نوع مقاله : مقاله پژوهشی
نویسندگان
1 کارشناسی ارشد فیزیولوژی ورزشی دانشگاه مازندران
2 دانشیار گروه فیزیولوژی ورزشی/دانشکده تربیت بدنی و علوم ورزشی/ دانشگاه مازندران
3 دانشجوی دکتری فیزیولوژی ورزشی/ دانشکده تربیت بدنی علوم ورزشی/ دانشگاه بیرجند
چکیده
زمینه و هدف: هدف از اجرای این پژوهش بررسی اثر هشت هفته تمرین استقامتی با مدت های مختلف بر سطوح پروتئین شوک گرمایی 27 پلاسما در موش های صحرایی نر نژاد ویستار بود. روش تحقیق: برای این منظور 40 سر موش نر هشت هفته ای با میانگین وزن 10 ± 189 گرم از انستیتو پاستور شمال ایران تهیه و به طور تصادفی در گروه کنترل و سه گروه تمرینی تقسیم شدند. گروه های تمرینی به مدت هشت هفته، هر هفته پنج روز، با شدت 20 متر بر دقیقه )معادل 50 تا 55 درصد حداکثر اکسیژن مصرفی( با مدت های 30 ، 60 و 90 دقیقه و شیب صفر درجه روی نوار گردان ویژه جوندگان، به تمرین پرداختند. برای اندازه گیری سطوح پروتئین شوک گرمایی 27 پلاسما پس از هشت هفته تمرین و 72 ساعت پس از آخرین جلسه تمرین، موش ها بی هوش شدند. سطح پروتئین شوک گرمایی 27 پلاسما با استفاده از کیت EIA و به روش آنزیم لینک ایمنواسی ( ELISA ) اندازه گیری شد. داده ها به روش آنالیز واریانس یک طرفه و آزمون تعقیبی LSD تجزیه و تحلیل گردیدند. مقدار p<0/05 به عنوان حداقل سطح معنی داری تفاوت میانگین ها مورد استفاده قرار گرفت. یافته ها: نتایج نشان داد که سطوح پروتئین شوک گرمایی27 پلاسما در گروه تمرینی 60 دقیقه، به طور معناداری (P<0/05) بالاتر از سایر گروه ها است. نتیجه گیری: نتایج این تحقیق نشان می دهد که تمرینات استقامتی با شدت و مدت متوسط (60دقیقه) در مقایسه با مدت کوتاه تر و بلندتر، باعث افزایش بیشتری در سطوح پروتئین شوک گرمایی 27 پلاسما می شود.
کلیدواژهها
عنوان مقاله [English]
The effect of eight weeks endurance training at different durations on plasma heat shock protein 27 (HSP27) level in male rats
نویسندگان [English]
- Saeed Mirzaei 1
- Ziya Fallah Mohammadi 2
- Ali Yaghoubi 3
1
2
3
چکیده [English]
Background and Aim: The aim of this study was to investigate the effect of eight weeks endurance training at different durations on plasma heat shock protein 27 in male rats. Materials and Methods: Forty adult Wistar male rats (eight weeks old, 189 ± 10g weight) were used for this study. Animals were divided into 4 groups including control, 30 min/session training, 60 min/session, and 90 min/session training groups. The training was included of treadmill exercise at 20 m/min (0% grade) in five days/week for eight weeks. Subjects were sacrificed 72 h after the last session of exercise for measurement of heat shock protein 27 levels in the plasma. Heat shock protein 27 content in the plasma was determined with EIA kit and ELISA system data were analyzed using one-way ANOVA and LSD at P≤0/05. Results: Findings showed that plasma concentrations of heat shock protein 27 were significantly (P < 0.05) higher in 60 min/session training group. Conclusion: This study show that chronic mild-duration exercise could yield to greater levels in heat shock protein 27 plasma concentrations compared to the less or more durations.
کلیدواژهها [English]
- Heat Shock Protein 27
- Duration of Training
- Wistar Rats
2-Bruey, J.M., Ducasse C., Bonniaud P., Ravagnan L., et al., 2000. HSP27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol, vol. 2, no. 9, pp. 645-652.
3-Byrd, S.K., 1992. Alterations in the sarcoplasmic reticulum: a possible link to exercise-induced muscle damage. Med Sci Sports Exerc, vol. 24, no. 5, pp. 531-536.
4-Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., Fuqua S.A., 1993. Biological and clinical implications of heat shock protein 27 (HSP27): a review. J Natl Cancer Inst, vol. 6, no. 85, pp. 1558-1570.
5-Febbraio M.A., Steensberg A., Walsh R., Koukoulas I., et al., 2002. Reduced glycogen availability is associated with an elevation in Hsp72 in contracting human skeletal muscle. J Physiol, vol. 1, no. 538, pp. 911-917.
6-Fehrenbach E., Niess A.M., Schlotz E., Passek F., et al., 2000. Transcriptional and translational regulation of heat shock proteins in leukocytes of endurance runner. J Appl Physiol, vol. 89, no. 2,pp. 704-710.
7-Friden J., Sjostrom M., Ekblom B., 1983. Myofibrillar damage following intense eccentric exercise in man. Int J Sports Med, vol. 4, no. 3, pp. 170-176.
8-Gandevia S.C., 2001. Spinal and supraspinal factors in human muscle fatigue. Physiol Rev, vol. 81, no. 4, pp.1725-1789.
9-Gorman A.M., 2008. Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling. J Cell Mol Med, vol. 12, no. 6. pp.2263–2280.
10-Hu S., Ying Z., Gomez-Pinilla F., Frautschy, S.A., 2009. Exercise can increase small heat shock proteins (sHSP) and pre- and post-synaptic proteins in the hippocampus. Brain res, 1249, pp. 191–201.
11-Jakob U., Gaestel M., Engel K., Buchner J., 1993. Small heat shock proteins are molecular chaperones. J Biol Chem, vol. 25, no. 268, pp.1517–1520.
12-Jammes Y., Steinberg J.G., Delliaux S., Brégeon F., 2009. Chronic fatigue syndrome combines increased exercise-induced oxidative stress and reduced cytokine and Hsp responses. J Intern Med, vol. 266, no. 2, pp. 196-206.
13-Kalmar B., Burnstock G., Vrbova G., Greensmith L., 2002. The effect of neonatal nerve injury on the expression of heat shock proteins in developing rat Motoneurones. J Neurotraum, vol. 19, no. 5, pp. 667–679.
14-Ooyama K., Wu J., Nosaka N., Aoyama T., Kasai M., 2008. Combined intervention of mediumchain triacylglycerol diet and exercise reduces body fat mass and enhances energy expenditure in rats. J Nutr Sci Vitaminol, vol, 54, no. 2, pp. 136-41.
15-Lavoie J.N., Gingras-Breton G., Tanguay R.M., Landry J., 1993. Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J Biol Chem, vol. 15, no. 268, pp. 3420-3429.
16-Lee T.H., Jang M.H., Shin M.C., Lim B.V., et al., 2003. Dependence of rat hippocampal c-Fos expression on intensity and duration of exercise. Life Sci, vol. 7, no. 12, pp. 1421-1436.
17-Liu Y., Mayr S., Opitz-Gress A., Zeller C., et al., 1999. Human skeletal muscle HSP70 response to training in highly trained rowers. J Appl Physio, vol. 86, no. 1, pp. 101-104.
18-Locke M., Noble E.G., Atkinson B.G., 1990. Exercising mammals synthesize stress proteins. Am J Physio, vol. 258, no. 4, pp. 723-729.
19-Morton J.P., MacLaren D.P., Cable N.T., Bongers T., et al., 2006. Time-course and differential expression of the major heat shock protein families in human skeletal muscle following acute nondamaging treadmill exercise. J Appl Physio, vol. 101, no. 1, pp. 176-182.
20-Patil S.B., Pawar M.D., Bitar K.N., 2004. Phosphorylated HSP27 essential for acetylcholine-induced association of RhoA with PKC alpha. Am J Physiol Gastrointest Liver Physio, vol. 286, no. 4, pp. 635-644.
21-Paulsen G., Hanssen K.E., Rønnestad B.R., Kvamme N.H., et al., 2012. Strength training elevates HSP27, HSP70 and B-crystallin levels in musculi vastus lateralis and trapezius. Eur J Appl Physio, vol. 112, no. 5, pp. 1773-1782.
22-Puntschart A., Vogt M., Widmer H.R., Hoppeler H., Billeter R., 1996. HSP70 expression in human skeletal muscle after exercise. Acta Physiol Scan, vol. 157, no. 4, pp. 411-417.
23-Rinaldi B., Corbi G., Boccuti S., Filippelli W., et al., 2006. Exercise training affects age-induced changes in SOD and heat shock protein expression in rat heart. Exp Gerontol, vol. 41, no. 8, pp. 764–770.
24-Salo D.C., Donovan C.M., Davies K.J., 1991. HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise. Free Radic Biol Med, vol. 11, no. 3, pp. 239-246.
25-Sanders B.M., 1993. Stress proteins in aquatic organisms: an environmental perspective. Crit Rev Toxicol, vol. 23, no. 1, pp. 49-75.
26-Thompson H.S., Maynard E.B., Morales E.R., Scordilis S.P., 2003. Exercise-induced HSP27, HSP70 and MAPK responses in human skeletal muscle. Acta Physiol Scan, vol. 178, no. 1, pp. 61–72.
27-Thompson H.S., Scordilis S.P., Clarkson P.M., Lohrer W.A., 2001. A single bout of eccentric exercise increases HSP27 and HSC/ HSP70 in human skeletal muscle. Acta Physiol Scan, vol. 171, no. 2, pp. 187-193.
28-Vos M.J., Hageman J., Carra S., Kampinga H.H., 2008. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry, vol. 8, no.47. pp. 7001–7011.
29-Welch W.J., 1992. Mammalian stress response: cell physiology, structure / function of stress proteins, and implications for medicine and disease. Physiol Rev, vol. 72, no. 4, pp. 1063-1081.
30-Williams K.L., Rahimtula M., Mearow K.M., 2005. HSP27 and axonal growth in adult sensory neurons in vitro. BMC Neurosci [online] ,vol. 8, no. 6, (8 April 2005). Available from:http//www.biomedcenteral.com/1471-2202/6/24.