaard J, Joensen UN, Carlsen E, Erenpreiss J, Blomberg Jensen M, Matulevicius V, et al. Varicocele Is Associated with Impaired Semen Quality and Reproductive Hormone Levels: A Study of 7035 Healthy Young Men from Six European Countries. Eur Urol 2016; 70:1019-1029.
1
2. Sheehan MM, Ramasamy R, Lamb DJ. Molecular mechanisms involved in varicocele-associated infertility. J Assist Reprod Genet 2014; 31:521-526.
2
3. Zha WL, Yu W, Zhang X, Zheng YQ, Cheng F, Rao T, et al. Effects of artery-ligating and artery-preserving varicocelectomy on ipsilateral epididymis of varicocele-induced rats. Urology 2011; 77:1008 e1009-1008 e1015.
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4. Sullivan R, Mieusset R. The human epididymis: its function in sperm maturation. Hum Reprod Update 2016; 22:574-587.
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5. Vivas-Acevedo G, Lozano-Hernandez R, Camejo MI. Varicocele decreases epididymal neutral alpha-glucosidase and is associated with alteration of nuclear DNA and plasma membrane in spermatozoa. BJU Int 2014; 113:642-649.
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6. Johnson D, Sandlow J. Treatment of varicoceles: techniques and outcomes. Fertil Steril 2017; 108:378-384.
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7. Abdel-Meguid TA, Al-Sayyad A, Tayib A, Farsi HM. Does varicocele repair improve male infertility? An evidence-based perspective from a randomized, controlled trial. European Urology 2011; 59:455-461.
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11. Nussbaum BL, Vogt J, Wachter U, McCook O, Wepler M, Matallo J, et al. Metabolic, cardiac, and renal effects of the slow hydrogen sulfide-releasing molecule GYY4137 during resuscitated septic shock in swine with Pre-existing coronary artery disease. Shock 2017; 48:175-184.
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12. Wu D, Luo N, Wang L, Zhao Z, Bu H, Xu G, et al. Hydrogen sulfide ameliorates chronic renal failure in rats by inhibiting apoptosis and inflammation through ROS/MAPK and NF-κB signaling pathways. Scientific Reports 2017; 7.
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48
ORIGINAL_ARTICLE
Allantoin improves methionine-choline deficient diet-induced nonalcoholic steatohepatitis in mice through involvement in endoplasmic reticulum stress and hepatocytes apoptosis-related genes expressions
Objective(s): Non-alcoholic steatohepatitis (NASH) is defined by steatosis and inflammation in the hepatocytes, which can progress to cirrhosis and possibly hepatocellular carcinoma. However, current treatments are not entirely effective. Allantoin is one of the principal compounds in many plants and an imidazoline I receptor agonist as well. Allantoin has positive effects on glucose metabolism and inflammation. In this study, the effects of allantoin on the NASH induced animals and the pathways involved have been evaluated. Materials and Methods: C57/BL6 male mice received saline and allantoin as the control groups. In the next group, NASH was induced by the methionine-choline-deficient diet (MCD) for eight weeks. In the NASH+allantoin group, allantoin was injected four weeks in the mice feeding on an MCD diet. Histopathological evaluations, serum analysis, ELISA assay, and real-time RT-PCR were performed. Results: Allantoin administration decreased serum alanine aminotransferase (ALT), cholesterol, low-density lipoprotein (LDL), hepatic lipid accumulation, and liver tumor necrosis factor (TNFα) level. Also, treatment with allantoin down-regulated the gene expression of glucose-regulated protein 78 (GRP78), activating transcription factor 6 (AFT6), TNFα, sterol regulatory element binding proteins 1c (SREBP1c), fatty acid synthase (FAS), Bax/Bcl2 ratio, caspase3, and P53. On the other hand, peroxisome proliferator-activated receptor alpha (PPARα), apolipoprotein B (Apo B), and acetyl-coenzyme acetyltransferase 1 (ACAT1) gene expression increased after allantoin injection. Conclusion: This study indicated that allantoin could improve animal induced NASH by changes in the expression of endoplasmic reticulum stress-related genes and apoptotic pathways.
https://ijbms.mums.ac.ir/article_13009_2f19f6202f8dedda2bc0f4cd4dc175a4.pdf
2019-07-01
736
744
10.22038/ijbms.2019.33553.8012
Allantoin
Liver
Non-alcoholic steatohepatitis
PPARα
SREBP1c
Steatosis
Tahereh
Komeili Movahhed
t_komeili.m@gmail.com
1
Cellular & Molecular Research Center, Qom University of Medical Sciences, Qom, Iran
AUTHOR
Azam
Moslehi
moslehi2000@gmail.com
2
Cellular & Molecular Research Center, Qom University of Medical Sciences, Qom, Iran
LEAD_AUTHOR
Mohammad
Golchoob
m.golchoob@gmail.com
3
Student Research Committee, Qom University of Medical Sciences, Qom, Iran
AUTHOR
shima
ababzadeh
shimaababzadeh@gmail.com
4
Cellular & Molecular Research Center, Qom University of Medical Sciences, Qom, Iran
AUTHOR
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19. Rezazadeh. A, Yazdanparast. R, Molaei. M, Amelioration of diet-induced nonalcoholic steatohepatitis in rats by Mn-salen complexes via reduction of oxidative stress, J Biomed Sci 2012;19: 26.
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20. Moslehi A, Nabavizadeh F, Zekri A, Amiri F. Naltrexone changes the expression of lipid metabolism-related proteins in the endoplasmic reticulum stress induced hepatic steatosis in mice. Clin Exp Pharmacol Physiol 2017; 44: 207-212.
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21. Kleiner DE, Brunt EM, Van Natta M, Behling C, Contos MJ, Cummings OW, et al. Design and validation of a histological scoring system for nonalcoholic fatty liver disease. Hepatology 2005;41: 1313-1321.
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22. Bozaykut P, Sahin A, Karademir B, Ozer NK. Endoplasmic reticulum stress related molecular mechanisms in nonalcoholic steatohepatitis. Mech Ageing Dev 2016; 157: 17-29.
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23. Moslehi A, Nabavizadeh F, Dehpour AR, Tavangar SM, Hassanzadeh G, Zekri A, et al. Naltrexone attenuates endoplasmic reticulum stress induced hepatic injury in mice. Acta Physiol Hung 2014;101: 341-352.
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29. Lin KC, Yeh LR, Chen LJ, Wen YJ, Cheng KC, Cheng JT. Plasma glucose-lowering action of allantoin is induced by activation of imidazoline I-2 receptors in streptozotocin-induced diabetic rats. Horm Metab Res 2012; 44: 41-46.
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30. Lee JP, Chen W, Wu HT, Lin KC, Cheng JT. Metformin can activate imidazoline I-2 receptors to lower plasma glucose in type 1-like diabetic rats. Horm Metab Res 2011; 43: 26-30.
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38
ORIGINAL_ARTICLE
The effect of titanium dioxide nanoparticles on mice midbrain substantia nigra
Objective(s): Widely used Titanium dioxide nanoparticles (TiO2) enter into the body and cause various organ damages. Therefore, we aimed to study the effect of TiO2 on the substantia nigra of midbrain. Materials and Methods: 40 male BALB/c mice were randomly divided into five groups: three groups received TiO2 at doses of 10, 25, and 50 mg/kg, the fourth group received normal saline for 45 days by gavage, and control group (without intervention). Then, Motor tests including pole and hanging tests were done to investigate motor disorders. The animal brain was removed for histological purposes. Accordingly, immunohistochemistry was performed to detect tyrosine hydroxylase positive cells, and then toluidine blue staining was done to identify dark neurons in the substantia nigra. Eventually, the total number of these neurons were counted using stereological methods in different groups.Results: The results showed that the time recorded for mice to turn completely downward on the pole in the TiO2-50 group increased and also the time recorded for animals to hang on the wire in the hanging test significantly decreased (P<0.05) in comparison with other groups. Also, the average number of tyrosine hydroxylase positive neurons in TiO2-25 and TiO2-50 groups significantly decreased as compared to the TiO2-10 and control groups (P<0.05). The total number of dark neurons in the TiO2-25 and TiO2-50 groups was substantially higher than the TiO2-10, control and normal saline groups (P<0.05).Conclusion: Our findings indicated that TiO2, depending on dose, can cause the destruction of dopaminergic neurons and consequently increase the risk of Parkinson’s disease.
https://ijbms.mums.ac.ir/article_13162_7a514878e78959136bce619c6aeaa9ad.pdf
2019-07-01
745
751
10.22038/ijbms.2019.33611.8018
Dark neurons
Mice
Substantia nigra
Titanium dioxide nanoparticles
Tyrosine hydroxylase neurons
Zahra
Heidari
heidariz941@mums.ac.ir
1
Department of Anatomy and Cell Biology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Abbas
Mohammadipour
mohammadipa@mums.ac.ir
2
Department of Anatomy and Cell Biology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Parisa
Haeri
haerip941@mums.ac.ir
3
Department of Anatomy and Cell Biology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Alireza
Ebrahimzadeh-bideskan
ebrahimzadehba@mums.ac.ir
4
Department of Anatomy and Cell Biology, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
LEAD_AUTHOR
1. Chen X, Mao S. Titanium dioxide nanomaterials: synthesis, properties, modifications, and applications. Chem Rev 2007; 107:2891-2959.
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7. Gheshlaghi ZN, Riazi GH, Ahmadian S, Ghafari M, Mahinpour R. Toxicity and interaction of titanium dioxide nanoparticles with microtubule protein. Acta Biochim Biophys Sin 2008; 40:777-782.
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10. Liu H, Ma L, Zhao J, Liu J, Yan J, Ruan J, et al. Biochemical toxicity of nano-anatase TiO2 particles in mice. Biol Trace Elem Res 2009; 129:170-180.
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11. Mohammadipour A, Fazel A, Haghir H, Motejaded F, Rafatpanah H, Zabihi H, et al. Maternal exposure to titanium dioxide nanoparticles during pregnancy; impaired memory and decreased hippocampal cell proliferation in rat offspring. Environ Toxicol Pharmacol 2014; 37:617-625.
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12. Mohammadipour A, Hosseini M, Fazel A. The effects of exposure to titanium dioxide nanoparticles during lactation period on learning and memory of rat offspring. Toxicol Ind Health 2016; 32: 221-228.
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17. Hu R, Gong X, Duan Y, Li N, Che Y, Cui Y, et al. Neurotoxicological effects and the impairment of spatial recognition memory in mice caused by exposure to TiO2 nanoparticles. Biomaterials 2010; 31:8043-8050.
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18. Lotfipour AK, Wharton S, Schwarz ST. High resolution magnetic susceptibility mapping of the substantia nigra in Parkinson’s disease. J Magn Reson Imaging 2012; 35:48-55.
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23. Ahn S, Song TJ, Park SU, Jeon S, Kim J, Oh J, et al. Effects of a combination treatment of KD5040 and L-dopa in a mouse model of Parkinson’s disease. BMC Complement Altern Med 2017; 17:220-232.
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24. Jalayeri-Darbandi Z, Rajabzadeh A, Hosseini M, Beheshti F, Ebrahimzadeh-bideskan AR. The effect of methamphetamine exposure during pregnancy and lactation on hippocampal doublecortin expression, learning and memory of rat offspring. Anat Sci Int 2018; 93: 351-363.
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25. Mohammadzadeh E, Nikravesh MR, Jalali M, Fazel A, Ebrahimi V, Ebrahimzadeh-bideskan A. Immunohistochemical study of type III collagen expression during pre and post-natal rat skin morphogenesis. Iran J Basic Med Sci 2014; 17:196-200.
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26. Baghishani F, Mohammadipour A, Hosseinzadeh H, Hosseini M, Ebrahimzadeh-bideskan A. The effects of tramadol administration on hippocampal cell apoptosis, learning and memory in adult rats and neuroprotective effects of crocin. Metab Brain Dis 2018; 33:907-916.
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27. 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.
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28. Pourzaki M, Homayoun M, Sadeghi S, Seghatoleslam M, Hosseini M, Ebrahimzadeh-bideskan A. Preventive effect of coriandrum sativum on neuronal damages in pentylentetrazole-induced seizure in rats. Avicenna J Phytomed 2017; 7:116-128.
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29. Hu Q, Guo F, Zhao F, Fuet Z. Effects of titanium dioxide nanoparticles exposure on parkinsonism in zebrafish larvae and PC12. Chemosphere 2017; 173:373-379.
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30. Disdier C, Devoy J, Cosnefroy A, Chalansonnet M, Herlin-Boime N, Brun E, et al. Tissue bio distribution of intravenously administrated titanium dioxide nanoparticles revealed blood-brain barrier clearance and brain inflammation in rat. Part Fibre Toxicol 2015; 12:27-36.
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48
49. Ebrahimzadeh-bideskan A, Mohammadipour A, Fazel A, Haghir H, Rafatpanah H, Hosseini M, et al. Maternal exposure to titanium dioxide nanoparticles during pregnancy and lactation alters offspring hippocampal mRNA BAX and Bcl-2 levels, induces apoptosis and decreases neurogenesis. Exp Toxicol Pathol 2017; 69:329-337.
49
ORIGINAL_ARTICLE
Evaluation of the neuroprotective, anticonvulsant, and cognition-improvement effects of apigenin in temporal lobe epilepsy: Involvement of the mitochondrial apoptotic pathway
Objective(s): Cognitive deficit is a common problem in epilepsy. A major concern emergent from the use of antiepileptic drugs includes their side effects on learning and memory. Herbal medicine is considered a complementary and alternative therapy in epilepsy. Apigenin is a safe flavone with antioxidant properties. However, there is little information about the beneficial effect of apigenin on cognition in epilepsy. Materials and Methods: For evaluating the anticonvulsant effect of apigenin in the kainite temporal epilepsy model, apigenin was orally administered at 50 mg/kg for six days. Reference and working memory were examined via the Morris water maze and Y-maze task spontaneously. Results: Results showed that apigenin had significant anticonvulsant activity (P<0.01) and restored the memory-deficit induced by kainic acid (P<0.05). Furthermore, apigenin significantly increased the number of living neurons in the hilus (P<0.001). Immunohistochemical analysis showed that apigenin reduced the release of cytochrome c (P<0.01), suggesting an inhibitory role in the intrinsic apoptotic pathway. Conclusion: These results suggest that apigenin restores memory impairment via anticonvulsant and neuroprotective activity.
https://ijbms.mums.ac.ir/article_13163_7cf851177534a02d69c45dd9ea6bb49d.pdf
2019-07-01
752
758
10.22038/ijbms.2019.33892.8064
Apigenin
Anticonvulsant
Cognition
Cytochrome c
Neuroprotection
Temporal lobe epilepsy
Paria
Hashemi
pr.hashemi@yahoo.com
1
Department of Physiology, School of Medicine and Cellular and Molecular Research Centre, Iran University of Medical Sciences, Tehran, Iran
AUTHOR
Javad
Fahanik Babaei
fahanikbabaei.j@iums.ac.ir
2
Physiology Research Centre, Iran University of Medical Sciences, Tehran, Iran
AUTHOR
Somayeh
Vazifehkhah
somayeh.vazifekhah@yahoo.com
3
Department of Physiology, School of Medicine and Cellular and Molecular Research Centre, Iran University of Medical Sciences, Tehran, Iran
AUTHOR
Farnaz
Nikbakht
farnazinikbakht@yahoo.com
4
Cellular and Molecular Research Center, School of Medicine, Iran University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
1. Giblin KA, Blumenfeld H. Is epilepsy a preventable disorder? New evidence from animal models. Neuroscientist 2010; 16:253-275.
1
2. Kuruba R, Hattiangady B, Shetty AK. Hippocampal neurogenesis and neural stem cells in temporal lobe epilepsy. Epilepsy Behav. 2009; 14:65-73.
2
3. Pauli E, Hildebrandt M, Romstöck J, Stefan H, Blümcke I. Deficient memory acquisition in temporal lobe epilepsy is predicted by hippocampal granule cell loss. Neurology 2006; 67:1383-1389.
3
4. Lévesque M, Avoli M. The kainic acid model of temporal lobe epilepsy. Neurosci Biobehav Rev 2013; 37:2887-2899.
4
5. Helmstaedter C, Elger C. Chronic temporal lobe epilepsy: a neurodevelopmental or progressively dementing disease? Brain 2009; 132:2822-2830.
5
6. Höller Y, Trinka E. What do temporal lobe epilepsy and progressive mild cognitive impairment have in common? Front Syst Neurosci 2014; 8.
6
7. Kotloski R, Lynch M, Lauersdorf S, Sutula T. Repeated brief seizures induce progressive hippocampal neuron loss and memory deficits. Prog Brain Res 2002; 135:95-110.
7
8. Cock H. The role of mitochondria in status epilepticus. Epilepsia 2007; 48:24-27.
8
9. Dalic L, Cook MJ. Managing drug-resistant epilepsy: challenges and solutions. Neuropsychiatr Dis Treat 2016; 12:2605-2616.
9
10. Meador KJ. Cognitive and memory effects of the new antiepileptic drugs. Epilepsy Res 2006; 68:63-67.
10
11. Lasoń W, Leśkiewicz M. Effect of plant polyphenols on seizures–animal studies. Journal of Epileptology 2013; 21:79-87.
11
12. Tang D, Chen K, Huang L, Li J. Pharmacokinetic properties and drug interactions of apigenin, a natural flavone. Expert Opin Drug Metab Toxicol 2017; 13:323-330.
12
13. Ali F, Rahul, Naz F, Jyoti S, Siddique YH. Health functionality of apigenin: A review. International Journal of Food Properties 2017; 20:1197-1238.
13
14. Zhao L, Wang J-L, Liu R, Li X-X, Li J-F, Zhang L. Neuroprotective, anti-amyloidogenic and neurotrophic effects of apigenin in an Alzheimer’s disease mouse model. Molecules 2013; 18:9949-9965.
14
15. Zheng P-W, Chiang L-C, Lin C-C. Apigenin induced apoptosis through p53-dependent pathway in human cervical carcinoma cells. Life Sci 2005; 76:1367-1379.
15
16. Shukla S, Gupta S. Molecular targets for apigenin-induced cell cycle arrest and apoptosis in prostate cancer cell xenograft. Mol Cancer Ther. 2006; 5:843-852.
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17. Way T-D, Kao M-C, Lin J-K. Apigenin induces apoptosis through proteasomal degradation of HER2/neu in HER2/neu-overexpressing breast cancer cells via the phosphatidylinositol 3-kinase/Akt-dependent pathway. J Biol Chem 2004; 279:4479-4489.
17
18. Hu J, Li Z, Xu L-t, Sun A-j, Fu X-y, Zhang L, et al. Protective effect of apigenin on ischemia/reperfusion injury of the isolated rat heart. Cardiovasc Toxicol 2015; 15:241-249.
18
19. Dang Y, Li Z, Luo B, Pan L, Wei Q, Zhang Y. Protective effects of apigenin against acrylonitrile-induced subchronic sperm injury in rats. Food Chem Toxicol 2017; 109:517-525.
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20. Schmued LC, Hopkins KJ. Fluoro-Jade B: a high affinity fluorescent marker for the localization of neuronal degeneration. Brain Res 2000; 874:123-130.
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21. Liang H, Sonego S, Gyengesi E, Rangel A, Niedermayer G, Karl T, et al. Anti-inflammatory and neuroprotective effect of apigenin: studies in the GFAP-IL6 mouse model of chronic neuroinflammation. Free Radic Biol Med 2017; 108:S10.
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22. Taupin P. Apigenin and related compounds stimulate adult neurogenesis: Mars, Inc., the Salk Institute for Biological Studies: WO2008147483. Expert Opin Ther Pat 2009; 19:523-527.
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24. Höller Y, Trinka E. What do temporal lobe epilepsy and progressive mild cognitive impairment have in common? Front Syst Neurosci 2014; 8:58.
24
25. Han J-Y, Ahn S-Y, Kim C-S, Yoo S-K, Kim S-K, Kim H-C, et al. Protection of apigenin against kainate-induced excitotoxicity by anti-oxidative effects. Biol Pharm Bull 2012; 35:1440-1446.
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26. Gazola AC, Costa GM, Castellanos L, Ramos FA, Reginatto FH, Lima T, et al. Involvement of GABAergic pathway in the sedative activity of apigenin, the main flavonoid from Passiflora quadrangularis pericarp. Revista Brasileira de Farmacognosia 2015; 25:158-163.
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29. Aiyer RS, Nath JR. Mechanisms of memory deficit in temporal lobe epilepsy. Neropathology 2011; 22:6052-6061.
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30
ORIGINAL_ARTICLE
Rhopalurus junceus scorpion venom induces antitumor effect in vitro and in vivo against a murine mammary adenocarcinoma model
Objective(s): In Cuba the endemic scorpion species Rhopalurus junceus has been used in traditional medicine for cancer treatment and related diseases. However there is no scientific evidence about its therapeutic potential for cancer treatment. The aim of the study was to determine the antitumor effect of scorpion venom against a murine mammary adenocarcinoma F3II. Materials and Methods: The cytotoxic activity was determined by MTT assay with venom concentrations ranging from 0.1–1 mg/ml. Apoptosis was determined by RT-PCR and flow cytometry. Toxic effect in healthy animals and tumor growth kinetics in F3II bearing-mice were evaluated by using scorpion venom doses (0.2; 0.8; 3.2 mg/kg) after one and ten injections respectively by the intraperitoneal route. Results: Scorpion venom induced a significant cytotoxic effect (P<0.05) in F3II cells in a concentration-dependent manner. The cell death event involves the apoptotic pathway due to up-regulation of pro-apoptotic genes (p53, bax), down-regulation of antiapoptotic gene (bcl-2), and 33% of Annexin V+/PI- cells at early apoptosis and 10.21% of Annexin V+/PI+ cells at late apoptosis. Scorpion venom induced significant inhibition of tumor progression (P<0.05) in F3II bearing-mice in a dose-dependent manner. The antitumor effect was confirmed due to dose-dependent reduction of Ki-67 and CD31 proteins present in tumor tissue. Conclusion: Evidence indicates that scorpion venom can be an attractive natural product for deep investigation and developing a novel therapeutic agent for breast cancer treatment.
https://ijbms.mums.ac.ir/article_13100_8a2b9b6bc6cbc66f8d50819fd62ba3f1.pdf
2019-07-01
759
765
10.22038/ijbms.2019.33308.7956
Antitumor
Apoptosis
Cytotoxicity
Murine mammary adenocarcinoma
Scorpion venom
Alexis
Díaz-García
alediaz@ipk.sld.cu
1
Research Department, Laboratories of Biopharmaceuticals and Chemistries Productions (LABIOFAM), Havana, Cuba
LEAD_AUTHOR
Jenny Laura
Ruiz-Fuentes
jlaura@ipk.sld.cu
2
Microbiology Department, Tropical Medicine Institute “Pedro Kouri”, Havana, Cuba
AUTHOR
Yahima
Frión-Herrera
yahima81@gmail.com
3
Department of Pharmaceutical Science, Padova University, Italy
AUTHOR
Arianna
Yglesias-Rivera
ariannay@ipk.sld.cu
4
Research Department, Laboratories of Biopharmaceuticals and Chemistries Productions (LABIOFAM), Havana, Cuba
AUTHOR
Yanelis
Riquenez Garlobo
yanelis.riquenez@labiofam.cu
5
Research Department, Laboratories of Biopharmaceuticals and Chemistries Productions (LABIOFAM), Havana, Cuba
AUTHOR
Hermis
Rodríguez Sánchez
hermis@ipk.sld.cu
6
Microbiology Department, Tropical Medicine Institute “Pedro Kouri”, Havana, Cuba
AUTHOR
Juan C
Rodríguez Aurrecochea
jucara@infomed.sld.cu
7
Investigation Department, Laboratory of Experimental pathology, Oncology and Radiobiology National Institute, Havana, Cuba
AUTHOR
Ledys X
López Fuentes
ledy@ipk.sld.cu
8
Laboratory of pathology, Tropical Medicine Institute “Pedro Kouri”, Havana, Cuba
AUTHOR
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24. Das Gupta S, Debnath A, Saha A, Giri B, Tripathi G, Vedasiromoni J, et al. Indian black scorpion (Heterometrus bengalensis Koch) venom induced antiproliferative and apoptogenic activity against human leukemic cell lines U937 and K562. Leuk Res 2007; 31:817-823.
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40
ORIGINAL_ARTICLE
Kinetics of T cell response in the testes and CNS during experimental autoimmune encephalomyelitis: Simultaneous blood-brain and -testis barrier permeability?
Objective(s): Multiple sclerosis (MS) and its animal model, experimental autoimmune encephalomyelitis (EAE), are regarded as autoimmune diseases of the central nervous system (CNS). The CNS, testes, and eyes are immune privileged sites. It was initially presumed that ocular involvement in EAE and infertility in MS are neural-mediated. However, inflammatory molecules have been detected in the eyes of animals affected by EAE. It prompted us to investigate if the testes may also be targeted by immune response during EAE.Materials and Methods: kinetics of T cell response was investigated in the CNS and testes in EAE at different clinical scores. IFN-γ, IL-4, IL-17, and FoxP3 mRNA expressions were considered as representatives of Th1, Th2, Th17, and Treg, respectively.Results: In CNS, IL-17 and IFN-γ were initially up-regulated and attenuated at the late phase of the disease. IL-4 and FoxP3 were markedly down-regulated, but IL-4 was then up-regulated at the late phase of the disease. In the testes, IFN-γ and IL-17 were diminished but increased at the late phase of the disease. FoxP3 was gradually increased from the initial step to the peak of the disease. IL-17/ IFN-γ showed a similar pattern between the CNS and testes. However, FoxP3 and IL-4 expression appeared to have different timing patterns in the CNS and testes.Conclusion: Given the permeability in blood-retina/brain/CSF barrier by complete Freund’s adjuvant, the pattern of T cells may be changed in the testes during EAE as a consequence of the blood-testis barrier permeability. More research is required to explore the connection between immune privileged organs.
https://ijbms.mums.ac.ir/article_13165_720c40ff934feb61af9b9d413cafa763.pdf
2019-07-01
766
773
10.22038/ijbms.2019.34510.8185
Barrier
CFA
CNS
EAE
Immune privilege
T cell
Testes
Nafiseh
Pakravan
nafiseh.pakravan@gmail.com
1
Division of Immunology, Medical School, Alborz University of Medical Sciences, Karaj, Iran
LEAD_AUTHOR
Ameneh
Ghaffarinia
hiva.heaven63@gmail.com
2
Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
AUTHOR
Shahram
Parvaneh
shparvaneh79@gmail.com
3
Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
AUTHOR
Cyrus
Jalili
cjalili@yahoo.com
4
Department of Anatomy, Medical School, Kermanshah University of Medical Sciences, Kermanshah, Iran
AUTHOR
Farhad
Riazirad
riazirad@yahoo.com
5
Department of Immunology, Pasture Institute of Iran, Tehran, Iran
AUTHOR
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45. Veräjänkorva E, Setälä N, Teros T, Salmi AA, Pöllänen P. Testicular-associated immune deviation: flushing of the testicular lymph sinusoids induces immunosuppression and inhibits formation of EAE in SJL mice. Scand J Immunol 2002; 55: 478-483.
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50. Flake NM, Hermanstyne TO, Gold MS. Testosterone and estrogen have opposing actions on inflammation-induced plasma extravasation in the rat temporomandibular joint. Am J Physiol Regul Integr Comp Physiol 2006; 291: R343-R348.
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54
ORIGINAL_ARTICLE
Sesquiterpene fractions of Artemisia plants as potent inhibitors of inducible nitric oxide synthase and cyclooxygenase-2 expression
Objective(s): Artemisia species are important medicinal plants throughout the world. Some species are traditionally used for their anti-inflammatory effect. The present study was designed to isolate sesquiterpene fractions from several Artemisia species and evaluate their anti-inflammatory activities on key mediators and signaling molecules involved in regulation of inflammation.Materials and Methods: Sesquiterpene fractions were prepared from several Artemisia species using the Herz-Högenauer technique. Lipopolysaccharide (LPS)-stimulated J774A.1 macrophages were exposed to isolated fractions. Their possible cytotoxic effect was examined using MTT assay. In addition, nitric oxide (NO) release was measured using Griess method and prostaglandin E2 (PGE2) level was determined by enzyme-linked immunosorbent assay (ELISA). Moreover, protein expression of pro-inflammatory enzymes, inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) were investigated using Western blot analysis. Results: Nitric oxide level produced by LPS-primed macrophages was significantly decreased with all prepared fractions in a dose-dependent manner. Saturated sesquiterpene lactones-rich species (Artemisia kopetdaghensis, Artemisia santolina, Artemisia sieberi) showed the highest suppressive activity on NO and PGE2 production via suppression of iNOS and COX-2 expression. Fractions bearing unusual (Artemisia fragrans and Artemisia absinthium) and unsaturated sesquiterpene lactones (Artemisia ciniformis) possess less modulatory effect on PGE2 production and COX-2 expression. Conclusion: It can be concluded that some of the medicinally beneficial effects attributed to Artemisia plants may be associated with the inhibition of pro-inflammatory signaling pathways. However, these effects could be dependent on the type of their sesquiterpene content. These findings also introduce new Artemis species cultivated in Iran as a useful anti-inflammatory agents.
https://ijbms.mums.ac.ir/article_13104_0db8febcbf8b1bde714337108e737247.pdf
2019-07-01
774
780
10.22038/ijbms.2019.34792.8249
Artemisia
Asteraceae
Sesquiterpene lactone fraction
Macrophage
Inflammation
Shahrzad
Zamani
shahrzad.zamanitaghizadehrabe@monash.edu
1
Immunology Research Center, Bu-Ali Research Institute, School of Medicine, Mashhad University of Medical Science, Mashhad, Iran
AUTHOR
Ahmad
Emami
emamia@mums.ac.ir
2
Department of Pharmacognosy, School of Pharmacy; Mashhad University of Medical Science, Mashhad, Iran
AUTHOR
Mehrdad
Iranshahi
iranshahim@mums.ac.ir
3
Biotechnology Research Center, Mashhad University of Medical Science, Mashhad, Iran
AUTHOR
Shahin
Zamani Taghizadeh Rabe
zamani.imnl@gmail.com
4
Immunology Research Center, Bu-Ali Research Institute, School of Medicine, Mashhad University of Medical Science, Mashhad, Iran
AUTHOR
Mahmoud
Mahmoudi
mahmoudim@mums.ac.ir
5
Immunology Research Center, Bu-Ali Research Institute, School of Medicine, Mashhad University of Medical Science, Mashhad, Iran
LEAD_AUTHOR
1. Salmaki Y, Bendiskby M, Heubl G. Molecular phylogeny confirms the placement of enigmatic Stachys persepolitana in Lamium (Lamiaceae; subfam. Lamioideae) 2015; 192:13.
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2. Emami SA, Aghazari F, Johartchi MR. Les phanérogames endémiques de la flore d’Iran. Téhéran: L’Université de Téhéran des Sciences Médicales, Institut des Études d’Histoire de la Médecine, de Médecine Islamique et de Médecine Complémentaire 2011.
2
3. Zargaran A, Mehdizadeh A, Zarshenas MM, Mohagheghzadeh A. Avicenna (980-1037 AD). J Neurol 2012; 259:389-390.
3
4. Emami SA, Zamanai Taghizadeh Rabe S, Ahi A, Mahmoudi M. Inhibitory activity of eleven Artemisia species from Iran against leishmania major parasites. Iran J Basic Med Sci 2012; 15:807-811.
4
5. Emami S, Zamani Taghizadeh Rabe S, Ahi A, Mahmoudi M, Tabasi N. Study the cytotoxic and pro-apoptotic activity of Artemisia Annua extracts. Pharmacologyonline 2009; 3:1062-1069.
5
6. Taghizadeh Rabe SZ, Mahmoudi M, Ahi A, Emami SA. Antiproliferative effects of extracts from Iranian Artemisia species on cancer cell lines. Pharm Biol 2011; 49:962-969.
6
7. Mahmoudi M, Zamani Taghizadeh Rabe S, Ahi A, Emami SA. Evaluation of the cytotoxic activity of different Artemisia Khorassanica samples on cancer cell lines. Pharmacologyonline 2009; 2:778-286.
7
8. Kordali S, Cakir A, Mavi A, Kilic H, Yildirim A. Screening of chemical composition and antifungal and antioxidant activities of the essential oils from three Turkish Artemisia species. J Agric Food Chem 2005; 53:1408-1416.
8
9. Ahn H, Kim JY, Lee HJ, Kim YK, Ryu JH. Inhibitors of inducible nitric oxide synthase expression fromartemisia iwayomogi. Arch Pharm Res 2003; 26:301-305.
9
10. Noori S, Naderi GA, Hassan ZM, Habibi Z, Bathaie SZ, Hashemi SMM. Immunosuppressive activity of a molecule isolated from Artemisia annua on DTH responses compared with cyclosporin A. Int Immunopharmacol 2004; 4:1301-1306.
10
11. Emami SA, Taghizadeh Rabe SZ, Iranshahi M, Ahi A, Mahmoudi M. Sesquiterpene lactone fraction from Artemisia khorassanica inhibits inducible nitric oxide synthase and cyclooxygenase-2 expression through the inactivation of NF-κB. Immunopharmacol Immunotoxicol 2010; 32:688-695.
11
12. Rustaiyan A, Masoudi S. Chemical constituents and biological activities of Iranian Artemisia species. Phytochem Lett 2011; 4:440-447.
12
13. Konkimalla VB, Blunder M, Korn B, Soomro SA, Jansen H, Chang W, et al. Effect of artemisinins and other endoperoxides on nitric oxide-related signaling pathway in RAW 264.7 mouse macrophage cells. Nitric Oxide 2008; 19:184-191.
13
14. Choi EJ, Lee S, Chae JR, Lee HS, Jun CD, Kim SH. Eupatilin inhibits lipopolysaccharide-induced expression of inflammatory mediators in macrophages. Life Sci 2011; 88:1121-1126.
14
15. Han S, Lee JH, Kim C, Nam D, Chung WS, Lee SG, et al. Capillarisin inhibits iNOS, COX-2 expression, and proinflammatory cytokines in LPS-induced RAW 264.7 macrophages via the suppression of ERK, JNK, and NF-κB activation. Immunopharmacol Immunotoxicol 2013; 35:34-42.
15
16. Kim HJ, Jang SI, Kim YJ, Chung HT, Yun YG, Kang TH, et al. Scopoletin suppresses pro-inflammatory cytokines and PGE2 from LPS-stimulated cell line, RAW 264.7 cells. Fitoterapia 2004; 75:261-266.
16
17. Kröncke K, Fehsel K, Kolb-Bachofen V. Inducible nitric oxide synthase in human diseases. Clin Exp Immunol 1998; 113:147.
17
18. Lee SH, Soyoola E, Chanmugam P, Hart S, Sun W, Zhong H, et al. Selective expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide. J Biol Chem 1992; 267:25934-25938.
18
19. Spitzer JA, Zheng M, Kolls JK, Vande Stouwe C, Spitzer JJ. Ethanol and LPS modulate NF-kappaB activation, inducible NO synthase and COX-2 gene expression in rat liver cells in vivo. Front Biosci 2002; 7:99-108.
19
20. Hori M, Kita M, Torihashi S, Miyamoto S, Won KJ, Sato K et al. Upregulation of iNOS by COX-2 in muscularis resident macrophage of rat intestine stimulated with LPS. Am J Physiol Gastrointest Liver Physiol 2001; 280:930-938.
20
21. Suthar SK, Sharma M. Recent developments in chimeric NSAIDs as safer anti-inflammatory agents. Med Res Rev 2015; 35:341-407.
21
22. Iranshahi M, Emami SA, Mahmoud-Soltani M. Detection of sesquiterpene lactones in ten Artemisia species population of Khorasan provinces. Iran J Basic Med Sci 2007; 10:183-188.
22
23. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunological Methods 1983; 65:55-63.
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24
25. Zamanai Taghizadeh Rabe S, Iranshahi M, Rastin M, Tabasi N, Mahmoudi M. In vitro immunomodulatory properties of a sesquiterpene lactone-bearing fraction from Artemisia khorassanica. J Immunotoxicol 2015; 12:223-230.
25
26. Kim SF, Huri DA, Snyder SH. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Sci 2005; 310:1966-1970.
26
ORIGINAL_ARTICLE
Effects of nano-copper on maize yield and inflammatory response in mice
Objective(s): Copper (Cu) is an essential dietary supplement in animal feeds, which plays an important role in maintaining the balance of all living organisms. Copper nanoparticles (nCu) participate in catalysing activities of multiple antioxidant/defensive enzymes and exerts pro-inflammatory and pro-apoptotic effects on systemic organs and tissues. The present study explored whether nCu affects maize growth and yield and grain mineral nutrients as well as physiological functions in mice. Materials and Methods: Maize seeds were treated with nCu (20 mg/kg and 1000 mg/kg dry weight (DW)) and their grain productions were used for mouse feed. For testing of autoimmune response, mice were treated with nCu at concentration of 2 mg/l and 1000 mg/l and ultimately serum biochemical indicators, numbers and activation of immune cells infiltrated in mouse spleens were examined. Results: Treatment of maize seeds with nCu at dose of 20 mg/kg DW, but not 1000 mg/kg DW enhanced germination rate, plant growth and grain yield as well as grain mineral nutrients as compared to control group. Importantly, administration of mice with 1000 mg/l nCu resulted in their morphological change due to excessive accumulation of nCu in liver and blood, leading to inflammatory responses involved in upregulated expression of serum biochemical indicators of liver and kidney as well as increased infiltration and activation of splenic immune cells. Conclusion: nCu concentration at 20 mg/kg DW facilitated the morphological and functional development of maize plants, whose production was safe to feed mice.
https://ijbms.mums.ac.ir/article_13016_8f41c852ccc368c06f03687abe4cb502.pdf
2019-07-01
781
788
10.22038/ijbms.2019.35787.8526
ALT
AST
Copper
Leukocytes
Maize
Le
Hien
hienlethu@igr.ac.vn
1
Institute of Genome Research, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Hanoi, Vietnam
AUTHOR
Phi
Trang
trangphi@igr.ac.vn
2
Institute of Genome Research, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Hanoi, Vietnam
AUTHOR
Pham
Phuong
camphuongmd@yahoo.com
3
Nuclear Medicine and Oncology Center, Bach Mai Hospital, 78 Giai Phong, Hanoi, Vietnam
AUTHOR
Pham
Tam
xtltam76@gmail.com
4
Hanoi Open University, 101 Nguyen Hien, Hai Ba Trung, Hanoi, Vietnam
AUTHOR
Nguyen
Xuan
ntxuan@igr.ac.vn
5
Institute of Genome Research, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Hanoi, Vietnam
LEAD_AUTHOR
1. Uauy R, Maass A, and Araya M. Estimating risk from copper excess in human populations. Am J Clin Nutr 2008; 88: 867S-71S.
1
2. Galhardi CM, Diniz YS, Faine LA, Rodrigues HG, Burneiko RC, Ribas BO, et al. Toxicity of copper intake: lipid profile, oxidative stress and susceptibility to renal dysfunction. Food Chem Toxicol 2004; 42: 2053-2060.
2
3. Liu L, Geng X, McDermott J, Shen J, Corbin C, Xuan S, et al. Copper deficiency in the lungs of TNF-alpha transgenic mice. Front Physiol 2016; 7: 234.
3
4. Yen CF, Harischandra DS, Kanthasamy A, and Sivasankar S. Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity. Sci Adv 2016; 2: e1600014.
4
5. Rout JR, Ram SS, Das R, Chakraborty A, Sudarshan M, and Sahoo SL. Copper-stress induced alterations in protein profile and antioxidant enzymes activities in the in vitro grown Withania somnifera L. Physiol Mol Biol Plants 2013; 19: 353-61.
5
6. Kim BE, Nevitt T, and Thiele DJ. Mechanisms for copper acquisition, distribution and regulation. Nat Chem Biol 2008; 4: 176-85.
6
7. Fitzgerald DJ. Safety guidelines for copper in water. Am J Clin Nutr 1998; 67: 1098S-1102S.
7
8. Ognik K, Stepniowska A, Cholewinska E, and Kozlowski K. The effect of administration of copper nanoparticles to chickens in drinking water on estimated intestinal absorption of iron, zinc, and calcium. Poult Sci 2016; 95: 2045-2051.
8
9. Zhai Y, Hunting ER, Wouterse M, Peijnenburg W, and Vijver MG. Importance of exposure dynamics of metal-based nano-ZnO, -Cu and -Pb governing the metabolic potential of soil bacterial communities. Ecotoxicol Environ Saf 2017; 145: 349-358.
9
10. Li S, Zhao H, Wang Y, Shao Y, Li J, Liu J, et al. The inflammatory responses in Cu-mediated elemental imbalance is associated with mitochondrial fission and intrinsic apoptosis in Gallus gallus heart. Chemosphere 2017; 189: 489-497.
10
11. Chen GF, Sudhahar V, Youn SW, Das A, Cho J, Kamiya T, et al. Copper transport protein antioxidant-1 promotes inflammatory neovascularization via chaperone and transcription factor function. Sci Rep 2015; 5: 14780.
11
12. Xuan NT, Wang X, Nishanth G, Waisman A, Borucki K, Isermann B, et al. A20 expression in dendritic cells protects mice from LPS-induced mortality. Eur J Immunol 2015; 45: 818-828.
12
13. Meng H, Chen Z, Xing G, Yuan H, Chen C, Zhao F, et al. Ultrahigh reactivity provokes nanotoxicity: explanation of oral toxicity of nano-copper particles. Toxicol Lett 2007; 175: 102-110.
13
14. Xuan NT, Shumilina E, Schmid E, Bhavsar SK, Rexhepaj R, Gotz F, et al. Role of acidic sphingomyelinase in thymol-mediated dendritic cell death. Mol Nutr Food Res 2010; 54: 1833-1841.
14
15. Keswani T, Mitra S, and Bhattacharyya A. Copper-induced immunotoxicity involves cell cycle arrest and cell death in the liver. Environ Toxicol 2015; 30: 411-21.
15
16. Xu P, Xu J, Liu S, and Yang Z. Nano copper induced apoptosis in podocytes via increasing oxidative stress. J Hazard Mater 2012; 241-242: 279-286.
16
17. Subramanian I, Vanek ZF, and Bronstein JM. Diagnosis and treatment of Wilson‘s disease. Curr Neurol Neurosci Rep 2002; 2: 317-323.
17
18. Worthington KL, Adamcakova-Dodd A, Wongrakpanich A, Mudunkotuwa IA, Mapuskar KA, Joshi VB, et al. Chitosan coating of copper nanoparticles reduces in vitro toxicity and increases inflammation in the lung. Nanotechnology 2013; 24: 395101.
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19. Adrees M, Ali S, Rizwan M, Ibrahim M, Abbas F, Farid M, et al. The effect of excess copper on growth and physiology of important food crops: a review. Environ Sci Pollut Res Int 2015; 22: 8148-8162.
19
20. Merlos MA, Zitka O, Vojtech A, Azcon-Aguilar C, and Ferrol N. The arbuscular mycorrhizal fungus Rhizophagus irregularis differentially regulates the copper response of two maize cultivars differing in copper tolerance. Plant Sci 2016; 253: 68-76.
20
21. Saharan V, Sharma G, Yadav M, Choudhary MK, Sharma SS, Pal A, et al. Synthesis and in vitro antifungal efficacy of Cu-chitosan nanoparticles against pathogenic fungi of tomato. Int J Biol Macromol 2015; 75: 346-353.
21
22. Choudhary RC, Kumaraswamy RV, Kumari S, Sharma SS, Pal A, Raliya R, et al. Cu-chitosan nanoparticle boost defense responses and plant growth in maize (Zea mays L.). Sci Rep 2017; 7: 9754.
22
23. Ngo QB, Dao TH, Nguyen HC, Tran XT, Nguyen TTV, Khuu TD, et al. Effects of nanocrystalline powders (Fe, Co and Cu) on the germination, growth, crop yield and product quality of soybean (Vietnamese species DT-51). Adv Nat Sci-NanoSci 2014; 5: 1-7.
23
24. Hoe PT, Mai NC, Lien LQ, Ban NK, Minh CV, Chau NH, et al. Germination responses of soybean seeds under Fe, ZnO, Cu and Co nanoparticle treatments. Int J Agric Biol 2018; 20: 1562‒1568.
24
25. Van loon JC. Analytical Atomic Absorption Spectroscopy: Selected methods. Academic press, Inc; Ltd; London 1996.
25
26. Munzuroglu O and Geckil H. Effects of metals on seed germination, root elongation, and coleoptile and hypocotyl growth in Triticum aestivum and Cucumis sativus. Arch Environ Contam Toxicol 2002; 43: 203-13.
26
27. Zhang H, Wu X, Mehmood K, Chang Z, Li K, Jiang X, et al. Intestinal epithelial cell injury induced by copper containing nanoparticles in piglets. Environ Toxicol Pharmacol 2017; 56: 151-156.
27
28. Manna P, Ghosh M, Ghosh J, Das J, and Sil PC. Contribution of nano-copper particles to in vivo liver dysfunction and cellular damage: role of IkappaBalpha/NF-kappaB, MAPKs and mitochondrial signal. Nanotoxicology 2012; 6: 1-21.
28
29. Ivask A, Juganson K, Bondarenko O, Mortimer M, Aruoja V, Kasemets K, et al. Mechanisms of toxic action of Ag, ZnO and CuO nanoparticles to selected ecotoxicological test organisms and mammalian cells in vitro: a comparative review. Nanotoxicology 2014; 8 Suppl 1: 57-71.
29
ORIGINAL_ARTICLE
Effects of silibinin on hepatic warm ischemia-reperfusion injury in the rat model
Objective(s): Liver ischemia-reperfusion injuries (I/RI) are typically the main causes of liver dysfunction after various types of liver surgery especially liver transplantation. Radical components are the major causes of such direct injuries. We aimed to determine the beneficial effects of silibinin, a potent radical scavenger on liver I/RI.Materials and Methods: Thirty-two rats were divided into 4 groups. Group I: VEHICLE, the rats underwent laparotomy and received DMSO, group II: SILI, laparotomy was done and silibinin was administered. Group III: I/R, the rats received DMSO and were subjected to a liver I/R procedure and group IV: I/R+SILI, the animals underwent the I/R procedure and received silibinin. After 1 hr of ischemia followed by 3 hr reperfusion, blood was collected to evaluate the serum marker of liver injuries. Hepatic tissue was harvested to investigate glycogen content, histological changes, and vasoregulatory gene expression.Results: Results showed that serum AST, ALT, LDH, GGT, ALP, and hyaluronic acid (HA) increased significantly in I/R group compared with the VEHICLE group. Silibinin reduced this elevation except for GGT. Silibinin inhibited hepatocyte vacuolization and degeneration, endothelium damages, sinusoidal congestion and inflammation, and glycogen depletion during I/R. ET-1 mRNA was overproduced in the I/R group compared with the VEHICLE group which was decreased by silibinin. KLF2 and eNOS expression was reduced during I/R compared with the VEHICLE group. Silibinin elevated KLF2 expression but had no meaningful effect on eNOS expression.Conclusion: Silibinin protected the liver from I/RI. Silibinin could improve liver circulation by preventing sinusoidal congestion, inflammation, and perhaps modification of the vasoregulatory gene expression.
https://ijbms.mums.ac.ir/article_13011_ce35cb862ebae281f61ab0b2999c2704.pdf
2019-07-01
789
796
10.22038/ijbms.2019.34967.8313
eNOS
ET-1
KLF2
Liver Ischemia/reperfusion
Silibinin
Vahid
Akbari-Kordkheyli
akbari.vahid89@gmail.com
1
Student Research Committee, Mazandaran University of Medical Sciences, Sari, Iran
AUTHOR
Soheil
Azizi
soheil_azizi@yahoo.com
2
Department of Laboratory Medicine, Faculty of Allied Medical Sciences, Mazandaran University of Medical Sciences, Sari, Iran
AUTHOR
Abbas
Khonakdar-Tarsi
khonakdarab@gmail.com
3
Department of Biochemistry, Biophysics and Genetics, Cellular and molecular biology research center, Faculty of Medicine, Mazandaran University of Medical Sciences, Sari, Iran
LEAD_AUTHOR
1. MorenoGonzález E, García G, Ía I, Sanz RG, González‐Pinto I, Segurola CL, et al. Liver transplantation in patients with thrombosis of the portal, splenic or superior mesenteric vein. Br J Surg. 1993;80:81-85.
1
2. Montalvo-Jave EE, Escalante-Tattersfield T, Ortega-Salgado JA, Piña E, Geller DA. Factors in the pathophysiology of the liver ischemia-reperfusion injury. J Surg Res. 2008;147:153-159.
2
3. Akbari Kordkheyli V, Zarpou S, Khonakdar Tarsi A. Effects of dexamethasone on hepatic ischemia-reperfusion injuries. JMUMS 2017;27:196-209.
3
4. Amani H, Habibey R, Hajmiresmail S, Latifi S, Pazoki-Toroudi H, Akhavan O. Antioxidant nanomaterials in advanced diagnoses and treatments of ischemia-reperfusion injuries. J Mater Chem B. 2017;5:9452-9476.
4
5. Sonin NV, Garcia-Pagan J-C, Nakanishi K, Zhang JX, Clemens MG. Patterns of vasoregulatory gene expression in the liver response to ischemia/reperfusion and endotoxemia. Shock. 1999;11:175-179.
5
6. Lin Z, Kumar A, SenBanerjee S, Staniszewski K, Parmar K, Vaughan DE, et al. Kruppel-like factor 2 (KLF2) regulates endothelial thrombotic function. Circ Res. 2005;96:e48-e57.
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7. Moseley R, Leaver M, Walker M, Waddington R, Parsons D, Chen W, et al. Comparison of the antioxidant properties of HYAFF®-11p75, AQUACEL® and hyaluronan towards reactive oxygen species in vitro. Biomaterials. 2002;23:2255-2264.
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9. Saller R, Melzer J, Reichling J, Brignoli R, Meier R. An updated systematic review of the pharmacology of silymarin. Forsch Komplementmed. 2007;14:70-80.
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10. Karimi G, Vahabzadeh M, Lari P, Rashedinia M, Moshiri M. “Silymarin”, a promising pharmacological agent for treatment of diseases. Iran J Basic Med Sci 2011;14:308-317.
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11. Beckmann‐Knopp S, Rietbrock S, Weyhenmeyer R, Böcker RH, Beckurts KT, Lang W, et al. Inhibitory effects of silibinin on cytochrome P‐450 enzymes in human liver microsomes. Pharmacol Toxicol 2000;86:250-256.
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12. Koçarslan A, Koçarslan S, Aydin MS, Gunay Ş, Karahan MA, Taşkın A, et al. Intraperitoneal administration of silymarin protects end organs from multivisceral ischemia/reperfusion injury in a rat model. Braz J Cardiovasc Surg 2016;31:434-439.
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13. Clavien P-A, Selzner M, Rüdiger HA, Graf R, Kadry Z, Rousson V, et al. A prospective randomized study in 100 consecutive patients undergoing major liver resection with versus without ischemic preconditioning. Ann Surg 2003;238:843-850.
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14. Mikaeili S, Kadkhodaee M, Golab F, Zahmatkesh M, Mahdavi-Mazdeh M, Seifi B, et al. Effects of liver ischemia-reperfusion on renal functional and oxidative stress indices. Physiol Pharmacol 2009;13:254-262.
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15. Massip‐Salcedo M, Roselló‐Catafau J, Prieto J, Avila MA, Peralta C. The response of the hepatocyte to ischemia. Liver Int. 2007;27:6-16.
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16. Pannen BH, Al‐Adili F, Bauer M, Clemens MG, Geiger KK. Role of endothelins and nitric oxide in hepatic reperfusion injury in the rat. Hepatology 1998;27:755-764.
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17. Hassan‐Khabbar S, Cottart CH, Wendum D, Vibert F, Clot JP, Savouret JF, et al. Postischemic treatment by trans‐resveratrol in rat liver ischemia‐reperfusion: a possible strategy in liver surgery. Liver Transpl 2008;14:451-459.
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18. Ahmadiasl N, Banaei S, Alihemmati A. Combination antioxidant effect of erythropoietin and melatonin on renal ischemia-reperfusion injury in rats. Iran J Basic Medi Sci 2013;16:1209-1216.
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19. He Q, Kim J, Sharma RP. Silymarin protects against liver damage in BALB/c mice exposed to fumonisin B1 despite increasing accumulation of free sphingoid bases. Toxicol Sci 2004;80:335-342.
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20. Razavi BM, Karimi G. Protective effect of silymarin against chemical-induced cardiotoxicity. Iran J Basic Med Sci 2016;19:916-923.
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21. Akbari Kordkheyli V, Nabipur E, Tafazoli A. An overview on the effects of silibinin on different microRNAs expression in cancer. JMUMS 2018;28:213-229.
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22. Dulk AC, Sebib Korkmaz K, Rooij BJF, Sutton ME, Braat AE, Inderson A, et al. High peak alanine aminotransferase determines extra risk for nonanastomotic biliary strictures after liver transplantation with donation after circulatory death. Transpl Int 2015;28:492-501.
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40
ORIGINAL_ARTICLE
Asiaticoside attenuates hyperoxia-induced lung injury in vitro andin vivo
Objective(s): Asiaticoside (AS) displays anti-inflammation, and anti-apoptosis effect, but the role of AS in hyperoxia-induced lung injury (HILI) treatment is undefined. Therefore, the aim of this study was to investigate the effects of AS on HILI on premature rats and alveolar type II (AEC II) cells.Materials and Methods: Sprague-Dawley premature rats (n=25/group) were exposed to 80% O2 with or without AS. Then, we detected 80% O2-induced lung injury and survival rate of premature rat. We tested the concentration of malondialdehyde (MDA), myeloperoxidase (MPO), total antioxidant capacity (TAOC), tumor necrosis factor α (TNF-α), interleukin 6 (IL-6), and interleukin 1β (IL-1β) in premature rats’ blood. Then, the AEC II cell apoptosis was observed by Hoechst 33258 staining and flow cytometry. Simultaneously, nuclear factor (erythroid-derived 2)-like 2 (Nrf2) signaling pathway was measured by Western blot.Results: Our results found that AS-treated group rats had significantly higher survival rates than 80% O2 group at day 14 (P<0.05). AS protected HILI, decreased the MPO and MDA concentration, and reversed TAOC level (P<0.05). AS also downregulated the levels of TNF-α, IL-1β, and IL-6 in the premature rat’s blood (P<0.01). Moreover, AS markedly attenuated AEC II cell apoptosis and increased Nrf2 and Heme oxygenase 1 (HO-1) expression in the nucleus (P<0.05).Conclusion: AS showed protective effects on premature rats of HILI in vitro and in vivo. AS can potentially be developed as a novel agent for the treatment of HILI diseases.
https://ijbms.mums.ac.ir/article_12775_26a5f62dc5f0eca2260c2670726f0e5a.pdf
2019-07-01
797
805
10.22038/ijbms.2019.35913.8556
Apoptosis
Asiaticoside
Hyperoxia
Inflammation
Lung injury
Premature
Jia-wen
Dang
390286978@qq.com
1
Department of Newborn Medicine, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan 646000, China
AUTHOR
Xiao-ping
Lei
leixiaopingde@126.com
2
Department of Newborn Medicine, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan 646000, China
AUTHOR
Qing-ping
Li
lzlqp@126.com
3
Department of Newborn Medicine, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan 646000, China
AUTHOR
Wen-bin
Dong
swmudwb@163.com
4
Department of Newborn Medicine, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan 646000, China
LEAD_AUTHOR
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44
ORIGINAL_ARTICLE
Prevalence of β-lactamase genes, class 1 integrons, major virulence factors and clonal relationships of multidrug-resistant Pseudomonas aeruginosa isolated from hospitalized patients in southeast of Iran
Objective(s): Pseudomonas aeruginosa is one of the most important nosocomial pathogens causing a high rate of mortality among hospitalized patients. Herein, we report the prevalence of antibiotic resistance genes, class 1 integrons, major virulence genes and clonal relationship among multidrug- resistant (MDR) P. aeruginosa, isolated from four referral hospitals in the southeast of Iran.Materials and Methods: In this study, 208 isolates of P. aeruginosa were collected from four referral hospitals in southeast of Iran. Disk diffusion method was used to determine susceptibility to 13 antibacterial agents. AmpC was detected by phenotypic method and β-lactamase genes, virulence genes and class 1 integrons were detected by PCR. Clonal relationship of the isolates was determined by RAPD-PCR.Results: All the isolates were susceptible to polymyxin-B and colistin. Overall, 40.4% of the isolates were MDR, among which resistance to third generation cephalosporins, aminoglycosides, and carbapenems was 47.5%, 32.3% and 40%, respectively. None of the isolates was positive for blaNDM-1 genes, while 84.5% and 4.8% were positive for the blaIMP-1 and blaVIM, metallo-β-lactamase genes, respectively. Incidence of class 1 integrons was 95% and AmpC was detected in 33% of the isolates. Prevalence of exoA, exoS, exoU, pilB and nan1 were 98.8%, 44%, 26%, 8.3% and 33.3%, respectively. RAPD profiles identified four large clusters consisting of 77 isolates, and two small clusters and three singletons.Conclusion: The rate of MDR P. aeruginosa isolates was high in different hospitals in this region. High genetic similarity among MDR isolates suggests cross-acquisition of infection in the region.
https://ijbms.mums.ac.ir/article_13202_a694b6b9c9e483cf5137394672af4fc2.pdf
2019-07-01
806
812
10.22038/ijbms.2019.35063.8340
Antibiotic resistance
Beta-lactamases
Class 1 integrons
Pseudomonas aeruginosa
RAPD-PCR
virulence factors
Hossein
Sharifi
sharif465@yahoo.com
1
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran
AUTHOR
Gholamreza
Pouladfar
pouladfar_ghr@hotmail.com
2
Prof Alborzi Clinical Microbiology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Mohammad Reza
Shakibaie
mr_shakibaei@kmu.ac.ir
3
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran
AUTHOR
Bahman
Pourabbas
bpourabbas@yahoo.com
4
Prof Alborzi Clinical Microbiology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Jalal
Mardaneh
jalalmardaneh@yahoo.com
5
Department of Microbiology, School of Medicine, Gonabad University of Medical Sciences, Gonabad, Iran
AUTHOR
Shahla
Mansouri
mansouri.shahla97@gmail.com
6
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran
LEAD_AUTHOR
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1
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6. Khosravi AD, Motahar M, Montazeri EA. The frequency of class1 and 2 integrons in Pseudomonas aeruginosa strains isolated from burn patients in a burn center of Ahvaz, Iran. PloS one 2017; 12:e0183061.
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35. Neyestanaki DK, Mirsalehian A, Rezagholizadeh F, Jabalameli F, Taherikalani M, Emaneini M. Determination of extended spectrum beta-lactamases, metallo-beta-lactamases and AmpC-beta-lactamases among carbapenem resistant Pseudomonas aeruginosa isolated from burn patients. Burns 2014; 40:1556-1561.
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37. Akya A, Salimi A, Nomanpour B, Ahmadi K. Prevalence and clonal dissemination of metallo-beta-lactamase-producing Pseudomonas aeruginosa in Kermanshah. Jundishapur J Microbiol 2015; 8:e20980.
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38. Strateva T, Mitov I. Contribution of an arsenal of virulence factors to pathogenesis of Pseudomonas aeruginosa infections. Ann Microbiol 2011; 61:717-732.
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39. Khan AA, Cerniglia CE. Detection of Pseudomonas aeruginosa from clinical and environmental samples by amplification of the exotoxin A gene using PCR. Appl Environ Microbiol 1994; 60:3739-3745.
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40. Taheri ZM, Shahbazi N, Khoddami M. Genetic diversity of Peudomonas aeruginosa Strains isolated from hospitalized patients. Tanaffos 2008; 7:32-39.
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41. Doosti M, Ramazani A, Garshasbi M. Identification and characterization of metallo-β-lactamases producing Pseudomonas aeruginosa clinical isolates in university hospital from Zanjan Province, Iran. Iran Biomed J 2013; 17:129-133.
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42. Kali A, Srirangaraj S, Kumar S, Divya H, Kalyani A, Umadevi S. Detection of metallo-beta-lactamase producing Pseudomonas aeruginosa in intensive care units. Australas Med J 2013; 6:686–693.
42
ORIGINAL_ARTICLE
Toxin profiles and antimicrobial resistance patterns among toxigenic clinical isolates of Clostridioides (Clostridium) difficile
Objective(s): Clostridioides (Clostridium) difficile infection as a healthcare-associated infection can cause life-threatening infectious diarrhea in hospitalized patients. The aim of this study was to investigate the toxin profiles and antimicrobial resistance patterns of C. difficile isolates obtained from hospitalized patients in Shiraz, Iran.Materials and Methods: This study was performed on 45 toxigenic C. difficile isolates. Determination of toxin profiles was done using polymerase chain reaction method. Antimicrobial susceptibility to vancomycin, metronidazole, clindamycin, tetracycline, moxifloxacin, and chloramphenicol was determined by the agar dilution method. The genes encoding antibiotic resistance were detected by the standard procedures.Results: The most frequent toxin profile was tcdA+, tcdB+, cdtAˉ, cdtBˉ (82.2%), and only one isolate harboured all toxin associated genes (tcdA+, tcdB+, cdtA+, cdtB+) (2.2%). The genes encoding CDT (binary toxin) were also found in six (13.3%) isolates. Resistance to tetracycline, clindamycin and moxifloxacin was observed in 66.7%, 60% and 42.2% of the isolates, respectively. None of the strains showed resistance to other antibiotics. The distribution of the ermB gene (the gene encoding resistance to clindamycin) was 57.8% and the tetM and tetW genes (the genes encoding resistance to tetracycline) were found in 62.2% and 13.3% of the isolates, respectively. The substitutions Thr82 to Ile in GyrA and Asp426 to Asn in GyrB were seen in moxifloxacin resistant isolates.Conclusion: Our data contributes to the present understanding of virulence and resistance traits amongst the isolates. Infection control strategies should be implemented carefully in order to curb the dissemination of C. difficile strains in hospital.
https://ijbms.mums.ac.ir/article_13015_2f36447812c3ad3bd2e5f26afb1a936d.pdf
2019-07-01
813
819
10.22038/ijbms.2019.35223.8390
Clostridioides (Clostridium) difficile
C. difficile infection
Toxins
CDT
Antibiotic resistance
Hamid
Heidari
heidarii.hamid@gmail.com
1
Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Hadi
Sedigh Ebrahim-Saraie
seddigh.hadi@gums.ac.ir
2
Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Ali
Amanati
aliamanati1356@gmail.com
3
Professor Alborzi Clinical Microbiology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Mohammad
Motamedifar
vahid.s13@gmail.com
4
Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Nahal
Hadi
nahalhadi.nh@gmail.com
5
Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
AUTHOR
Abdollah
Bazargani
bazarganiia@gmail.com
6
Department of Bacteriology and Virology, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
LEAD_AUTHOR
1. Berger FK, Rasheed SS, Araj GF, Mahfouz R, Rimmani HH, Karaoui WR, et al. Molecular characterization, toxin detection and resistance testing of human clinical Clostridium difficile isolates from Lebanon. Int J Med Microbiol 2018; 308:358-363.
1
2. Lim SC, Androga GO, Knight DR, Moono P, Foster NF, Riley TV. Antimicrobial susceptibility of Clostridium difficile isolated from food and environmental sources in Western Australia. Int J Antimicrob Agents 2018; 52:411-415.
2
3. Janoir C. Virulence factors of Clostridium difficile and their role during infection. Anaerobe 2016; 37:13-24.
3
4. Aktories K, Papatheodorou P, Schwan C. Binary Clostridium difficile toxin (CDT) - a virulence factor disturbing the cytoskeleton. Anaerobe 2018; 53:21-29.
4
5. Tokimatsu I, Shigemura K, Osawa K, Kinugawa S, Kitagawa K, Nakanishi N, et al. Molecular epidemiologic study of Clostridium difficile infections in university hospitals: results of a nationwide study in Japan. J Infect Chemother 2018; 24:641-647.
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9. Abuderman AA, Mateen A, Syed R, Sawsan Aloahd M. Molecular characterization of Clostridium difficile isolated from carriage and association of its pathogenicity to prevalent toxic genes. Microb Pathog 2018; 120:1-7.
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10. Yang J, Zhang X, Liu X, Cai L, Feng P, Wang X, et al. Antimicrobial susceptibility of Clostridium difficile isolates from ICU colonized patients revealed alert to ST-37 (RT 017) isolates. Diagn Microbiol Infect Dis 2017; 89:161-163.
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12. Sedigh Ebrahim-Saraie H, Heidari H, Amanati A, BazarganiA, Alireza Taghavi S, Nikokar I, et al. A multicenter-based study on epidemiology, antibiotic susceptibility and risk factors of toxigenic Clostridium difficile in hospitalized patients in southwestern Iran. Infez Med 2018; 26: 308-315.
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21. Spigaglia P, Barbanti F, Mastrantonio P, Brazier JS, Barbut F, Delmee M, et al. Fluoroquinolone resistance in Clostridium difficile isolates from a prospective study of C. difficile infections in Europe. J Med Microbiol 2008; 57:784-789.
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22. Karlowsky JA, Adam HJ, Kosowan T, Baxter MR, Nichol KA, Laing NM, et al. PCR ribotyping and antimicrobial susceptibility testing of isolates of Clostridium difficile cultured from toxin-positive diarrheal stools of patients receiving medical care in Canadian hospitals: the Canadian Clostridium difficile Surveillance Study (CAN-DIFF) 2013-2015. Diagn Microbiol Infect Dis 2018; 91:105-111.
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23. Costa CL, Mano de Carvalho CB, Gonzalez RH, Gifoni MAC, Ribeiro RA, Quesada-Gomez C, et al. Molecular epidemiology of Clostridium difficile infection in a Brazilian cancer hospital. Anaerobe 2017; 48:232-236.
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26. Rezazadeh Zarandi E, Mansouri S, Nakhaee N, Sarafzadeh F, Iranmanesh Z, Moradi M. Frequency of antibiotic associated diarrhea caused by Clostridium difficile among hospitalized patients in intensive care unit, Kerman, Iran. Gastroenterol Hepatol Bed Bench 2017; 10:229-234.
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27. Goncalves C, Decre D, Barbut F, Burghoffer B, Petit JC. Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile. J Clin Microbiol 2004; 42:1933-1939.
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29. Cejas D, Rios Osorio NR, Quiros R, Sadorin R, Berger MA, Gutkind G, et al. Detection and molecular characterization of Clostridium difficile ST 1 in Buenos Aires, Argentina. Anaerobe 2018; 49:14-17.
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35. Gao Q, Wu S, Huang H, Ni Y, Chen Y, Hu Y, et al. Toxin profiles, PCR ribotypes and resistance patterns of Clostridium difficile: a multicentre study in China, 2012-2013. Int J Antimicrob Agents 2016; 48:736-739.
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36. Hidalgo-Villeda F, Tzoc E, Torres L, Bu E, Rodriguez C, Quesada-Gomez C. Diversity of multidrug-resistant epidemic Clostridium difficile NAP1/RT027/ST01 strains in tertiary hospitals from Honduras. Anaerobe 2018; 52:75-78.
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39. Goudarzi M, Goudarzi H, Alebouyeh M, Azimi Rad M, Shayegan Mehr FS, Zali MR, et al. Antimicrobial susceptibility of Clostridium difficile clinical isolates in Iran. Iran Red Crescent Med J 2013; 15:704-711.
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43. Cheng JW, Yang QW, Xiao M, Yu SY, Zhou ML, Kudinha T, et al. High in vitro activity of fidaxomicin against Clostridium difficile isolates from a university teaching hospital in China. J Microbiol Immunol Infect 2018; 51:411-416.
43
ORIGINAL_ARTICLE
Exploring the role and inter-relationship among nitric oxide, opioids, and KATP channels in the signaling pathway underlying remote ischemic preconditioning induced cardioprotection in rats
Objective(s): This study explored the inter-relationship among nitric oxide, opioids, and KATP channels in the signaling pathway underlying remote ischemic preconditioning (RIPC) conferred cardioprotection. Materials and Methods: Blood pressure cuff was placed around the hind limb of the animal and RIPC was performed by 4 cycles of inflation (5 min) followed by deflation (5 min). An ex vivo Langendorff’s isolated rat heart model was used to induce ischemia (of 30 min duration)-reperfusion (of 120 min duration) injury. Results: RIPC significantly decreased ischemia-reperfusion associated injury assessed by decrease in myocardial infarct, LDH and CK release, improvement in postischemic left ventricular function, LVDP, dp/dtmax, and dp/dtmin. Pretreatment with L-NAME and naloxone abolished RIPC-induced cardioprotection. Moreover, preconditioning with sodium nitroprusside (SNP) and morphine produced a cardioprotective effect in a similar manner to RIPC. L-NAME, but not naloxone, attenuated RIPC and SNP preconditioning-induced increase in serum nitrite levels. Morphine preconditioning did not increase the NO levels, probably suggesting that opioids may be the downstream mediators of NO. Furthermore, glibenclamide and naloxone blocked cardioprotection conferred by morphine and SNP, respectively. Conclusion: It may be proposed that the actions of NO, opioids, and KATP channels are interlinked. It is possible to suggest that RIPC may induce the release of NO from endothelium, which may trigger the synthesis of endogenous opioids, which in turn may activate heart localized KATP channels to induce cardioprotection.
https://ijbms.mums.ac.ir/article_13167_018ab5a0239a5989a1345fe16cf04b14.pdf
2019-07-01
820
826
10.22038/ijbms.2019.34609.8211
Cardioprotection
KATP channels
Nitric oxide
Opioids
Remote ischemic preconditioning
Sapna
Aggarwal
amteshwar_jaggi@rediffmail.com
1
Department of Pharmaceutical Sciences and Drug Research, Punjabi University Patiala, 147002 India
AUTHOR
Jasleen
Kaur Virdi
jkaur2807@gmail.com
2
Department of Pharmaceutical Sciences and Drug Research, Punjabi University Patiala, 147002 India
AUTHOR
Nirmal
Singh
nirmal_puru@rediffmail.com
3
Department of Pharmaceutical Sciences and Drug Research, Punjabi University Patiala, 147002 India
AUTHOR
Amteshwar
Singh Jaggi
jaggiamteshwar@gmail.com
4
Department of Pharmaceutical Sciences and Drug Research, Punjabi University Patiala, 147002 India
LEAD_AUTHOR
1. Hausenloy DJ, Yellon DM. Remote ischaemic preconditioning: underlying mechanisms and clinical application. Cardiovasc Res 2008; 79:377–386.
1
2. Murry CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 1986; 74:1124–1136.
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3. Taliyan R, Singh M, Sharma PL, Yadav HN, Sidhu KS. Possible involvement of α1-adrenergic receptor and K (ATP) channels in cardioprotective effect of remote aortic preconditioning in isolated rat heart. J Cardiovasc Dis Res 2010; 1:145–151.
3
4. Wolfrum S, Schneider K, Heidbreder M, Nienstedt J, Dominiak P, Dendorfer A. Remote preconditioning protects the heart by activating myocardial PKCepsilon-isoform. Cardiovasc Res 2002; 55:583–589.
4
5. Kant R, Diwan V, Jaggi AS, Singh N, Singh D. Remote renal preconditioning-induced cardioprotection: a key role of hypoxia inducible factor-prolyl 4-hydroxylases. Mol Cell Biochem 2008; 312:25–31.
5
6. Tokuno S, Hinokiyama K, Tokuno K, Löwbeer C, Hansson L, Valen G. Spontaneous ischemic events in the brain and heart adapt the hearts of severely atherosclerotic mice to ischemia. Arterioscler Thromb Vasc Biol 2002; 22:995–1001.
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7. Liem DA, Verdouw PD, Ploeg H, Kazim S, Duncker DJ. Sites of action of adenosine in interorgan preconditioning of the heart. Am J Physiol Heart Circ Physiol 2002; 283:H29–H37.
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9. Kharbanda RK, Mortensen UM, White PA, Kristiansen SB, Schmidt MR, Hoschtitzky JA, et al. Transient limb ischemia induces remote ischemic preconditioning in vivo. Circulation 2002; 106:2881–2883.
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10. Botker HE, Kharbanda R, Schmidt MR, Bøttcher M, Kaltoft AK, Terkelsen CJ, et al. Remote ischemic conditioning before hospital admission, as a complement to angioplasty, and effect on myocardial salvage in patients with acute myocardial infarction: a randomized trial. Lancet 2010; 375:727–734.
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11. Ali N, Rizwi F, Iqbal A, Rashid A. Induced remote ischemic preconditioning on ischemia-reperfusion injury in patients undergoing coronary artery bypass. J Coll Physicians Surg Pak 2010; 20:427–431.
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12. Cheung MM, Kharbanda RK, Konstantinov IE, Shimizu M, Meng HF, Li J, et al. Randomized controlled trial of the effects of RIPC on children undergoing cardiac surgery: first clinical application in humans. J Am Coll Cardiol 2006; 47:2277–2282.
12
13. Aggarwal S, Randhawa PK, Singh N, Jaggi AS. Preconditioning at a distance: involvement of endothelial vasoactive substances in cardioprotection against ischemia-reperfusion injury. Life Sci 2016; 151:250-258.
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14. Kitakaze M, Node K, Minamino T, Inoue M, Hori M, Kamada T. Evidence for nitric oxide generation in the cardiomyocytes: its augmentation by hypoxia. J Am Coll Cardiol 1995; 27:2149-2154.
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16. Ignarro LJ, Napoli C, Loscalzo J. Nitric oxide donors and cardiovascular agents modulating the bioactivity of nitric oxide: an overview. Circ Res 2002; 90:21–28.
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17. Bolli R. Cardioprotective function of inducible nitric oxide synthase and role of nitric oxide in myocardial ischemia and preconditioning: an overview of a decade of research. J Mol Cell Cardiol 2001; 33:1897–1918.
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18. Shahid M, Tauseef M, Sharma KK, Fahim M. Brief femoral artery ischaemia provides protection against myocardial ischaemia-reperfusion injury in rats: the possible mechanisms. Exp Physiol 2008; 93:954–968.
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19. Rassaf T, Totzeck M, Cotta UB, Shiva S, Heusch G, Kelm M. Circulating nitrite contributes to cardioprotection by Remote Ischemic Preconditioning. Circ Res 2014; 114:1601-1610.
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20. Headrick JP, Pepe S, Peart JN. Non-analgesic effects of opioids: cardiovascular effects of opioids and their receptor systems. Curr Pharm Des 2012; 18:6090-6100.
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21. Romano MA, Seymour EM, Berry JA, McNish RA, Bolling SF. Relative contribution of endogenous opioids to myocardial ischemic tolerance. J Surg Res 2004; 118:32-37.
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22. Tanaka K, Kersten JR, Riess ML. Opioid-induced cardioprotection. Curr Pharm Des 2014; 20:5696–5705.
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25. Schultz JJ, Hsu AK, Gross GJ. Ischemic preconditioning and morphine-induced cardioprotection involve the delta-opioid receptor in the intact rat heart. J Mol Cell Cardiol 1997; 29:2187–2195.
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26. Patel HH, Moore J, Hsu AK, Gross GJ. Cardioprotection at a distance: mesenteric artery occlusion protects the myocardium via an opioid sensitive mechanism. J Mol Cell Cardiol 2002; 34:1317–1323.
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27. Dickson EW, Tubbs RJ, Porcaro WA, Lee WJ, Blehar DJ, Carraway RE, et al. Myocardial preconditioning factors evoke mesenteric ischemic tolerance via opioid receptors and K(ATP) channels. Am J Physiol Heart Circ Physiol 2002; 283:H22–H28.
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32. Sharma R, Randhawa PK, Singh N, Jaggi AS. Possible role of thromboxane A2 in remote hind limb preconditioning-induced cardioprotection. Naunyn Schmiedebergs Arch Pharmacol 2016; 389:1-9.
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34. Singh B, Randhawa PK, Singh N, Jaggi AS. Investigations on the role of leukotrienes in remote hind limb preconditioning-induced cardioprotection in rats. Life Sci 2016; 152:238-243.
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44
ORIGINAL_ARTICLE
Determination of antimicrobial effect of protamine by transmission electron microscopy and SDS PAGE on Pseudomonas aeruginosa isolates from diabetic foot infection
Objective(s): Diabetic foot infection is one of the major complications of diabetes leading to lower limb amputations. Isolation and identification of bacteria causing diabetic foot infection, determination of antibiotic resistance, antimicrobial potential of protamine by electron microscopy and SDS-PAGE analysis, arethe aims of this study.Materials and Methods: 285 pus samples from diabetic foot infection patients were collected from different hospitals of Karachi and Capital Health Hospital, Halifax, Canada. Clinical history of each patient was recorded. Bacterial isolates were cultured on appropriate media; identification was done by morphology, cultural and biochemical tests. Effect of protamine against multi drug resistant strains of Pseudomona aeruginosa was checked by minimum inhibitory concentration in 96 well micro-titer plates. The isolates were grown in bactericidal concentration of protamine on plates to isolate mutants. Effect of protamine on protein expression was checked by SDS- PAGE and ultra-structural morphological changes by transmission electron microscopy.Results: Results indicated prevalence of foot infection as 92% in diabetic patients. Major bacterial isolates were Staphylococcus aureus 65 (23%), P. aeruginosa 80 (28.1%), Klebsiella spp. 37 (13%), Proteus mirabilis 79 (27.7%), and Escherichia coli 24 (12%). These isolates were highly resistant to different antibiotics. MIC value of protamine was 500 µg/ml against P. aeruginosa. SDS-PAGE analysis revealed that protamine can suppress expression of various virulence proteins and electron micrographs indicated condensation of cytoplasm and accumulation of protamine in cytoplasm without damaging the cell membrane. Conclusion: P. aeruginosa and S. aureus were the major isolates expressing multi-drug resistance and protamine sulfate represented good antimicrobial potential.
https://ijbms.mums.ac.ir/article_13101_de48af981ccf7c114f290d3fcaeed439.pdf
2019-07-01
827
832
10.22038/ijbms.2019.32414.7989
Diabetic foot
Pseudomonas aeruginosa
Protamine
Transmission electron microscopy
Polyacrylamide Gel
Mubashar
Aziz
mubashirazizsheikh@gmail.com
1
Department of Pathobiology, Bahauddin Zakariya University, Multan, Pakistan
LEAD_AUTHOR
Rafael
Garduno
rafael.garduno@inspection.gc.ca
2
Department of Microbiology, Dalhousie University, Halifax, Canada,
AUTHOR
Zulfiqar
Mirani
mirani_mrsa@yahoo.com
3
PCSIR Laboratories Complex, Karachi, Pakistan
AUTHOR
Rakhshanda
Baqai
r_baqai@yahoo.com
4
Department of Microbiology, University of Karachi, Karachi, Pakistan
AUTHOR
Ahsan
Sheikh
assheikh@bzu.edu.pk
5
Institute of Food Science and Nutrition, Bahauddin Zakariya University, Multan, Pakistan
AUTHOR
Humera
Nazir
humeranazir27@gmail.com
6
Islamic International University, Islamabad
AUTHOR
Mazhar
Ayyaz
mazharayaz@bzu.edu.pk
7
Department of Pathobiology, Bahauddin Zakariya University, Multan, Pakistan
AUTHOR
Shahana
Kazmi
shahanaurooj@yahoo.com
8
Department of Microbiology, University of Karachi, Karachi, Pakistan
AUTHOR
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2. Raja, NS. Microbiology of diabetic foot infections in a teaching hospital in Malaysia: a retrospective study of 194 cases. J. Microbiol Immunol Infect 2007;40:39.
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3. Siripornmongcolchai, T, Chomvarin, C, Chaicumpar, K, Limpaiboon, T, Wongkhum, C. Evaluation of different primers for detecting mecA gene by PCR in comparison with phenotypic methods for discrimination of methicillin-resistant Staphylococcus aureus. S. Asian J Trop Med Public Health. 2002;33:758-763.
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4. Frieri, M, Kumar, K, Boutin, A. Antibiotic resistance. J. Infect Public Health. 2017; 10:369-378.
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5. Haynes, A, Ruda, F, Oliver, J, Hamood, AN, Griswold, JA, Park, PW, Rumbaugh, KP, Syndecan, shedding contributes to Pseudomonas aeruginosa sepsis. Infect. Immunity 2005; 73:7914-7921.
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6. Aspedon, A, Groisman, EA. The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium. Microbiol 1996; 142:3389-3397.
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7. Gao, B, Stieger, B, Noé, B, Fritschy, JM, Meier, PJ. Localization of the organic anion transporting polypeptide 2 (Oatp2) in capillary endothelium and choroid plexus epithelium of rat brain. J. Histochem. Cytochem. 1999; 47:1255-1263
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8. Matsuzaki, K, Yoneyama, S, Fujii, N, Miyajima, K, Yamada KI, Kirino Y, Anzai K. Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, Tachyplesin I, and its linear analog. Biochem 1997; 36:9799-9806.
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9. Wu, M, Maier, E, Benz, R, Hancock, RE. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochem 1999; 38:7235-7242.
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10. Hancock, RE. Antibacterial peptides and the outer membranes of gram-negative bacilli. J Med Microbiol 1997; 46:1.
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11. Hancock, RE. Peptide antibiotics. The Lancet 1997; 349:418-422.
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12. Pink, DA, Hasan, FM, Quinn, BE, Winterhalter, M, Mohan, M, Gill, TA. Interaction of protamine with gram‐negative bacteria membranes: possible alternative mechanisms of internalization in Escherichia coli, Salmonella typhimurium and Pseudomonas aeruginosa. J. Peptide Sci 2014; 20:240-250.
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13. Pink D, Hansen LT, Gill T, Quinn B, Jericho M. Beveridge T. Divalent calcium ions inhibit the penetration of protamine through the polysaccharide brush of the outer membrane of Gram-negative bacteria. Langmuir 2003. 19: 8852-8858.
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14. Hansen, LT, Gill, TA. Solubility and antimicrobial efficacy of protamine on Listeria monocytogenes and Escherichia coli as influenced by pH J Appl Microbiol 2000; 88:1049-1055.
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15. Johansen, C, Verheul, A, Gram, L, Gill, T, Abee, T. Protamine-induced permeabilization of cell envelopes of gram-positive and gram-negative bacteria. Appl. Environ. Microbiol 1997; 63:1155-159.
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16. Johansen, C, Gill, T, Gram, L. Changes in cell morphology of Listeria monocytogenes and Shewanella putrefaciens resulting from the action of protamine. Appl Environ Microbiol 1996; 62:1058-1064.
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17. Johansen, C, Gill, T, Gram, L. Antibacterial effect of protamine assayed by impedimetry. J Appl Bacteriol 1995; 78:297-303.
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18. Uyttendaele, M, Debevere, J. Evaluation of the antimicrobial activity of protamine. Food Microbiol 1994; 11:417-427.
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19. Rosa-Fraile, M, Camacho-Muñoz, E, Rodríguez-Granger, J, Liébana-Martos, C. Specimen storage in transport medium and detection of group B Streptococci by culture. J Clin Microbiol 2005; 43:928-930.
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20. Gadepalli, R, Dhawan, B, Sreenivas, V, Kapil, A, Ammini, AC, Chaudhry, RA. Clinico-Microbiological study of diabetic foot ulcers in an Indian tertiary care hospital. Diabetes Care 2006; 29:1727-1732.
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21. Willcox, MD, Hume, EB, Aliwarga, Y, Kumar, N, Cole, N. A novel cationic‐peptide coating for the prevention of microbial colonization on contact lenses. J Appl Microbiol 2008;105:1817-1825.
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22. Garduno, RA, Garduno, E, Hiltz, M, Hoffman, PS. Intracellular growth of Legionella pneumophila gives rise to a differentiated form dissimilar to stationary-phase forms. Infect. Immunity 2002; 70:6273-6283.
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23. Murugan, S, Mani, KR & Uma Devi P. Prevalence of methicillin resistant Staphylococcus aureus among diabetes patients with foot ulcers and their antimicrobial susceptibility pattern. J Clin Diagn Res 2008;2:979-984.
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24. Ozer, B, Kalaci, A, Semerci, E, Duran, N, Davul, S, Yanat, AN. Infections and aerobic bacterial pathogens in diabetic foot. Afr. J Microbiol Res 2010; 4:2153-2160.
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25. Khoharo, HK, Ansari, S, Qureshi, F. Diabetic foot ulcers; common isolated pathogens and in vitro antimicrobial activity. Profess. Med J Quart 2009;53-60.26.
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26. Olid, AS, Solà I, Barajas‐Nava LA, Gianneo OD, Cosp XB and Lipsky BA, 2015. Systemic antibiotics for treating diabetic foot infections. Cochrane Database of Systematic Reviews, (9).
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27. Pränting, M, Andersson, DI. Mechanisms and physiological effects of protamine resistance in Salmonella enterica serovar typhimurium LT2 J Antimicrob Chemother 2010; 65:876-887.
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28. Koo, SP, Bayer, AS, Yeaman, MR. Diversity in antistaphylococcal mechanisms among membrane-targeting antimicrobial peptides. Infect. Immunity 2001; 69:4916-4922.
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29. Soboh, F, Khoury, AE, Zamboni, AC, Davidson, D, Mittelman, MW. Effects of Ciprofloxacin and Protamine sulfate combinations against catheter-associated Pseudomonas aeruginosa biofilms. Antimicrob. agents Chemother 1995; 39:1281-1286.
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30. Himly, M, Mills-Goodlet, R, Geppert, M, Duschl, A. Nanomaterials in the Context of Type 2 immune Responses—Fears and Potentials. Frontiers Immunol 2017; 8:471.
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31. Schweizer, HP. Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: unanswered questions. Genet Mol Res 2003; 2:48-62.
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32. Sun, J, Deng, Z, Yan, A. Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations. Biochem. Biophys. Res. Commun. 2014; 453:254-267.
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33. Mohan, M. Effects of Protamine on Pseudomonas aeruginosa cell envelope components: surface remodeling [M Sc dissertation]. Dalhousie University, Halifax Canada; 2010.
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34. Broutin, I, Benabdelhak, H, Moreel, X, Lascombe, MB, Lerouge, D, Ducruix, A. Expression, purification, crystallization and preliminary X-ray studies of the outer membrane efflux proteins OprM and OprN from Pseudomonas aeruginosa. Acta Crystallograph Section F: Struct Biol Crystal Commun 2005; 61:315-318.
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35. MacMillan, WG, Hibbitt, KG. The effect of antimicrobial proteins on the fine structure of Staphylococcus aureus. Microbiol 1969; 56:373-377.
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36. Mahendran, KR, Kreir, M, Weingart, H, Fertig, N, Winterhalter, M. Permeation of antibiotics through Escherichia coli OmpF and OmpC porins: screening for influx on a single-molecule level. J Biomol Screening 2010; 15:302-307.
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37. Danelon, C, Nestorovich, EM, Winterhalter, M, Ceccarelli, M, Bezrukov, SM. Interaction of zwitterionic penicillins with the OmpF channel facilitates their translocation. Biophys J 2006; 90:1617-1627.
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38. Aspedon, A, Groisman, EA. The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium. Microbiology 1996; 142:3389-3397.
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