ORIGINAL_ARTICLE
Update on riboflavin and multiple sclerosis: a systematic review
Multiple sclerosis (MS) is an inflammatory demyelinating disease of the central nervous system (CNS). Riboflavin plays an important role in myelin formation, and its deficiency is implicated as a risk factor for multiple sclerosis. Here, we systematically reviewed the literature concerning the health benefits of riboflavin on MS. The literature recorded within four main databases, including relevant clinical trials, experimental, and case-control studies from 1976 to 2017 were considered. Both human and animal studies were included for review, with no restrictions on age, gender, or ethnicity. Experimental studies demonstrated that riboflavin deficiency triggers neurologic abnormalities related to peripheral neuropathies such as demyelinating neuropathy. Moreover, randomized controlled trials (RCT) and case-control studies in which MS patients received riboflavin supplementation or had higher dietary riboflavin intake showed improvements in neurological motor disability. Riboflavin is a cofactor of xanthine oxidase and its deficiency exacerbates low uric acid caused by high copper levels, leading to myelin degeneration. The vitamin additionally plays a significant role in the normal functioning of glutathione reductase (GR) as an antioxidant enzyme, and conditions of riboflavin deficiency lead to oxidative damage. Riboflavin promotes the gene and protein levels of brain-derived neurotrophic factor (BDNF) in the CNS of an animal model of MS, suggesting that BDNF mediates the beneficial effect of riboflavin on neurological motor disability. Research to date generally supports the role of riboflavin in MS outcomes. However, further observational and interventional studies on human populations are warranted to validate the effects of riboflavin.
https://ijbms.mums.ac.ir/article_9257_ade7e86fc936c350b2fd84a974bed072.pdf
2017-09-01
958
966
10.22038/ijbms.2017.9257
Brain-derived neurotrophic factor
Demyelinating disease
Multiple Sclerosis
Riboflavin
Riboflavin deficiency
Mahshid
Naghashpour
mnaghashpour@gmail.com
1
Abadan School of Medical Sciences, Abadan, Iran
AUTHOR
Sima
Jafarirad
2
Nutrition and Metabolic Diseases Research Center, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Khuzestan, Iran
AUTHOR
Reza
Amani
amani.r@ajums.ac.ir
3
Food Security Research Center, Department of Clinical Nutrition, School of Nutrition and Food Science, Isfahan University of Medical Sciences, Isfahan, Iran
LEAD_AUTHOR
Alireza
Sarkaki
sarkaki_@ajums.ac.ir
4
Physiology Research Center, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Khuzestan, Iran
AUTHOR
Ahmad
Saedisomeolia
5
Department of Cellular and Molecular Nutrition, School of Nutritional Sciences and Dietetics, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
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ORIGINAL_ARTICLE
Cancer/Testis genes in relation to sperm biology and function
Cancer testis antigens (CTAs), a large family of tumor-associated and immunogenic antigens expressed in human tumors of various histological origins, are highly restricted to the testis and trophoblast. CTAs have been identified as potent targets for tumor-specific immunotherapeutic advances and have immensely lead to the development of different clinical trials of CTA-based vaccine therapy because of their resilient in vivo immunogenicity and tumor-restricted expression pattern. Bladder cancer, non-small cell lung carcinoma, and melanoma are grouped as high CT gene expressors. Prostate and breast cancer as moderate, and colon and renal cancers are considered as low CT gene expressors. Large percentages of these identified CT genes are expressed during spermatogenesis but their function is still vaguely unknown. Researchers have taken a keen interest in CT genes as pertaining to their role in tumor growth and spermatogenesis. Testis has many similarities with cancerous tissues like cell division, immigration, and immortalization. The aim is to give a concise in-depth review on the role of some specific CT genes in spermatogenesis.
https://ijbms.mums.ac.ir/article_9259_8cc4b2fff45cfc33c7f5afce683164db.pdf
2017-09-01
967
974
10.22038/ijbms.2017.9259
Cancer testis genes
Carcinogenesis
Spermatogenesis
Sperm biology
Sperm genes functions
Testis genes
Kehinde
Adebayo Babatunde
1
Clinical Anatomy/ Immunology Division, Department of Medicine, University of Fribourg, Fribourg, Switzerland
AUTHOR
Ali
Najafi
najafi74@ibb.ut.ac.ir
2
Medical Genetics Department, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Pouya
Salehipour
psp_pouya@yahoo.com
3
Medical Genetics Department, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Mohammad Hossein
Modarressi
s-asgharzade@razi.tums.ac.ir
4
Medical Genetics Department, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Maryam Beigom
Mobasheri
maryam.mobasheri@gmail.com
5
Medical Genetics Department, Faculty of Medicine, Tehran University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
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74
ORIGINAL_ARTICLE
Synthesis, characterization, molecular docking studies and biological evaluation of some novel hybrids based on quinazolinone, benzofuran and imidazolium moieties as potential cytotoxic and antimicrobial agents
Objective(s): Hybridization of bioactive natural and synthetic compounds is one of the most promising novel approaches for the design of hit and lead compounds with new molecular structures. In this investigation, a series of novel hybrid structures bearing quinazolinone, benzofuran and imidazolium moieties were designed and synthesized. Materials and Methods:Novel hybrid compounds were prepared and their structures were characterized by spectral and analytical data. In order to evaluate the biological activities, the synthesized hybrid compounds were studied for in vitro antibacterial activity against three Gram positive bacteria (Staphylococcus aureu, Bacillus subtilis, Listeria monocitogenes) and three Gram-negative bacteria (Escherichia coli, Pseudomonas aeruginosa, Salmonella entritidis) and also, Candida albicans as one yeast-like fungi strain. Cytotoxic activities of the synthesized compounds were also evaluated by the MTT assay in the human breast cancer cell line (MCF-7) and finally docking studies of cytotoxic derivatives were performed on aromatase enzyme. Results:The results of antimicrobial activity showed that compound 14e, with two halogen atoms on quinazolinone and benzofuran was the most active against all the tested strains of microorganisms with the MIC value 16-128 µg/ml. Some of the tested compounds showed good cytotoxicity on MCF-7, and compound 14c with IC50=0.59 micromolar (μM) was found to be the most cytotoxic compound among the studied hybrid derivatives. The docking analysis showed acceptable binding interactions for these compounds. Conclusion: Based on the obtained results, the hybrid derivatives of quinazolinone, benzofuran and imidazolium could be regarded as efficient candidates for further molecular developments of anticancer and antimicrobial agents.
https://ijbms.mums.ac.ir/article_9260_9f93f6453c0f4dfa2f59e74877cbd35c.pdf
2017-09-01
975
989
10.22038/ijbms.2017.9260
Antibacterial
Benzofuran
Cytotoxic
Imidazolium salt
QM/MM Docking
Quinazolinone
Parvin
Asadi
asadi@pharm.mui.ac.ir
1
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Ghadamali
Khodarahmi
khodarahmi@pharm.mui.ac.ir
2
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
LEAD_AUTHOR
Ali
Jahanian-Najafabadi
jahanian2001@yahoo.com
3
Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Lotfollah
Saghaie
saghaie@pharm.mui.ac.ir
4
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
Farshid
Hassanzadeh
5
Department of Medicinal Chemistry, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
AUTHOR
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18. Zahedifard M, Faraj FL, Paydar M, Looi CY, Hajrezaei M, Hasanpourghadi M, et al. Synthesis, characterization and apoptotic activity of quinazolinone Schiff base derivatives toward MCF-7 cells via intrinsic and extrinsic apoptosis pathways. Sci Rep 2015; 5:11544.
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35
ORIGINAL_ARTICLE
Apatinib has anti-tumor effects and induces autophagy in colon cancer cells
Objective(s): Apatinib recently has been used to treat patients with gastric cancer, but the function of apatinib in colon cancer remains unclear. This study was conducted to investigate the impacts of apatinib on the biological function and its potential mechanism of colon cancer cells in vitro. Materials and Methods:The effect of apatinib in colon cancer cells were detected by assessing cell viability, migration and invasion capabilities. Apoptosis cells and the cell cycle distribution of colon cancer cells were analyzed by flow cytometry. The potential mechanism was investigated via autophagy related proteins and pathways in vitro. Results: The proliferation, migration and invasion of colon cancer cells were inhibited when they were treated with different concentration of apatinib (20, 40 μM). When HCT116 and SW480 cells were treated with apatinib at the concentration of 20 μM, the apoptosis percentage were 3.7% and 5.8% respectively. As the drug concentration increased to 40μΜ, the the apoptosis percentage increased to 11.9% and 13.5%. Meanwhile, cell cycle was also altered. Furthermore, apatinib inhibited the expression of AKT-mTOR signaling pathway and increased the expression of LC3-Ⅱ. Conclusion: Apatinib can significantly inhibit the malignant phenotype of colon cancer cells, and it was involved in regulation of autophagy.
https://ijbms.mums.ac.ir/article_9263_1e1c4ccdbf26d0cc6f0a4ba62bcfcdb9.pdf
2017-09-01
990
995
10.22038/ijbms.2017.9263
Apatinib
Apoptosis
Autophagy
Colon cancer
Migration
mTOR
Wu
Lu
1
Department of Gastroenterology, Renmin Hospital of Wuhan University, Wuhan, 430060, Hubei province, China
AUTHOR
He
Ke
2
Department of General Surgery, Guangdong Second Provincial General Hospital, Guangzhou, Guangdong, China
AUTHOR
Ding
Qianshan
3
Department of Gastroenterology, Renmin Hospital of Wuhan University, Wuhan, 430060, Hubei province, China
AUTHOR
Wang
Zhen
4
Jiangsu Hengrui Medicine Co, Ltd, Lian yungang, 222047, China
AUTHOR
Xiang
Guoan
5
Department of General Surgery, Guangdong Second Provincial General Hospital, Guangzhou, Guangdong, China
AUTHOR
Yu
Honggang
yhg_rmhwh@163.com
6
Department of Gastroenterology, Renmin Hospital of Wuhan University, Wuhan, 430060, Hubei province, China
LEAD_AUTHOR
1. Brenner H, Kloor M, Pox CP. Colorectal cancer. Lancet 2014; 383:1437.
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2. bParkin DM. Global cancer statistics in the year 2000. Lancet Oncol 2001; 2:533-543.
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3. Gill S, Thomas RR, Goldberg RM. Colorectal cancer chemotherapy. Aliment Pharmacol Ther 2003; 18:683-692.
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4. Hu T, Li Z, Gao CY, Cho CH. Mechanisms of drug resistance in colon cancer and its therapeutic strategies. World J Gastroenterol 2016; 22:6876-6889.
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5. Thomas H, Coley HM. Overcoming multidrug resistance in cancer: an update on the clinical strategy of inhibiting p-glycoprotein. Cancer Control 2003; 10:159-165.
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6. Chatterjee S, Heukamp LC, Siobal M, Schottle J, Wieczorek C, Peifer M, et al. Tumor VEGF:VEGFR2 autocrine feed-forward loop triggers angiogenesis in lung cancer. J Clin Invest 2013; 123:1732-1740.
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8. Jayson GC, Kerbel R, Ellis LM, Harris AL. Antiangiogenic therapy in oncology: current status and future directions. Lancet 2016; 388:518-529.
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9. Roviello G, Ravelli A, Polom K, Petrioli R, Marano L, Marrelli D, et al. Apatinib: A novel receptor tyrosine kinase inhibitor for the treatment of gastric cancer. Cancer Lett 2016; 372:187-191.
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10. Ding J, Chen X, Gao Z, Dai X, Li L, Xie C, et al. Metabolism and pharmacokinetics of novel selective vascular endothelial growth factor receptor-2 inhibitor apatinib in humans. Drug Metab 2013; 41:1195-1210.
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13. Scott AJ, Messersmith WA, Jimeno A. Apatinib: a promising oral antiangiogenic agent in the treatment of multiple solid tumors. Drugs Today 2015; 51:223-229.
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14. Yang J, Carra S, Zhu WG, Kampinga HH. The regulation of the autophagic network and its implications for human disease. Int J Biol Sci 2013; 9:1121-1133.
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15. Aoyama T, Yoshikawa T. Targeted therapy: Apatinib - new third-line option for refractory gastric or GEJ cancer. Nat Rev Clin Oncol 2016; 13:268-2670.
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16. Roviello G, Ravelli A, Fiaschi AI, Cappelletti MR, Gobbi A, Senti C, et al. Apatinib for the treatment of gastric cancer. Exp Rev Gastroenterol Hepatol 2016; 10:887-892.
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21. Fornaro L, Vasile E, Falcone A. Apatinib in Advanced Gastric Cancer: A Doubtful Step Forward. J Clin Oncol 2016; pii: JCO686931.
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27
ORIGINAL_ARTICLE
The effect of sodium thiopental as a GABA mimetic drug in neonatal period on expression of GAD65 and GAD67 genes in hippocampus of newborn and adult male rats
Objective(s): Development of the nervous system in human and most animals is continued after the birth. Critical role of this period in generation and specialization of the neuronal circuits is confirmed in numerous studies. Any pharmacological intervention in this period may result in structural, functional or behavioral abnormalities. In this study, sodium thiopental a GABA mimetic drug was administrated to newborn rats and their GAD65 and GAD67 expression in hippocampus was evaluated before and after puberty. Materials and Methods: Newborn male Wistar rats were received sodium thiopental (35 mg/kg) daily for 11 days (from 4 to 14 days after birth). Expression of GAD65 and GAD67 in their hippocampus was compared with control groups in 15 and 45 days after birth with RT-qPCR method. Results: Significant down regulation of GAD65 and GAD67 gene expression was observed in treated rats compared with control group in 45 days after birth animals. But no significant difference was shown between experimental and control groups 15 days after birth animals. Conclusion: The effect of sodium thiopental on GAD65 and GAD67 expression only at adult rats showed a latent period of influence which can be attributed to dosage or intension of sodium thiopental neurotoxicity. Significant down regulation of GAD65 and GAD67 showed unwanted effect of sodium thiopental as GABA mimetic drug in critical period of development.
https://ijbms.mums.ac.ir/article_9264_d726d25ed460dc8c6e953c67dbf0528c.pdf
2017-09-01
996
1001
10.22038/ijbms.2017.9264
Gamma aminobutyric acid
Glutamate decarboxylase 1
Glutamate decarboxylase 2
Real-time polymerase chain reaction
Thiopental
Masoud
Naseri
masoudnaseri@stu.um.ac.ir
1
Division of Physiology, Department of Basic Sciences, Faculty of Veterinary Medicine, Ferdowsi University of Mashhad, Mashhad, Iran
AUTHOR
Abbas
Parham
parham@um.ac.ir
2
Division of Physiology, Department of Basic Sciences, Faculty of Veterinary Medicine, Ferdowsi University of Mashhad, Mashhad, Iran
AUTHOR
Ali
Moghimi
moghimi@un.ac.ir
3
Rayan Center for Neuroscience and Behavior, Department of Biology, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran
LEAD_AUTHOR
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23.Asada H, Kawamura Y, Maruyama K, Kume H, Ding RG, Kanbara N, et al. Cleft palate and decreased brain gamma-aminobutyric acid in mice lacking the 67-kDa isoform of glutamic acid decarboxylase. Proc Natl Acad Sci U S A 1997; 94:6496-6499.
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24.Hyde TM, Lipska BK, Ali T, Mathew SV, Law AJ, Metitiri OE, et al. Expression of GABA signaling molecules KCC2, NKCC1, and GAD1 in cortical development and schizophrenia. J Neurosci 2011; 31:11088-11095.
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25.Charych EI, Liu F, Moss SJ, Brandon NJ. GABA(A) receptors and their associated proteins: implications in the etiology and treatment of schizophrenia and related disorders. Neuropharmacology 2009; 57:481-495.
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27.Heckers S, Konradi C. GABAergic mechanisms of hippocampal hyperactivity in schizophrenia. Schizophr Res 2015; 167:4-11.
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30.LoTurco JJ, Owens DF, Heath MJ, Davis MB, Kriegstein AR. GABA and glutamate depolarize cortical progenitor cells and inhibit DNA synthesis. Neuron 1995; 15:1287-1298.
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31.Obrietan K, van den Pol AN. GABA neurotransmission in the hypothalamus: developmental reversal from Ca2+ elevating to depressing. J Neurosci 1995; 15:5065-5077.
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37.Gargiulo S, Greco A, Gramanzini M, Esposito S, Affuso A, Brunetti A, et al. Mice anesthesia, analgesia, and care, Part I: anesthetic considerations in preclinical research. ILAR J 2012; 53:E55-E69.
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38.Kaila K. Ionic basis of GABAA receptor channel function in the nervous system. Prog Neurobiol 1994; 42:489-537.
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39.Yamada J, Okabe A, Toyoda H, Kilb W, Luhmann HJ, Fukuda A. Cl- uptake promoting depolarizing GABA actions in immature rat neocortical neurones is mediated by NKCC1. J Physiol 2004; 557:829-841.
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40.Blaesse P, Airaksinen MS, Rivera C, Kaila K. Cation-chloride cotransporters and neuronal function. Neuron 2009; 61:820-838.
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41.Owens DF, Kriegstein AR. Is there more to GABA than synaptic inhibition? Nat Rev Neurosci 2002; 3:715-727.
41
42.Zhang Z, Sun QQ. The balance between excitation and inhibition and functional sensory processing in the somatosensory cortex. Int Rev Neurobiol 2011; 97:305-333.
42
ORIGINAL_ARTICLE
Effects of mild hypothermia on expression of NF-E2-related factor 2 and heme-oxygenase-1 in cerebral cortex and hippocampus after cardiopulmonary resuscitation in rats
Objective(s): The aim of this study was to investigate the effects of mild hypothermia on expression of NF-E2-related factor 2 (Nrf2) and heme-oxygenase-1 (HO-1) of rat cerebral cortex and hippocampus after cardiopulmonary resuscitation and further investigate the possible mechanism of action. Material and Methods:To copy an asphyxia heart arrest model, Sprague Dawley rats were randomly divided into normothermia group, mild hypothermia group before restoration of spontaneous circulation (ROSC), and mild hypothermia group after ROSC. Body temperature in normothermia group was maintained at 37.5-39℃, while in mild hypothermia group maintained at 32-34 °C by surface cooling with the ice pack. Each group then divided into three subgroups: 15 min, 30 min, and 60 min. Reverse transcription-polymerase chain reaction (RT-PCR) was performed to detect the expression of Nrf2 and HO-1 mRNA in cerebral cortex and hippocampus. Hematoxylin-eosin (H&E) staining was performed to observe histological changes. Immunohistochemistry was performed to detect the expression of Nrf2 and HO-1 protein expression. Results: The expression of Nrf2 and HO-1 in cerebral cortex and hippocampus after cardiopulmonary resuscitation (CPR) was significantly increased and mild hypothermia up regulated this level. HE staining showed that mild hypothermia significantly improved neuronal injury. Conclusion: Mild hypothermia has neuroprotective effects on cerebral ischemia/reperfusion injury after cardiac arrest. The possible mechanism is that Nrf2-ARE pathway in cerebral cortex and hippocampus after CPR is activated.
https://ijbms.mums.ac.ir/article_9266_5908f37bcbcaac27f5390f9370f71277.pdf
2017-09-01
1002
1008
10.22038/ijbms.2017.9266
Heart Arrest
Heme-oxygenase-1
Mild hypothermia
Neuroprotection
NF-E2-related factor 2
Nrf2
DunLing
Xia
1
Department of Emergency, the First Affiliated Hospital of Anhui Medical University, Hefei, Anhui Province, China
AUTHOR
Hong
Zhang
hzhang19@126.com
2
Department of Emergency, the First Affiliated Hospital of Anhui Medical University, Hefei, Anhui Province, China
LEAD_AUTHOR
1. Ali B, Zafari AM. Narrative review: cardiopulmonary resuscitation and emergency cardiovascular care: review of the current guidelines. Ann Intern Med 2007; 147:171–179.
1
2. Hua W, Zhang LF, Wu YF, Liu XQ, Guo DS, Zhou XL, et al. Incidence of sudden cardic death in China-analysis of 4 regional populations. JACC 2009; 54:1110-1118.
2
3. Robert WN, Jerry PN, Christophe A. Post–cardiac arrest syndrome: epidemiology, pathophysiology, treatment, and Prognostication a consensus statement from the international liaison committee on resuscitation (American Heart Association, Australian and New Zealand Council on Resuscitation, European Resuscitation Council, Heart and Stroke Foundation of Canada, InterAmerican Heart Foundation, Resuscitation Council of Asia, and the Resuscitation Council of Southern Africa); the American Heart Association Emergency Cardiovascular Care Committee; the Council on Cardiovascular Surgery and Anesthesia; the Council on Cardiopulmonary, Perioperative, and Critical Care; the Council on Clinical Cardiology; and the Stroke Council. Circulation 2008; 118:2452-2483.
3
4. Laver S, Farrow C, Turner D, Nolan J. Mode of death after admission to an intensive care unit following cardiac arrest. Intensive Care Med 2004; 30:2126–2128.
4
5. Navaz K, Romergryko GG. Post-cardiac arrest syndrome update on brain injury management and prognostication. Curr Treat Options Neurol 2011; 13:191-203.
5
6. Kobayash M, Yamamoto M. Nrf2-keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Adv Enzyme Regul 2006; 46:113-140.
6
7. Chan KH, Ng MK, Stocker R. Haem oxygenase-1 and cardiovascular disease: mechanisms and therapeutic potential. Clin Sci 2011; 120:493-504.
7
8. Polderman KH. Mechanisms of action, physiological effects, and complications of hypothermia. Crit Care Med 2009; 37:S186–202.
8
9. Zhao H, Chen Y. Effects of mild hypothermia therapy on the levels of glutathione in rabbit blood and cerebrospinal fluid after cardiopulmonary resuscitation. Iran J Basic Med Sci 2015; 18:194-198.
9
10. Deniz T, Agalar C, Ozdogan M, Edremitlioglu M, Eryilmaz M, Devay SD, et al. Mild hypothermia improves survival during hemorrhagic shock without affecting bacterial translocation. J Invest Surg 2009; 22:22-28.
10
11. Takeuchi I, Takehana H, Satoh D, Fukaya H, Tamura Y, Nishi M, et al. Effect of hypothermia therapy after outpatient cardiac arrest due to ventricular fibrillation. Circ J 2009; 73:1877-1880.
11
12. Lu J, Shen Y, Qian H, Liu L, Zhou B, Xiao Y, et al. Effects of mild hypothermia on the ROS and expression of caspase-3 mRNA and LC3 of hippocampus nerve cells in rats after cardiopulmonary resuscitation. World J Emerg Med 2014; 4:298-304.
12
13. Idris AH, Becker LB, Ornato JP, Hedges JR, Bircher NG, Chandra NC, et al. Utstein-style guidelines for uniform reporting of laboratory CPR research. A statement for healthcare professionals from a task force of the American Heart Association, the American College of Emergency Physicians, the American College of Cardiology, the European Resuscitation Council, the Heart and Stroke Foundation of Canada, the European Resuscitation Care Medicine, the Safar Center for Resuscitation Research, and the Society for Academic Emergency Medicine. Writing Group. Circulation 1996; 94:2324-2336.
13
14. Bano D, Nicotera P. Ca2+ signals and neuronal death in brain ischemia. Stroke 2007; 38:674-676.
14
15. Geocadin RG, Koenig MA, Stevens RD, Peberdy MA. Intensive care for brain injury after cardiac arrest: therapeutic hypothermia and related neuroprotective strategies. Crit Care Clin 2006; 22:619-636.
15
16. Lee JM, Shih AY, Murphy TH, Johnson JA. NF-E2-related factor-2 mediateds neuroproteciton against mitochondrial complex Ⅰ inhibitors and increased concentrations of intracellular calcium in primary cortical neurons. J Biol Chem 2003; 278:37948-37956.
16
17. Mizuno K, Kume T, Muto C, Takada-Takatori Y, Izumi Y, Sugimoto H, et al. Glutathione biosynthesis via activation of the nuclear factor E2-related factor 2 (Nrf2)--antioxidant-response element (ARE) pathway is essential for neuroprotective effects of sulforaphane and 6-(methylsulfinyl) hexyl isothiocyanate. J Pharmacol Sci 2011; 115:320-328.
17
18. Calkins MJ, Jakel RJ, Johnson DA, Chan K, Kan YW, Johnson JA. Protection from mitochondrial complex Ⅱ inhibition in vitro and in vivo by Nrf2-mediated transcription. Proc Natl Acad Sci USA 2005; 102:244-249.
18
19. Chen MJ, Wong CH, Peng ZF, Manikandan J, Melendez AJ, Tan TM, et al. A global transcriptomic view of the multifaceted role of glutathione peroxidase-1 in cerebral ischemic-reperfusion injury. Free Radic Biol Med 2011; 50:736-748.
19
20. Grigore AM, Murray CF, Ramakrishna H, Djaiani G. A Core Review of Temperature Regimens and Neuroprotection During Cardiopulmonary Bypass: Does Rewarming Rate Matter? Anesth. Analg 2009; 109:1741 – 1751.
20
ORIGINAL_ARTICLE
Therapeutic potential of genistein in ovariectomy-induced pancreatic injury in diabetic rats: The regulation of MAPK pathway and apoptosis
Objective(s): Genistein, as a phytoestrogen found in legumes, has several biological activities in general and anti-diabetic activity particularly. In this study, we investigated the effect of genistein on proteins involved in β-cell proliferation, survival and apoptosis to further reveal its anti-diabetic potential in the ovariectomized diabetic rat. Materials and Methods: We used three-month-old female Wistar rats that either underwent ovariectomy (OVX) or received a sham surgery (Sham). In a subsequent series of experiments, OVX rats received high-fat diet and low dose STZ to induce diabetes (OVX.D) and genistein treatment (OVX.D.G). Western blot analysis was used for the assessment of phosphorylation of ERK1/2 and AKT and expression of Bcl-2 and caspase-3 in pancreas tissue. Hematoxylin-Eosin (H&E) staining was used for histopathological assessment. Results: Genistein induced AKT and ERK1/2 phosphorylation protein expression of Bcl-2 in the pancreas. In addition, genistein suppressed protein level of caspase-3. Administration of genistein significantly improved hyperglycemia in ovariectomized diabetic rat, concomitant with improved islet β-cell morphology and mass. Conclusion: These findings suggest that the beneficial antidiabetic effect of genistein partially mediated by directly modulating pancreatic β-cell function via activation of the AKT, ERK1/2, and Bcl-2, as cell survival and anti-apoptotic factors, and decreasing of proapoptotic caspase-3.
https://ijbms.mums.ac.ir/article_9269_5d15a143ae971807d915b3a1523b177b.pdf
2017-09-01
1009
1015
10.22038/ijbms.2017.9269
AKT/ERK
Bcl-2
Caspase-3
Diabetes
Genistein
Ovariectomy
Hadi
Yousefi
1
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Pouran
Karimi
2
Neurosciences Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Alireza
Alihemmati
hemmati@yahoo.com
3
Department of Histology & Embryology, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Mohmmad Reza
Alipour
4
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Parisa
Habibi
dr.habibi@yahoo.com
5
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
AUTHOR
Nasser
Ahmadiasl
n.ahmadiacl@gmail.com
6
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
LEAD_AUTHOR
1. Carr MC. The emergence of the metabolic syndrome with menopause. JCEM 2003; 88:2404-2411.
1
2. Brand JS, van der Schouw YT, Onland-Moret NC, Sharp SJ, Ong KK, Khaw K-T, et al. Age at menopause, reproductive life Span, and Type 2 diabetes risk results from the EPIC-InterAct study. Diabetes Care 2013; 36:1012-61019.
2
3. Kim C, Edelstein SL, Crandall JP, Dabelea D, Kitabchi AE, Hamman RF, et al. Menopause and risk of diabetes in the Diabetes Prevention Program. Menopause 2011; 18:857.
3
4. Bonds D, Lasser N, Qi L, Brzyski R, Caan B, Heiss G, et al. The effect of conjugated equine oestrogen on diabetes incidence: the Women’s Health Initiative randomised trial. Diabetologia 2006; 49:459-468.
4
5. Appiah D, Winters SJ, Hornung CA. Bilateral oophorectomy and the risk of incident diabetes in postmenopausal women. Diabetes Care 2014; 37:725-733.
5
6. Pirimoglu Z, Arslan C, Buyukbayrak E, Kars B, Karsidag Y, Unal O, et al. Glucose tolerance of premenopausal women after menopause due to surgical removal of ovaries. Climacteric 2011; 14:453-457.
6
7. Gilbert ER, Liu D. Anti-diabetic functions of soy isoflavone genistein: mechanisms underlying its effects on pancreatic β-cell function. Food Funct 2013; 4:200-212.
7
8. Jayagopal V, Albertazzi P, Kilpatrick ES, Howarth EM, Jennings PE, Hepburn DA, et al. Beneficial effects of soy phytoestrogen intake in postmenopausal women with type 2 diabetes. Diabetes Care 2002; 25:1709-1714.
8
9. Lavigne C, Marette A, Jacques H. Cod and soy proteins compared with casein improve glucose tolerance and insulin sensitivity in rats. Am J Physiol Endocrinol Metab 2000; 278:E491-E500.
9
10. Park SA, Choi MS, Cho SY, Seo JS, Jung UJ, Kim MJ, et al. Genistein and daidzein modulate hepatic glucose and lipid regulating enzyme activities in C57BL/KsJ-db/db mice. Life Sci 2006; 79:1207-1213.
10
11. Cheng SY, Shaw NS, Tsai KS, Chen CY. The hypoglycemic effects of soy isoflavones on postmenopausal women.J Womens Health (Larchmt) 2004; 13:1080-1086.
11
12. Habibi P, Alihemmati A, NourAzar A, Yousefi H, Mortazavi S, Ahmadiasl N. Expression of the Mir-133 and Bcl-2 could be affected by swimming training in the heart of ovariectomized rats. Iran J Bacic Med Sci 2016; 19:381-387.
12
13. Srinivasan K, Ramarao P. Animal models in type 2 diabetes research: an overview. Indian J Med Res 2007; 125:451.
13
14.Yousefi H, Alihemmati A, Karimi P, Alipour MR, Habibi P, Ahmadiasl N. Effect of genistein on expression of pancreatic SIRT1, inflammatory cytokines and histological changes in ovariectomized diabetic rat. Iran J Bacic Med Sci 2017; 20:423-429.
14
15. Nikasa M, Karimi P, Rajavand H, Afshari F, Jafarlou M, Soltanali M. High cholesterol diet increases expression of cholesterol 24-hydroxylase and BACE1 in rat hippocampi: implications for the effect of diet cholesterol on memory. IRCMJ 2016.
15
16. Lee JS. Effects of soy protein and genistein on blood glucose, antioxidant enzyme activities, and lipid profile in streptozotocin-induced diabetic rats. Life Sci 2006; 79:1578-1584.
16
17. Skim F, Lazrek H, Kaaya A, El Amri H, Jana M. Pharmacological studies of two antidiabetic plants: Globularia alypum and Zygophyllum gaetulum. Therapie 1998; 54:711-715.
17
18. Dickson LM, Rhodes CJ. Pancreatic β-cell growth and survival in the onset of type 2 diabetes: a role for protein kinase B in the Akt? Am J Physiol Endocrinol Metab 2004; 287:E192-E198.
18
19. Acconcia F, Kumar R. Signaling regulation of genomic and nongenomic functions of estrogen receptors. Cancer Lett 2006; 238:1-14.
19
20. Acconcia F, Ascenzi P, Bocedi A, Spisni E, Tomasi V, Trentalance A, et al. Palmitoylation-dependent estrogen receptor α membrane localization: regulation by 17β-estradiol. Mol Biol Cell 2005; 16:231-237.
20
21. Wang A, Liu D, Luo J, Suh KS, Moore W, Alkhalidy H. Phytochemical genistein promotes pancreatic beta-cell survival and exerts anti-diabetic effect via GPR30-mediated mechanism (1045.44). FASEB J 2014; 28:1045.1044.
21
22. Wijesekara N, Krishnamurthy M, Bhattacharjee A, Suhail A, Sweeney G, Wheeler MB. Adiponectin-induced ERK and Akt phosphorylation protects against pancreatic beta cell apoptosis and increases insulin gene expression and secretion. J Biol Chem 2010; 285:33623-33631.
22
23. Lingohr MK, Dickson LM, McCuaig JF, Hugl SR, Twardzik DR, Rhodes CJ. Activation of IRS-2—Mediated signal transduction by IGF-1, but not TGF-α or EGF, augments pancreatic β-Cell proliferation. Diabetes 2002; 51:966-976.
23
24. Fu Z, Zhang W, Zhen W, Lum H, Nadler J, Bassaganya-Riera J, et al. Genistein induces pancreatic β-cell proliferation through activation of multiple signaling pathways and prevents insulin-deficient diabetes in mice. Endocrinology 2010; 151:3026-3037.
24
25. Liadis N, Murakami K, Eweida M, Elford AR, Sheu L, Gaisano HY, et al. Caspase-3-dependent β-cell apoptosis in the initiation of autoimmune diabetes mellitus. Mol Cell Biol 2005; 25:3620-3629.
25
26. Duxbury MS, Ito H, Benoit E, Zinner MJ, Ashley SW, Whang EE. RNA interference targeting focal adhesion kinase enhances pancreatic adenocarcinoma gemcitabine chemosensitivity. Biochem Biophys Res Commun 2003; 311:786-792.
26
27. El-Rayes BF, Ali S, Ali IF, Philip PA, Abbruzzese J, Sarkar FH. Potentiation of the effect of erlotinib by genistein in pancreatic cancer: the role of Akt and nuclear factor-κB. Cancer Res 2006; 66:10553-10559.
27
28. Aras AB, Guven M, Akman T, Alacam H, Kalkan Y, Silan C, et al. Genistein exerts neuroprotective effect on focal cerebral ischemia injury in rats. Inflam 2015; 38:1311-1321.
28
ORIGINAL_ARTICLE
Prenatal exposure to TAK242 affects the childhood autism in offspring in animal models of autism spectrum disorder
Objective(s): To evaluate whether prenatal exposure to TAK242 affects childhood autism in the offspring in animal models of autism spectrum disorder (ASD). Materials and Methods:The pregnant rats were pseudo-randomly divided into three groups, the ASD model group, the TAK242 treatment group, and the control group. The ASD model was constructed by injecting IP with LPS. The blood samples from 1-month-old offspring were collected for cytokine evaluation and the social interaction test was used in the offspring of ASD rats. Rats were killed and the hippocampus, cerebral cortex, and cerebellum were used for the immunohistochemical study. Results: As compared to the control, the levels of IFN-γ, IL-1β, IL-2, and IL-6 were significantly increased (P<0.05), and the levels of IL-4, IL-10, and TGF-β were significantly decreased (P <0.05) in the offspring of ASD rats; whereas those cytokines were significantly reversed after prenatal exposure to TAK242 (P<0.05). The hesitation time and none-social interaction time were significantly increased as compared to the control (P<0.05); whereas they were both decreased after prenatal exposure to TAK242 (P<0.05). This was contrary to the social interaction time (P<0.05). The expression of GFAP and IBA1 in the cortex, hippocampus, and cerebellum were stronger in the LPS group as compared to control group, and this effect was reversed after prenatal exposure to TAK242. Conclusion: Prenatal exposure to TAK242 affects serum cytokines levels and the social interaction time in rat offspring in animal models of ASD.
https://ijbms.mums.ac.ir/article_9270_013d903394c604698ba175885c2252c0.pdf
2017-09-01
1016
1020
10.22038/ijbms.2017.9270
Autism spectrum disorder
Childhood autism in offspring
Serum cytokines
Social interaction time
TAK242
Wistar rat
Xiaoyan
Xu
cath_yan@126.com
1
The Children’s Neurorehabilitation Center, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
AUTHOR
De
Wu
derk_wu@163.com
2
The Children’s Neurorehabilitation Center, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
AUTHOR
Shu
Hou
hou_shu@sohu.com
3
Department of Pediatrics, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
AUTHOR
Jing
Zhu
zhujing_ped@163.com
4
The Children’s Neurorehabilitation Center, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
AUTHOR
Jing
Li
jingjinglij@163.com
5
The Children’s Neurorehabilitation Center, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
AUTHOR
Jiulai
Tang
tang_jiulai@sohu.com
6
The Children’s Neurorehabilitation Center, the First Affiliated Hospital, Anhui Medical University, Hefei 230022, Anhui, China
LEAD_AUTHOR
1. Moy SS, Nadler JJ, Magnuson TR, Crawley JN. Mouse models of autism spectrum disorders: the challenge for behavioral genetics. Am J Med Genet C Semin Med Genet 2006; 142c:40-51.
1
2. Malkova NV, Yu CZ, Hsiao EY, Moore MJ, Patterson PH. Maternal immune activation yields offspring displaying mouse versions of the three core symptoms of autism. Brain Behav Immun 2012; 26:607-616.
2
3. Wink LK, Plawecki MH, Erickson CA, Stigler KA, Mcdougle CJ. Emerging drugs for the treatment of symptoms associated with autism spectrum disorders. Exp Opin Emerg Drugs 2010; 15:481-494.
3
4. Pardo CA, Vargas DL, Zimmerman AW. Immunity, neuroglia and neuroinflammation in autism. Int Rev Psychiatry 2006; 17:485-495.
4
5. Li X, Chauhn AA, Shiekh AAM, Patil AS, Chauhn BV, Li XM, et al. Elevated immune response in the brain of autistic patients. J Neuroimmunol 2009; 207:111-116.
5
6. Medzhitov R. Medzhitov R. Toll-like receptors and innate immunity. Nat Rev Immunol Nat Rev Immunol 2001; 1:135-145.
6
7. Lucas K, Maes M. Role of the toll like Receptor (TLR) radical cycle in chronic inflammation: possible treatments targeting the TLR4 pathway. Mol Neurobiol 2013; 48:190-204.
7
8. Rice TW, Wheeler AP, Bernard GR, Vincent JL, Angus DC, Aikawa N, et al. A randomized, double-blind, placebo-controlled trial of TAK-242 for the treatment of severe sepsis. Crit Care Med 2010; 38:1685-1694.
8
9. Kawamoto T, Ii M, Kitazaki T, Iizawa Y, Kimura H. TAK-242 selectively suppresses Toll-like receptor 4-signaling mediated by the intracellular domain. Eur J Pharmacol 2008; 584:40-48.
9
10. Xuan ICY. The maternal immune activation mouse model of autism spectrum disorders. Master 2013; 4:e400.
10
11. Goines PE, Croen LA, Braunschweig D, Yoshida CK, Grether J, Hansen R, et al. Increased midgestational IFN-γ, IL-4 and IL-5 in women bearing a child with autism: A case-control study. Mol Autism 2011; 2:13.
11
12. Brodkin ES, Hagemann A, Nemetski SM, Silver LM. Social approach-avoidance behavior of inbred mouse strains towards DBA/2 mice. Brain Res 2004; 1002:151–157.
12
13. Ferretti CJ, Hollander E. The role of inflammation in Autism Spectrum Disorder. Immunol Psychiatry 2015; 275-312.
13
14. Aderem A, Ulevitch RJ. Toll-like receptors in the induction of the innate immune response. Nature 2000; 406:782-787.
14
15. Sato A, Mizuguchi M, Ikeda K. Social interaction test: a sensitive method for examining autism-related behavioral deficits. Protocol Exchange 2013.
15
16. de Oliveira WH, Ak DSN, de França ME, Dos Santos LA, Lós DB, Santos Rocha SW, et al. Effects of metformin on inflammation and short-term memory in streptozotocin-induced diabetic mice. Brain Res 2016; 1644:149-160.
16
17. Park T, Chen H, Kevala K, Lee JW, Kim HY. N-Docosahexaenoylethanolamine ameliorates LPS-induced neuroinflammation via cAMP/PKA-dependent signaling. J Neuroinflammation 2016; 13:284.
17
18. Norden DM, Trojanowski PJ, Villanueva E, Navarro E, Godbout JP. Sequential activation of microglia and astrocyte cytokine expression precedes increased iba-1 or GFAP immunoreactivity following systemic immune challenge. Glia 2015; 64:300-316.
18
ORIGINAL_ARTICLE
shRNA-mediated downregulation of α-N-Acetylgalactosaminidase inhibits migration and invasion of cancer cell lines
Objective(s): Extracellular matrix (ECM) is composed of many kinds of glycoproteins containing glycosaminoglycans (GAGs) moiety. The research was conducted based on the N-Acetylgalactosamine (GalNAc) degradation of ECM components by α-N-acetylgalactosaminidase (Nagalase) which facilitates migration and invasion of cancer cells. This study aims to investigate the effects of Naga-shRNA downregulation on migration and invasion of cancer cell lines. Materials and Methods: In this study, MCF-7 cell line (human mammary carcinoma cell line) and A2780 (human ovarian carcinoma cell line) were used. The level of normalized Naga expression and Nagalase protein were evaluated by quantitative polymerase chain reaction and enzyme-linked immunosorbent assay/western blotting, respectively. Migration and invasion were determined using transwell assays, and statistical analysis was carried out by ANOVA test. Results: Response to transduction by shRNA compared to the control group, migrative and invasive properties of the transfected cells were significantly inhibited. Conclusion: These results indicate that Nagalase may have an important role in migration and invasion of cancer cells and can be considered as a candidate for further studies.
https://ijbms.mums.ac.ir/article_9271_452a27516d93e28ba9d3c97acf8e767c.pdf
2017-09-01
1021
1028
10.22038/ijbms.2017.9271
Alpha-N-Acetylgalactosamini dase
Cancer
Extracellular matrix
Invasion
Migration
shRNA
Ehsan
Saburi
1
Department of Molecular Medicine & Genetics, Zanjan University of Medical Sciences, Zanjan, Iran
AUTHOR
Jalil
Tavakolafshari
2
Department of Immunogenetics, Buali Institute, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Yousef
Mortazavi
mortazaviyou@yahoo.com
3
Department of Medical Biotechnology and Nanotechnology, Zanjan University of Medical Sciences, Zanjan, Iran
LEAD_AUTHOR
Alireza
Biglari
4
Department of Molecular Medicine & Genetics, Zanjan University of Medical Sciences, Zanjan, Iran
AUTHOR
Seyed Abbas
Mirzaei
dr-amirzaei@yahoo.com
5
Cellular and Molecular Research Center, Basic Health Sciences Institute, Shahrekord University Of Medical Sciences, Shahrekord, Iran
AUTHOR
Samad
Nadri
nadri_s@zumc.ac.ir
6
Department of Medical Biotechnology and Nanotechnology, Zanjan University of Medical Sciences, Zanjan, Iran
AUTHOR
1. Torre LA, Siegel RL, Ward EM, Jemal A. Global cancer incidence and mortality rates and trends--an update. Cancer Epidemiol Biomarkers Prev 2016; 25:16-27.
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23. Pacini S, Punzi T, Morucci G, Gulisano M, Ruggiero M. Effects of vitamin D-binding protein-derived macrophage-activating factor on human breast cancer cells. Anticancer Res 2012; 32:45-52.
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26. Thyer L, Ward E, Smith R, Fiore MG, Magherini S, Branca JJ, et al. A novel role for a major component of the vitamin D axis: vitamin D binding protein-derived macrophage activating factor induces human breast cancer cell apoptosis through stimulation of macrophages. Nutrients 2013; 5:2577-2589.
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28. Elahian F, Kalalinia F, Behravan J. Dexamethasone downregulates BCRP mRNA and protein expression in breast cancer cell lines. Oncol Res 2009; 18:9-15.
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29. Wang K, Wu F, Seo BR, Fischbach C, Chen W, Hsu L, et al. Breast cancer cells alter the dynamics of stromal fibronectin-collagen interactions. Matrix Biol 2016; 60:86-95.
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30. Theocharis AD, Skandalis SS, Gialeli C, Karamanos NK. Extracellular matrix structure. Adv Drug Deliv Rev 2016; 97:4-27.
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31. Varki A, Freeze HH. Glycans in Acquired Human Diseases. In: Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, et al. editors. Essentials of Glycobiology. 2nd ed. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009. Chapter 43.
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32. Sugahara K, Mikami T, Uyama T, Mizuguchi S, Nomura K, Kitagawa H. Recent advances in the structural biology of chondroitin sulfate and dermatan sulfate. Curr Opin Struct Biol 2003; 13:612-620.
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33. Lo CM, Wang HB, Dembo M, Wang YL. Cell movement is guided by the rigidity of the substrate. Biophys J 2000; 79:144-152.
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34. Murakami T, Murakami S, Fuyama Y, Taguchi T, Ohtsuka A. The extracellular matrix in the mature brain: its reactions to endo-alpha-N-acetylgalactosaminidase and collagenase. Ital J Anat Embryol 2001; 106:475-480.
34
35. Murakami T, Ohtsuka A, Su WD, Taguchi T, Oohashi T, Abe K, et al. The extracellular matrix in the mouse brain: its reactions to endo-alpha-N-acetylgalactosaminidase and certain other enzymes. Arch Histol Cytol 1999; 62:273-281.
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36. Murakami T, Murakami S, Fuyama Y, Taguchi T, Ohtsuka A. The extracellular matrix in the mature brain: its reactions to endo-alpha-N-acetylgalactosaminidase and collagenase. Ital J Anat Embryol 2001; 106:475-480.
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37. Springer NL, Fischbach C. Biomaterials approaches to modeling macrophage-extracellular matrix interactions in the tumor microenvironment. Curr Opin Biotechnol 2016; 40:16-23.
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38. Saburi E, Saburi A, Ghanei M. Promising role for Gc-MAF in cancer immunotherapy: from bench to bedside approach. Caspian J Intern Med 2017; 8:228-238.
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39. Epp A, Sullivan KC, Herr AB, Strait RT. Immunoglobulin glycosylation effects in allergy and immunity. Curr Allergy Asthma Rep 2016; 16:79.
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40. Hayes JM, Frostell A, Cosgrave EF, Struwe WB, Potter O, Davey GP, et al. Fc gamma receptor glycosylation modulates the binding of IgG glycoforms: a requirement for stable antibody interactions. J Proteome Res 2014; 13:5471-5485.
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41. Liu H, Gaza-Bulseco G, Xiang T, Chumsae C. Structural effect of deglycosylation and methionine oxidation on a recombinant monoclonal antibody. Mol Immunol 2008; 45:701-708.
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42. Kazuno S, Furukawa J, Shinohara Y, Murayama K, Fujime M, Ueno T, et al. Glycosylation status of serum immunoglobulin G in patients with prostate diseases. Cancer Med 2016; 5:1137-1146.
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43. Soliman C, Yuriev E, Ramsland PA. Antibody recognition of aberrant glycosylation on the surface of cancer cells. Curr Opin Struct Biol 2016; 44:1-8.
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44. Chen Z, Gulzar ZG, St Hill CA, Walcheck B, Brooks JD. Increased expression of GCNT1 is associated with altered O-glycosylation of PSA, PAP, and MUC1 in human prostate cancers. Prostate 2014; 74:1059-1067.
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46. Brooks SA, Carter TM, Bennett EP, Clausen H, Mandel U. Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer. Acta Histochem 2007; 109:273-284.
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48. Taniuchi K, Cerny RL, Tanouchi A, Kohno K, Kotani N, Honke K, et al. Overexpression of GalNAc-transferase GalNAc-T3 promotes pancreatic cancer cell growth. Oncogene 2011; 30:4843-4854.
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54
ORIGINAL_ARTICLE
Regulation of autophagy by AMP-activated protein kinase/ sirtuin 1 pathway reduces spinal cord neurons damage
Objective(s): AMP-activated protein kinase/sirtuin 1 (AMPK/SIRT1) signaling pathway has been proved to be involved in the regulation of autophagy in various models. The aim of this study was to evaluate the effect of AMPK/SIRT1 pathway on autophagy after spinal cord injury (SCI). Materials and Methods:The SCI model was established in rats in vivo and the primary spinal cord neurons were subjected to mechanical injury (MI) in vitro. The apoptosis in spinal cord tissue and neurons was assessed by TUNEL staining and Hoechst 33342 staining, respectively. The autophagy-related proteins levels were detected by Western blot. The activation of AMPK/SIRT1 pathway was determined by Western blot and immunohistochemical staining. Results: We found that the apoptosis of spinal cord tissue and cell damage of spinal cord neurons was obvious after the trauma. The ratio of LC3II/LC3I and level of p62 were first increased significantly and then decreased after the trauma in vivo and in vitro, indicating the defect in autophagy. The levels of p-AMPK and SIRT1 were increased obviously after the trauma in vivo and in vitro. Further activation of the AMPK/SIRT1 pathway by pretreatment with resveratrol, a confirmed activator of the AMPK/SIRT1 pathway, alleviated the cell damage and promoted the autophagy flux via downregulation of p62 in spinal cord neurons at 24 hr after MI. Conclusion: Our results demonstrate that regulation of autophagy by AMPK/SIRT1 pathway can restrain spinal cord neurons damage, which may be a potential intervention of SCI.
https://ijbms.mums.ac.ir/article_9272_50bfcb7565f4d79271bd59f953eeb9c6.pdf
2017-09-01
1029
1036
10.22038/ijbms.2017.9272
AMPK/SIRT1 pathway
Autophagy flux
p62
Resveratrol
Spinal cord injury
Peng
Yan
yanpeng2017@126.com
1
Department of Orthopaedic Surgery, The First Affiliated Hospital of China Medical University, Shenyang, Liaoning 110001, People’s Republic of China
AUTHOR
Liangjie
Bai
liangjiebai1988@sina.com
2
Department of Orthopaedic Surgery, The First Affiliated Hospital of China Medical University, Shenyang, Liaoning 110001, People’s Republic of China
AUTHOR
Wei
Lu
luweigk@sohu.com
3
Department of Orthopaedic Surgery, The First Affiliated Hospital of China Medical University, Shenyang, Liaoning 110001, People’s Republic of China
AUTHOR
Yuzhong
Gao
yuzhonggaozyd@163.com
4
Department of Orthopaedic Surgery, The First Affiliated Hospital of Jinzhou Medical University, Jinzhou, Liaoning 121001, People’s Republic of China
AUTHOR
Yunlong
Bi
zmcbyl@163.com
5
Department of Orthopaedic Surgery, The First Affiliated Hospital of Jinzhou Medical University, Jinzhou, Liaoning 121001, People’s Republic of China
AUTHOR
Gang
Lv
lvgangjz@126.com
6
Department of Orthopaedic Surgery, The First Affiliated Hospital of China Medical University, Shenyang, Liaoning 110001, People’s Republic of China
LEAD_AUTHOR
1. Wyndaele M, Wyndaele JJ. Incidence, prevalence and epidemiology of spinal cord injury: what learns a worldwide literature survey? Spinal Cord 2006; 44:523-529.
1
2. Karatas Y, Cengiz SL, Esen H, Toker A, Savas C. Effect of Carvedilol on Secondary Damage in Experimental Spinal Cord Injury in Rats. Turk Neurosurg 2015; 25:930-935.
2
3. Impellizzeri D, Ahmad A, Di Paola R, Campolo M, Navarra M, Esposito E, et al. Role of Toll like receptor 4 signaling pathway in the secondary damage induced by experimental spinal cord injury. Immunobiology 2015; 220:1039-1049.
3
4. Wang ZY, Lin JH, Muharram A, Liu WG. Beclin-1-mediated autophagy protects spinal cord neurons against mechanical injury-induced apoptosis. Apoptosis 2014; 19:933-945.
4
5. Tang P, Hou H, Zhang L, Lan X, Mao Z, Liu D, et al. Autophagy reduces neuronal damage and promotes locomotor recovery via inhibition of apoptosis after spinal cord injury in rats. Mol Neurobiol 2014; 49:276-287.
5
6. Lee IH, Cao L, Mostoslavsky R, Lombard DB, Liu J, Bruns NE, et al. A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci U S A 2008; 105:3374-3379.
6
7. Canto C, Jiang LQ, Deshmukh AS, Mataki C, Coste A, Lagouge M, et al. Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle. Cell Metab 2010; 11:213-219.
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8. Kume S, Koya D. Autophagy: A Novel Therapeutic Target for Diabetic Nephropathy. Diabetes Metab J 2015; 39:451-460.
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9. Song YM, Lee YH, Kim JW, Ham DS, Kang ES, Cha BS, et al. Metformin alleviates hepatosteatosis by restoring SIRT1-mediated autophagy induction via an AMP-activated protein kinase-independent pathway. Autophagy 2015; 11:46-59.
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10. Talero E, Alcaide A, Avila-Roman J, Garcia-Maurino S, Vendramini-Costa D, Motilva V. Expression patterns of sirtuin 1-AMPK-autophagy pathway in chronic colitis and inflammation-associated colon neoplasia in IL-10-deficient mice. Int Immunopharmacol 2016; 35:248-256.
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11. Sciarretta S, Hariharan N, Monden Y, Zablocki D, Sadoshima J. Is autophagy in response to ischemia and reperfusion protective or detrimental for the heart? Pediatr Cardiol 2011; 32:275-281.
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12. Wu Y, Li X, Zhu JX, Xie W, Le W, Fan Z, et al. Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease. Neurosignals 2011; 19:163-174.
12
13. Park SY, Lee HR, Lee WS, Shin HK, Kim HY, Hong KW, et al. Cilostazol Modulates Autophagic Degradation of beta-Amyloid Peptide via SIRT1-Coupled LKB1/AMPKalpha Signaling in Neuronal Cells. PLoS One 2016; 11:e0160620.
13
14. Liu J, Yi L, Xiang Z, Zhong J, Zhang H, Sun T. Resveratrol attenuates spinal cord injury-induced inflammatory damage in rat lungs. Int J Clin Exp Pathol 2015; 8:1237-1246.
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15. Zhang D, Xuan J, Zheng BB, Zhou YL, Lin Y, Wu YS, et al. Metformin Improves Functional Recovery After Spinal Cord Injury via Autophagy Flux Stimulation. Mol Neurobiol 2016.
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16. Zhou Y, Zheng B, Ye L, Zhang H, Zhu S, Zheng X, et al. Retinoic Acid Prevents Disruption of Blood-Spinal Cord Barrier by Inducing Autophagic Flux After Spinal Cord Injury. Neurochem Res 2016; 41:813-825.
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17. Que H, Liu Y, Jia Y, Liu S. Establishment and assessment of a simple and easily reproducible incision model of spinal cord neuron cells in vitro. In Vitro Cell Dev Biol Anim 2011; 47:558-564.
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18. Guo Y, Liu S, Zhang X, Wang L, Gao J, Han A, et al. G-CSF promotes autophagy and reduces neural tissue damage after spinal cord injury in mice. Lab Invest 2015; 95:1439-1449.
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19. Wang H, Wang Y, Li D, Liu Z, Zhao Z, Han D, et al. VEGF inhibits the inflammation in spinal cord injury through activation of autophagy. Biochem Biophys Res Commun 2015; 464:453-458.
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20. Kanno H, Ozawa H, Sekiguchi A, Itoi E. Spinal cord injury induces upregulation of Beclin 1 and promotes autophagic cell death. Neurobiol Dis 2009; 33:143-148.
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21. Zhang HY, Wang ZG, Wu FZ, Kong XX, Yang J, Lin BB, et al. Regulation of autophagy and ubiquitinated protein accumulation by bFGF promotes functional recovery and neural protection in a rat model of spinal cord injury. Mol Neurobiol 2013; 48:452-464.
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22. Sarkar C, Zhao Z, Aungst S, Sabirzhanov B, Faden AI, Lipinski MM. Impaired autophagy flux is associated with neuronal cell death after traumatic brain injury. Autophagy 2014; 10:2208-2222.
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23. Liu S, Sarkar C, Dinizo M, Faden AI, Koh EY, Lipinski MM, et al. Disrupted autophagy after spinal cord injury is associated with ER stress and neuronal cell death. Cell Death Dis 2015; 6:e1582.
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27. Maiese K. Targeting molecules to medicine with mTOR, autophagy and neurodegenerative disorders. Br J Clin Pharmacol 2016; 82:1245-1266.
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28. Cunha-Santos J, Duarte-Neves J, Carmona V, Guarente L, Pereira de Almeida L, Cavadas C. Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway. Nat Commun 2016; 7:11445.
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29. Guo H, Chen Y, Liao L, Wu W. Resveratrol protects HUVECs from oxidized-LDL induced oxidative damage by autophagy upregulation via the AMPK/SIRT1 pathway. Cardiovasc Drugs Ther 2013; 27:189-198.
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30. Wang XH, Zhu L, Hong X, Wang YT, Wang F, Bao JP, et al. Resveratrol attenuated TNF-alpha-induced MMP-3 expression in human nucleus pulposus cells by activating autophagy via AMPK/SIRT1 signaling pathway. Exp Biol Med (Maywood) 2016; 241:848-853.
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31. Gammoh N, Lam D, Puente C, Ganley I, Marks PA, Jiang X. Role of autophagy in histone deacetylase inhibitor-induced apoptotic and nonapoptotic cell death. Proc Natl Acad Sci U S A 2012; 109:6561-6565.
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32. Aparicio IM, Espino J, Bejarano I, Gallardo-Soler A, Campo ML, Salido GM, et al. Autophagy-related proteins are functionally active in human spermatozoa and may be involved in the regulation of cell survival and motility. Sci Rep 2016; 6:33647.
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33. Wu HJ, Pu JL, Krafft PR, Zhang JM, Chen S. The molecular mechanisms between autophagy and apoptosis: potential role in central nervous system disorders. Cell Mol Neurobiol 2015; 35:85-99.
33
34. Jin X, Chen M, Yi L, Chang H, Zhang T, Wang L, et al. Delphinidin-3-glucoside protects human umbilical vein endothelial cells against oxidized low-density lipoprotein-induced injury by autophagy upregulation via the AMPK/SIRT1 signaling pathway. Mol Nutr Food Res 2014; 58:1941-1951.
34
ORIGINAL_ARTICLE
Evaluation of bax, bcl-2, p21 and p53 genes expression variations on cerebellum of BALB/c mice before and after birth under mobile phone radiation exposure
Objective(s): The increasing rate of over using cell phones has been considerable in youths and pregnant women. We examined the effect of mobile phones radiation on genes expression variation on cerebellum of BALB/c mice before and after of the birth. Materials and Methods: In this study, amobile phone jammer, which is an instrument to prevent receiving signals between cellular phonesand base transceiver stations (two frequencies 900 and 1800 MHz) for exposure was used and twelve pregnant mice (BALB/c) divided into two groups (n=6), first group irradiated in pregnancy period (19th day), the second group did not irradiate in pregnancy period. After childbirth, offspring wereclassified into four groups (n=4):Group1: control, Group 2: B1 (Irradiated after birth), Group 3: B2 (Irradiated in pregnancy period and after birth), Group 4: B3 (Irradiated in pregnancy period). When maturity was completed (8-10 weeks old), mice were dissected and cerebellum was isolated. The expression level of bax, bcl-2, p21 and p53 genes examined by real-time reverse transcription polymerase chain reaction (Real-Time RT- PCR). Results: The data showed that mobile phone radio waves were ineffective on the expression level of bcl-2 and p53 genes) P>0.05(. Also gene expression level of bax decreased and gene expression level of p21 increased comparing to the control group (P<0.05). Conclusion: From the obtained data it could be concluded that the mobile phone radiations did not induce apoptosis in cells of the cerebellum and the injured cells canbe repaired by cell cycle arrest.
https://ijbms.mums.ac.ir/article_9273_bc74d60d42db99a45d61a4081d29fd6a.pdf
2017-08-01
1037
1041
10.22038/ijbms.2017.9273
Apoptosis
Cerebellum
Gene expression
Mobile Phone
Mice
Najmeh
Ghatei
najmeh_ghatei@yahoo.com
1
Department of Medical Physics, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Ariane
Sadr Nabavi
2
Department of Genetics, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Mohammad Hossein
Bahreyni Toosi
bahreynimh@mums.ac.ir
3
Medical Physics Research Center, Mashhad University of Medical Sciences, Mashhad, Iran
LEAD_AUTHOR
Hosein
Azimian
azimianh911@mums.ac.ir
4
Medical Physics Research Center, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Mansour
Homayoun
mansour.homayoun@yahoo.com
5
Department of Anatomy and Cell Biology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
Reza
Ghasemnezhad Targhi
6
Department of Radiation Biology, School of Allied, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
Hossein
Haghir
haghirh@mums.ac.ir
7
Department of Anatomy and Cell Biology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran
AUTHOR
1. Al-Serori H, Kundi M, Ferk F, Mišík M, Nersesyan A, Murbach M, et al. Evaluation of the potential of mobile phone specific electromagnetic fields (UMTS) to produce micronuclei in human glioblastoma cell lines. Toxicol In Vitro 2017; 40:264-271.
1
2. Liu Y-x, Tai J-l, Li G-q, Zhang Z-w, Xue J-h, Liu H-s, et al. Exposure to 1950-MHz TD-SCDMA electromagnetic fields affect the apoptosis of astrocytes via caspase-3-dependent pathway. PLoS One 2012; 7:e42332.
2
3. Yang L, Hao D, Wang M, Zeng Y, Wu S, Zeng Y. Cellular neoplastic transformation induced by 916 MHz microwave radiation. Cell Mol Neurobiol. 2012;32:1039-1046.
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4. Kim K-H, Kabir E, Jahan SA. The use of cell phone and insight into its potential human health impacts. Environ Monit Assess 2016;188:221.
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5. Gil-Garcia A. Output Power-Control Loop Design for GSM Mobile Phones. Agilent Technologies Inc Semiconductor Products Group, Santa Clara, CA, USA. 2003:1-8.
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6. Schaumburg F, Guarnieri F. Assessment of thermal effects in a model of the human head implanted with a wireless active microvalve for the treatment of glaucoma creating a filtering bleb. Phys Med Biol. 2017;62:N191.
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8. Bourdineaud J-P, Šrut M, Štambuk A, Tkalec M, Brèthes D, Malarić K, et al. Electromagnetic fields at a mobile phone frequency (900 MHz) trigger the onset of general stress response along with DNA modifications in Eisenia fetida earthworms. Arch Ind Hyg Toxicol 2017; 68:142-152.
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17. Gross A. BCL-2 family proteins as regulators of mitochondria metabolism. Biochim Biophys Acta 2016; 1857:1243-1246.
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19. Siganak M, Koutsopoulos AV, Neofytou E, Vlachaki E, Psarrou M, Soulitzis N, Pentilas N, Schiza S, Siafakas NM, Tzortzaki EG. Deregulation of apoptosis mediators' p53and bcl2 in lung tissue of COPD patients. Respir Res 2010;11:46.
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21. Liu M-L, Wen J-Q, Fan Y-B. Potential protection of green tea polyphenols against 1800 MHz electromagnetic radiation-induced injury on rat cortical neurons. Neurotox Res 2011; 20:270-276.
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24. Tohidi F, Toosi M, Azimian H, Khademi S, Fardid R, Sarab GA. The gene expression level of p53 and p21 in mouse brain exposed to radiofrequency field. Int J Radiat Res 2015; 13: 337-343.
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42
ORIGINAL_ARTICLE
Mechanism underlying the effects of doxepin on β-amyloid -induced memory impairment in rats
Objective(s): In previous studies, researchers observed that doxepin could improve cognitive processes and has protective effectson the central nervous system. Thus, this study was designed to analyze the effects of doxepin on β-amyloid (Aβ)-induced memory impairment and neuronal toxicity in ratand to explore the underlying mechanism. Materials and Methods: Rats were treated with Aβ1-42 and doxepin was injected to validate its effects on cognitive function. The Morris water maze test was performed to detect memory function. Aβ1-42-treated SH-SY5Y human neuroblastoma cell line was also used to detect the effects of doxepin and to explore the underlying mechanism. Western blotting analysis was used to detect the protein expression levels of PSD-95, synapsin 1, p-AKT and p-mTOR in rats. Results: After treated with 1 mg/kg of doxepin, Aβ1-42-treated rats showed markedly lower escape latency and higher platform-finding strategy score. Low doses of doxepin significantly reversed the effects of Aβ1-42 on the protein expression levels of PSD-95, synapsin 1, p-AKT and p-mTOR in rats. In vitro experiment showed the consistent results. Besides, PI3K inhibitor (LY294002) treatment could markedly reversed the effects of doxepin on Aβ1-42-treated SH-SY5Y cells. Conclusion: Our results demonstrated that doxepin could protect against the Aβ1-42-induced memory impairment in rats. The protective effect of doxepin was associated with the enhancement of PSD-95 and synapsin 1 expression via PI3K/AKT/mTOR signaling pathway.
https://ijbms.mums.ac.ir/article_9274_43317eaf6485286797f95dd2a815644b.pdf
2017-08-01
1044
1049
10.22038/ijbms.2017.9274
Alzheimer’s disease
Doxepin
Memory injury
PI3-K/AKT/mTOR- signaling
β-amyloid1-42
Jimei
Bu
jimei_bu@sohu.com
1
Department of Neurology, Jinshan Hospital, Fudan University, JinShan District 201508, Shanghai, China
AUTHOR
Hengbing
Zu
hengbing_zu@163.com
2
Department of Neurology, Jinshan Hospital, Fudan University, JinShan District 201508, Shanghai, China
LEAD_AUTHOR
1. Tan L, Yu JT, Zhang W, Wu ZC, Zhang Q, Liu QY, et al. Association of GWAS-linked loci with late-onset Alzheimer's disease in a northern Han Chinese population. Alzheimers Dement 2012; 9:546-553.
1
2. Tan MS, Yu JT, Jiang T, Zhu XC, Wang HF, Zhang W, et al. NLRP3 polymorphisms are associated with late-onset Alzheimer's disease in Han Chinese. J Neuroimmunol 2013; 265:91-95.
2
3. Weintraub D, Rosenberg PB, Drye LT, Martin BK, Frangakis C, Mintzer JE, et al. Sertraline for the treatment of depression in Alzheimer disease: week-24 outcomes. J Geriatr Psychiatry Neurol 2011; 24:222-228.
3
4. Lyketsos CG, Lopez O, Jones B, Fitzpatrick AL, Breitner J, Dekosky S. Prevalence of neuropsychiatric symptoms in dementia and mild cognitive impairment: results from the cardiovascular health study. Jama J Am Med Assoc 2002; 288:1475-1483.
4
5. Nyth AL, Gottfries CG, Lyby K, Smedegaardandersen L, Gyldingsabroe J, Kristensen M, et al. A controlled multicenter clinical study of citalopram and placebo in elderly depressed patients with and without concomitant dementia. Acta Psychiatr Scand 1992; 86:138-145.
5
6. Mossello E, Boncinelli M, Caleri V, Cavallini MC, Palermo E, Di BM, et al. Is antidepressant treatment associated with reduced cognitive decline in Alzheimer's disease? Dement Geriatr Cogn Dis 2008; 25:372-379.
6
7. Vermeeren A, Coenen AM. Effects of the use of hypnotics on cognition. Prog Brain Res 2011; 190:189.
7
8. Drake LA, Fallon JD, Sober A. Relief of pruritus in patients with atopic dermatitis after treatment with topical doxepin cream. The Doxepin Study Group. J Am Acad Dermatol 1994; 31:613-616.
8
9. Hajak G, Rodenbeck A, Voderholzer U, Riemann D, Cohrs S, Hohagen F, et al. Doxepin in the treatment of primary insomnia: a placebo-controlled, double-blind, polysomnogra-phic study. J Clin Psychiatr 2001; 62:453-463.
9
10. Ray SK, Fidan M, Nowak MW, Wilford GG, Hogan EL, Banik NL. Oxidative stress and Ca2+ influx upregulate calpain and induce apoptosis in PC12 cells. Brain Res 2000; 852:326-334.
10
11. Bian-shengJI, HeJI, Guo-qingLIU. Doxepin protects cultured neurons against oxidative stress-induced injury. Acta Pharm Sin 2004; 25:297-300.
11
12. Gharzi M, Dolatabadi HR, Reisi P, Javanmard SH. Effects of different doses of doxepin on passive avoidance learning in rats.Adv Biomed Res 2013; 2:66.
12
13. Azadbakht AA, Radahmadi M, Sh HJ, Reisi P. The effects of doxepin on stress-induced learning, memory impairments, and TNF-α level in the rat hippocampus. Res Pharm Sci 2015; 10:460-465.
13
14.O' NC. PI3-kinase/Akt/mTOR signaling: impaired on/off switches in aging, cognitive decline and Alzheimer's disease. Exp Gerontol 2013; 48:647-653.
14
15. Mairetcoello G, Courchet J, Pieraut S, Courchet V, Maximov A, Polleux F. The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Aβ oligomers through Tau phosphorylation. Neuron 2013; 78:94.
15
16. Stein SC, Woods A, Jones NA, Davison MD, Carling D. The regulation of AMP-activated protein kinase by phosphorylation. Biochem J 2000; 345 Pt 3:437-443.
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17. Carling D, Thornton C, Woods A, Sanders MJ. AMP-activated protein kinase: new regulation, new roles? Biochem J 2012; 445:11-27.
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18. CM T, SA R, Z X, AC M, TJ C, ML S, et al. beta-Amyloid-induced neuronal apoptosis requires c-Jun N-terminal kinase activation. J Neurochem 2001; 77:157-164.
18
19. Lin J, Li W, Zhang XL. Effects of Gingko biloba leaf extract on the learning and memory and expression of glial fibrillary acidic protein in hippocampal astrocytes of type 2 diabetic rats. Chinese J Clin Rehabil 2006; 10:176-179.
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20. Jämsä A, Hasslund K, Cowburn RF, Bäckström A, Vasänge M. The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer’s disease-like tau phosphorylation. Biochem Biophys Res Commun 2004; 319:993-1000.
20
21. Leblanc AC, Kovacs DM, Chen HY, Villaré F, Tykocinski M, Autilio-Gambetti L, et al. Role of amyloid precursor protein (APP): study with antisense transfection of human neuroblastoma cells. J Neurosci Res 1992; 31:635-645.
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22. Schonrock N, Matamales M, Ittner LM, Götz J. MicroRNA networks surrounding APP and amyloid-β metabolism--implications for Alzheimer's disease. Exp Neurol 2012; 235:447.
22
23. Li S, Yan Y, Jiao Y, Gao Z, Xia Y, Kong L, et al. Neuroprotective effect of osthole on neuron synapses in an alzheimer’s disease cell model via upregulation of microRNA-9. J Mol Neurosci 2016; 1-11.
23
24. Krystal AD, Durrence HH, Scharf M, Jochelson P, Rogowski R, Ludington E, et al. Efficacy and safety of doxepin 1 mg and 3 mg in a 12-week sleep laboratory and outpatient trial of elderly subjects with chronic primary lnsomnia. Sleep 2010; 33:1553-1561.
24
25. Weber J, Siddiqui MA, Wagstaff AJ, Mccormack PL. Low-dose doxepin: in the treatment of insomnia. CNS Drugs 2010; 24:713-720.
25
26. Chong ZZ, Shang YC, Wang S, Maiese K. A Critical kinase cascade in neurological disorders: PI 3-K, Akt, and mTOR. Future Neurol 2012; 7:733.
26
27. Griffin RJ, Moloney A, Kelliher M, Johnston JA, Ravid R, Dockery P, et al. Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer's disease pathology. J Neurochem 2005; 93:105-117.
27
28.Xian YF, Lin ZX, Mao QQ, Chen JN, Su ZR, Lai XP, et al. Isorhynchophylline Protects PC12 Cells Against Beta-Amyloid-Induced Apoptosis via PI3K/Akt Signaling Pathway. Evid Based Complementary Altern Med 2013; 2013:163057.
28
ORIGINAL_ARTICLE
Presenting a rapid method for detection of Bacillus cereus, Listeria monocytogenes and Campylobacter jejuni in food samples
Objective(s): Listeria monocytogens, Bacillus cereus and Campylobacter jejuni are three toxin producing bacteria over the world, especially in Iran, and it is essential to find a certain, rapid procedure to identify these microorganisms. In this research, these bacteria were simultaneously detected by multiplex PCR technique in foods. Materials and Methods: The primary approval of bacterial strains was performed by biochemical tests. PCR primers were designed based on the nucleotide sequences of the NHEB/NHEC gene of B. cereus, the hly gene of L. monocytogenes and the C gene of C. jejuni. The specificity of Multiplex PCR method was determined using seven food poisoning bacteria including Salmonella typhi, Shigella dysentery, Yersinia pestis, Staphylococcus aureus, Clostridium perfringens, Clostridium botulinum and Vibrio cholerae. To confirm the reaction, DNA extraction was performed from 30 food samples (milk), and gene amplification was performed by PCR. The length of amplified fragments was 300 bp, 210 bp and 160 bpfor NHEB/NHEC, hly and C genes, respectively. Results: The detection limits of the PCR method were 5, 4 and 3 pg for L. monocytogenes, B. cereus and C. jejuni, respectively. Specifisity test showed that this reaction is spesific to these 3 bacteria. Conclusion: In this study, we introduced a new multiplex PCR method for simultsnus detection of L. monocytogens, B. cereus and C. jejuni. These results can be used for detection of other toxin producing bacteria in food.
https://ijbms.mums.ac.ir/article_9275_c2643e4160267a68ff0687fcc3a3645f.pdf
2017-08-01
1050
1055
10.22038/ijbms.2017.9275
Bacillus cereus
Campylobacter jejuni
Hly
Listeria monocytogenes
Multiplex PCR
NHEB/NHEC
Ali
Razei
1
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
Rahim
Sorouri
r_sorouri@bmsu.ac.ir
2
Department of Microbiology, Faculty of Medicine, Baqiyatallah University of Medical Sciences, Tehran, Iran
LEAD_AUTHOR
Seyed Latif
Mousavi
3
Department of Biology, Faculty of Basic Sciences, Shahed University, Tehran, Iran
AUTHOR
Shahram
Nazarian
kpnazari@ihu.ac.ir
4
Biology Research Centre, Faculty of Basic Science, Imam Hossein University, Tehran, Iran
AUTHOR
Jafar
Amani
amani.j@bmsu.ac.ir
5
Applied Microbiology Research Center, Baqiyatallah University of Medical Science, Tehran, Iran
AUTHOR
Hosien
Aghamollaei
6
Applied Biotechnology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
AUTHOR
1. Mead PS, Slutsker L, Dietz V, McCaig LF, Bresee JS, Shapiro C, et al. Food-related illness and death in the United States. Emerg Infect Dis 1999l; 5:607.
1
2. Tauxe RV. Emerging foodborne pathogens. Int J Food Microbiol 2002; 78:31-41.
2
3. Jasson V, Jacxsens L, Luning P, Rajkovic A, Uyttendaele M, et al. Alternative microbial methods: An overview and selection criteria. Food Microbiol 2010; 27:710-730.
3
4. Singh A, Poshtiban S, Evoy S. Recent advances in bacteriophage based biosensors for food-borne pathogen detection. Sensors 2013; 13: 1763-1786.
4
5. Calvo J, Zaragoza P, Osta R. Technical note: A quick and more sensitive method to identify pork in processed and unprocessed food by PCR amplification of a new specific DNA fragment. J Anim Sci 2001; 79:2108-2112.
5
6. Gilmore MS, Cruz-Rodz AL, Leimeister-Wächter M, Kreft J, Goebel W, et al. A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage. J Bacteriol 1989; 171:744-753.
6
7. Schoeni JL, Lee Wong AC. Bacillus cereus food poisoning and its toxins. J Food Protect 2005; 68:636-648.
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8. Dierick K, Van Coillie E, Swiecicka I, Meyfroidt G, Devlieger H, Meulemans A, et al. Fatal family outbreak of Bacillus cereus-associated food poisoning. J Clin Microbiol 2005; 43:4277-4279.
8
9. Te Giffel M, Beumer RR, Granum PE, Rombouts FM. Isolation and characterisation of Bacillus cereus from pasteurised milk in household refrigerators in the Netherlands. Int J Food Microbiol 1997; 34:307-318.
9
10. Valero M, Hernandez-Herrero L, Giner M. Survival, isolation and characterization of a psychrotrophic Bacillus cereus strain from a mayonnaise-based ready-to-eat vegetable salad. Food Microbiol 2007; 24:671-677.
10
11. Novak JS, Call J, Tomasula P, Luchansky JB. An assessment of pasteurization treatment of water, media, and milk with respect to Bacillus spores. J Food Protect 2005; 68:751-757.
11
12. Rahimi E, Abdos F, Momtaz H, Baghbadorani ZT, Jalali M. Bacillus cereus in infant foods: prevalence study and distribution of enterotoxigenic virulence factors in Isfahan Province, Iran. ScientificWorldJournal 2013; 2013:292571.
12
13. Trends E. Sources of zoonoses and zoonotic agents and food-borne outbreaks in the European Union in 2008 EFSA J 2010; 8:1496.
13
14. Tam CC, Higgins CD, Neal KR, Rodrigues LC, Millership SE, O'Brien SJ, et al. Chicken consumption and use of acid-suppressing medications as risk factors for Campylobacter enteritis England. Emerg Infect Dis 2009; 15: 1402.
14
15. Hassanzadeh P, Motamedifar M. Occurrence of Campylobacter jejuni in Shiraz, southwestIran. Med Princ Pract 2007; 16:59-62.
15
16. Khoshbakht R, Tabatabaei M, Hosseinzadeh S, Shekarforoush SS, Aski HS. Distribution of nine virulence-associated genes in Campylobacter jejuni and C. coli isolated from broiler feces in Shiraz, Southern Iran. Foodborne Pathog Dis 2013; 10:764-770.
16
17. Ghorbanalizadgan M, Bakhshi B, Kazemnejad Lili A, Najar-Peerayeh S, Nikmanesh B. A molecular survey of Campylobacter jejuni and Campylobacter coli virulence and diversity. Iran Biomed J 2014; 18:158.
17
18. Hamidian M, Sanaei M, Bolfion M, Dabiri H, Zali MR, Walther-Rasmussen J. Prevalence of putative virulence markers in Campylobacter jejuni and Campylobacter coli isolated from hospitalized children, raw chicken, and raw beef in Tehran, Iran. Can J Microbiol 2011; 57:143-148.
18
19. Hosseinzadeh S, Shekarforoush SS, Ansari-Lari M, EsalatPanah-Fard Jahromi M, Berizi E, Abdollahi M. Prevalence and risk factors for listeria monocytogenes in broiler flocks in Shiraz, southern Iran. Foodborne Pathog Dis 2012; 9:568-572.
19
20. Burke D, Dawson D, Stearns T. Methods in yeast genetics: a Cold Spring Harbor Laboratory course manual 2000: Cold Spring Harbor Laboratory Course Manual Press.
20
21. Choma C, Guinebretière MH, Carlin F, Schmitt P, Velge P, Granum PE, et al. Prevalence, characterization and growth of Bacillus cereus in commercial cooked chilled foods containing vegetables. J Appl Microbiol 2000; 88:617-625.
21
22. Kathariou S. Listeria monocytogenes virulence and pathogenicity, a food safety perspective. J Food Protect 2002; 65:1811-1829.
22
23. Chen HM, Lin CW. Hydrogel‐coated streptavidin piezoelectric biosensors and applications to selective detection of strep‐tag displaying cells. Biotechnol Progress 2007; 23:741-748.
23
24. Zhang MJ, Qiao B, Xu XB, Zhang JZ. Advances in rapid detection methods for foodborne pathogens. J Microbiol Biotechnol 2014; 24:297-312.
24
25. Khoo CH, Cheah YK, Lee LH, Sim JH, Salleh NA, Sidik SM, et al. Virulotyping of Salmonella enterica subsp. enterica isolated from indigenous vegetables and poultry meat in Malaysia using multiplex-PCR. Antonie van Leeuwenhoek 2009; 96:441-457.
25
26. Cheah YK, Salleh NA, Lee L-H, Radu S, Sukardi S, Sim JH. Comparison of PCR fingerprinting techniques for the discrimination of Salmonella enterica subsp. enterica serovar Weltevreden isolated from indigenous vegetables in Malaysia. World J Microbiol Biotechnol 2008; 24:327-335.
26
27. Gilbert C, Winters D, O'Leary A, Slavik M. Development of a triplex PCR assay for the specific detection of Campylobacter jejuni, Salmonella spp., and Escherichia coli O157: H7. Mol Cell Probes 2003; 17:135-138.
27
28.Germini A, Masola A, Carnevali P, Marchelli R. Simultaneous detection of Escherichia coli O175: H7, Salmonella spp., and Listeria monocytogenes by multiplex PCR. Food Control 2009; 20:733-738.
28
29. Kumar TK, Murali H, Batra H. Simultaneous detection of pathogenic B. cereus, S. aureus and L. monocytogenes by multiplex PCR. Indian J Microbiol 2009; 49:283-289.
29
30. Wiwat C, Thiramanas R. Detection of Hemolysin BL Gene of Bacillus cereus Isolates. Mahidol Univ J Pharm Sci 2014; 41:22-30.
30
31. Forghani F, Singh P, Seo KH, Oh DH. A novel pentaplex real time (RT)-PCR high resolution melt curve assay for simultaneous detection of emetic and enterotoxin producing Bacillus cereus in food. Food Control 2016; 60:560-568.
31
32. Zhang MJ, Qiao B, Xu XB, Zhang JZ. Development and application of a real-time polymerase chain reaction method for Campylobacter jejuni detection. World J Gastroenterol 2013; 19:3090.
32
33. Gouws PA, Liedemann L. Evaluation of diagnostic PCR for the detection of Listeria monocytogenes in food products. Food Technol Biotechnol 2005; 43:201-205.
33
ORIGINAL_ARTICLE
Calycosin attenuates dextran sulfate sodium (DSS)-induced experimental colitis
Objective(s):Inflammatory bowel disease (IBD) results from dysregulation of intestinal mucosal immunity. It is an incurable disease that affects millions of people worldwide. Developing new strategies for the treatment of colitis has been a major challenge. Here, we report the effect of calycosin, a plant-derived flavonoid, in successfully managing colitis in murine model. Material and Methods:In vivo model of colitis was induced using 2.5% (w/v) dextran sodium sulfate (DSS, 36,000 to 50,000 Mw). Body weight and disease activity index (DAI) were evaluated every day. Hematoxylin-Eosin (H&E) staining was used to estimate the effect of calycosin on DSS-induced colon damage. The levels of proinflammatory genes and mRNA expression were determined using real-time PCR, whereas the proinflammatory cytokines were assessed with ELISA. The content of other parameters including myeloperoxidase (MPO), glutathione (GSH), superoxide dismutase (SOD) and malondialdehyde (MDA) were also evaluated. Western blot assay was further used to determine the effect of calycosin on both NF-κB and mitogen activated protein kinases (MAPK) pathways. Results: The results showed that calycosin prevented weight loss and shortening of the colon length, maintained an intact mucosa, increased GSH and SOD activities, and decreased MDA levels. The drug also significantly inhibited proinflammatory cytokine mRNA expression and decreased MPO activity. Additionally, it remarkably inhibited NF-κB pathway and c-Jun N-terminal kinase (JNK) phosphorylation with no effect on p38 and extracellular signal-regulated kinase (ERK1/2) phosphorylation levels in colon tissue. Conclusion: These findings revealed that calycosin successfully ameliorated the effect of DSS-induced colitis in mice, which could be associated with NF-κB and JNK pathway modulations.
https://ijbms.mums.ac.ir/article_9276_8caa298e9ba9d68fe2c98611219d4875.pdf
2017-08-01
1056
1062
10.22038/ijbms.2017.9276
Colitis
Calycosin
Free radical
Inflammatory cell
NF-κB
Signaling pathway
Liu
Chao
liuchao@126.com
1
Department of Gastroenterology, the Affiliated Second Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
Pengyuan
Zheng
zhengpengyuandr@126.com
2
Department of Gastroenterology, the Affiliated Fifth Hospital of Zhengzhou University, Zhengzhou, 450014, China
LEAD_AUTHOR
Liu
Xia
3
Department of Gastroenterology, the Affiliated Second Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
Yu
Yong
yuyong@126.com
4
Department of Gastroenterology, the Affiliated Fifth Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
Gaofeng
Lu
5
Department of Gastroenterology, the Affiliated Second Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
Fuai
Tang
6
Department of Gastroenterology, the Affiliated Second Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
Zhiguo
Zhao
7
Department of Gastroenterology, the Affiliated Second Hospital of Zhengzhou University, Zhengzhou, 450014, China
AUTHOR
1. Manichanh C, Borruel N, Casellas F, Guarner F. The gut microbiota in IBD. Nat Rev Gastroenterol Hepatol 2012; 9:599-608.
1
2. Erben U, Loddenkennper C, Spieckermann S, Heimesaat MM, Siegmund B, Kuehl AA. Histomorphology of intestinal inflammation in inflammatory bowel diseases (IBD) mouse models and its relevance for IBD in men. Int J Clin Exp Med 2016; 9:408-442.
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3. Podolsky, Daniel K. Inflammatory bowel disease. N Engl J Med 1991; 325:928-937.
3
4. Kumar S, Pandey AK. Chemistry and biological activities of flavonoids: an overview. ScientificWorldJournal 2013; 2013:162750.
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5. Yuting C, Rongliang Z, Zhongjian J, Yong J. Flavonoids as superoxide scavengers and antioxidants. Free Radic Biol Med 1990; 9:19-21.
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6. Ravishankar D, Rajora AK, Greco F, Osborn HM. Flavonoids as prospective compounds for anti-cancer therapy. Int J Biochem Cell B 2013; 45:2821-2831.
6
7. Fu Y, Chen J, Li Y J, Zheng Y F, Li P. Antioxidant and anti-inflammatory activities of six flavonoids separated from licorice. Food Chem 2013; 141:1063-1071.
7
8. Quan G H, Wang H, Cao J, Zhang Y, Wu D, Peng Q, et al. Calycosin suppresses RANKL-mediated osteoclastogenesis through inhibition of MAPKs and NF-κB. Int J Mol Sci 2015; 16:29496-507.
8
9. Zhao X, Li X, Ren Q, Tian J, Chen J. Calycosin induces apoptosis in colorectal cancer cells, through modulating the ERβ/MiR-95 and IGF-1R, PI3K/Akt signaling pathways. Gene 2016; 591:123-128.
9
10. Guo C, Tong L, Xi M, Yang H, Dong H, Wen A. Neuroprotective effect of calycosin on cerebral ischemia and reperfusion injury in rats. J Ethnopharmacol 2012; 144:768-774.
10
11. Nie XH, Ou-yang J, Xing Y, Li DY, Liu RE, Xu RX. Calycosin inhibits migration and invasion through modulation of transforming growth factor beta-mediated mesenchymal properties in U87 and U251 cells. Drug Des Devel Ther 2016; 10:767.
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ORIGINAL_ARTICLE
Hydroethanolic extract of Carthamus tinctorius induces antidepressant-like effects: modulation by dopaminergic and serotonergic systems in tail suspension test in mice
Objective(s): Studies indicate that major deficiency in the levels of monoaminergic transmitters is a reason for severe depression. On the other hand, it is shown that Carthamus tinctorius L. (CT) may improve neuropsychological injuries by regulation of the monoamine transporter action. Hence, the present study was undertaken to evaluate the involvement of monoaminergic systems in antidepressant-like effect of CT extract in the tail suspension test (TST) in mice. Materials and Methods: The mice were intraperitoneally (IP) treated with CT extract (100–400 mg/kg) 1hr before the TST. To investigate the involvement of monoaminergic systems in antidepressant-like effect, the mice were treated with receptor antagonists 15 min before CT extract treatment (400 mg/kg, IP) and 1hr before the TST. Results: Findings showed that CT extract (100–400 mg/kg, IP), dose-dependently induced antidepressant-like effect (P<0.001), but it was not accompanied by alterations in spontaneous locomotor activity in the open-field test. Pretreatment of mice with SCH23390, sulpiride, haloperidol, WAY100135, cyproheptadine, ketanserin and p-chlorophenylalanine (PCPA) inhibited the antidepressant-like effect of CT extract (400 mg/kg, IP), but not with prazosin and yohimbine. Co-administration of CT extract (100 mg/kg, IP) with sub-effective doses of fluoxetine (5 mg/kg, IP) or imipramine (5 mg/kg, IP) increased their antidepressant-like response. Conclusion: Our findings firstly showed that components (especially N-Hexadecanoic acid) of CT extract induce antidepressant-like effects by interaction with dopaminergic (D1 and D2) and serotonergic (5HT1A, 5-HT2A receptors) systems. These findings validate the folk use of CT extract for the management of depression.
https://ijbms.mums.ac.ir/article_9277_f3abb810566ef3d3fc114e43cec7b832.pdf
2017-08-01
1063
1073
10.22038/ijbms.2017.9277
Antidepressant-like effect
Carthamus tinctorius L
Mice
Monoaminergic system
Tail suspension test
Saeid
Abbasi-Maleki
s.abbasi@iaurmia.ac.ir
1
Department of Pharmacology & Toxicology, Faculty of Veterinary Medicine, Urmia Branch, Islamic Azad University, Urmia, Iran
LEAD_AUTHOR
Zahra
Mousavi
mosavisz50@gmail.com
2
Department of Pharmacology & Toxicology, Faculty of Pharmacy, Pharmaceutical Science Branch, Islamic Azad University, Tehran, Iran
AUTHOR
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