Document Type : Original Article
Authors
1 Assistant Professor, Department of Sport Sciences, Faculty of Educational Sciences and Psychology, Shiraz University, Shiraz, Iran
2 PhD Student of Biochemistry for Sport and Exercise Metabolism, Department of Sport Sciences, Faculty of Educational Sciences and Psychology, Shiraz University, Shiraz, Iran
Abstract
Background and Aim: To date, more than 100 types of kinases have been known that one of the most famous of them is the large family of mitochondria -cased kinases (MAPK), which regulated by the out-cell message (ERK). The ERK controls many important cellular functions, but the effect of resistance training on ERK protein has not been clearly revealed. The aim of this study was to investigate the effect of resistance training on the expression of total and phosphorylated ERK proteins in the flexor hallucis longus muscle (FHL) in healthy male rats. Materials and Methods: For this purpose, 12 male Sprague Dawley rats were randomly divided into groups as experimental (n=6) and control (n=6). The experimental groups exerted resistance training including climbing on a ladder during the 8 weeks, 5 sessions per week with a weight hanging on to the tail carried out increased load has been done weekly based on body weight of mice so that the first week was from 30% to 200% in 8 weeks. Fourty eight hours after the last training session, FHL muscle was extracted and the expression of the relevant protein was measured by ELISA. For statistical analysis, one-way ANOVA method was used with a significance level of 0.05. Results: The results showed that resistance exercise significantly increased the total protein content (p=0.01) but had no significantly increased its phosphorylated form (p=0.08). Conclusion: Probably, long-term resistance training is not an appropriate intervention to ERK activation. In order to investigate this exercise induced changes, perhaps it is better to examine other signalling pathways.
Keywords
kinases, Erk and p38, phosphorylate and regulate Foxo1. Cellular Signalling, 19(3), 519-527.
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., … & Yancopoulos, G. D.
(1991). ERKs: a family of protein-serine / threonine kinases that are activated and tyrosine phosphorylated in response
to insulin and NGF. Cell, 65(4), 663-675.
Casar, B., Pinto, A., & Crespo, P. (2009). ERK dimers and scaffold proteins: unexpected partners for a forgotten
(cytoplasmic) task. Cell Cycle, 8(7), 1007-1013.
Cheng, P., Alberts, I., & Li, X. (2013). The role of ERK1 / 2 in the regulation of proliferation and differentiation of
astrocytes in developing brain. International Journal of Developmental Neuroscience, 31(8), 783-789.
Cheung, K., Hume, P. A., & Maxwell, L. (2003). Delayed onset muscle soreness. Sports Medicine, 33(2), 145-164.
Coogan, A. N., & Piggins, H. D. (2003). Circadian and photic regulation of phosphorylation of ERK1 / 2 and Elk-1 in the
suprachiasmatic nuclei of the Syrian hamster. Journal of Neuroscience, 23(7), 3085-3093.
Creer, A., Gallagher, P., Slivka, D., Jemiolo, B., Fink, W., & Trappe, S. (2005). Influence of muscle glycogen availability
on ERK1 / 2 and Akt signaling after resistance exercise in human skeletal muscle. Journal of Applied Physiology, 99(3),
950-956.
Deane, C. S., Atherton, P. J., Szewczyk, N. J., Etheridge, T. E., & Phillips, B. E. (2015). The impact of eccentric and concentric exercise on muscle function in young and older men. In Proceeding of the Physiological Society 34, PC210. UK, Cardiff, May 20-23, 2015.
Jiang, W., Zhu, J., Zhuang, X., Zhang, X., Luo, T., Esser, K. A., & Ren, H. (2015). Lipin1 regulates skeletal muscle
differentiation through extracellular signal-regulated kinase (ERK) ativation and cyclin D complex-regulated cell cycle
withdrawal. Journal of Biological Chemistry, 290(39), 23646-23655.
Karlsson, H. K., Nilsson, P. A., Nilsson, J., Chibalin, A. V., Zierath, J. R., & Blomstrand, E. ( 2004).
Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise.
American Journal of Physiology-Endocrinology and Metabolism, 287(1), 1-7.
Kim, Y. B., Inoue, T., Nakajima, R., Nakae, K., Tamura, T., Tokuyama, K., & Suzuki, M. (1995). Effects of endurance
training of gene expression on insulin signal transduction pathway. Biochemical and Biophysical Research Communications, 210(3), 766-773.
Ma, Q. L., Harris-White, M. E., Ubeda, O. J., Simmons, M., Beech, W., Lim, G. P., … & Cole, G. M. (2007). Evidence of Aβ
and transgene-dependent defects in ERK-CREB signaling in Alzheimer’s models. Journal of Neurochemistry, 103(4),
1594-1607.
MacIntosh, B. R., Esau, S. P., Holash, R. J., & Fletcher, J. R. (2011). Procedures for rat in situ skeletal muscle contractile
properties. Journal of Visualized Experiments: JoVE, (56), 3167.
Martineau, L. C., & Gardiner, P. F. (2001). Insight into skeletal muscle mechanotransduction: MAPK activation is quantitatively related to tension. Journal of Applied Physiology, 91(2), 693-702.
Melo-Lima, S., Lopes, M. C., & Mollinedo, F. (2015). ERK1 / 2 acts as a switch between necrotic and apoptotic cell death
in ether phospholipid edelfosine-treated glioblastoma cells. Pharmacological Research, 95, 2-11.
Miyake, M., Goodison, S., Lawton, A., Gomes-Giacoia, E., & Rosser, C. J. (2015). Angiogenin promotes tumoral growth
and angiogenesis by regulating matrix metallopeptidase-2 expression via the ERK1 / 2 pathway. Oncogene, 34(7), 890-
901.
Murgia, M., Serrano, A. L., Calabria, E., Pallafacchina, G., Lømo, T., & Schiaffino, S. (2000). Ras is involved in
nerve-activity-dependent regulation of muscle genes. Nature Cell Biology, 2(3), 142-147.
Nader, G. A., & Esser, K. A. (2001). Intracellular signaling specificity in skeletal muscle in response to different modes
of exercise. Journal of Applied Physiology, 90(5), 1936-1942.
Nelson, D. L., Lehninger, A. L., & Cox, M. M. (2012). Lehninger principles of biochemistry. 2th Edition. Macmillan Learning.
Nemati, J., Norshahi, M., Rajabi, H., & Ghrakhanlo, R. (2010). The effects of eight weeks of resistance training on fast
and slow twitch muscle protein content integrin in Wistar rat. Olympics, 1(61), 35–45. [Persian]
Ouwens, D. M., de Ruiter, N. D., van der Zon, G. C., Carter, A. P., Schouten, J., van der Burgt, C., … & van Dam, H.
(2002). Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras–MEK–
ERK pathway and of Thr69 through RalGDS–Src–p38. The EMBO Journal, 21(14), 3782-3793.
Sherwood, D. J., Dufresne, S. D., Markuns, J. F., Cheatham, B., Moller, D. E., Aronson, D., & Goodyear, L. J. (1999).
Differential regulation of MAP kinase, p70S6K, and Akt by contraction and insulin in rat skeletal muscle. American Journal of Physiology-Endocrinology and Metabolism, 276(5), E870-E878.
Steelman, L. S., Chappell, W. H., Abrams, S. L., Kempf, C. R., Long, J., Laidler, P., … & Donia, M. (2011). Roles of the
Raf / MEK / ERK and PI3K / PTEN / Akt / mTOR path ways in controlling growth and sensitivity to therapy-implications for
cancer and aging. Aging (Albany NY), 3(3), 192.
Sung, J. H., Kim, M. O., & Koh, P. O. (2012). Nicotinamide prevents the down-regulation of MEK / ERK / p90RSK signaling
cascade in brain ischemic injury. Journal of Veterinary Medical Science, 74(1), 35-41.
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 physiologica Scandinavica, 178(1), 61-72.
Tidball, J. G. (2005). Inflammatory processes in muscle injury and repair. American Journal of Physiology-Regulatory,
Integrative and Comparative Physiology, 288(2), R345-R353.
Widegren, U., Jiang, X. J., Krook, A., Chibalin, A. V., Björnholm, M., Tally, M., … & Zierath, J. R. (1998). Divergent effects of
exercise on metabolic and mitogenic signaling pathways in human skeletal muscle. The FASEB Journal, 12(13),
1379-1389.
Widegren, U., Wretman, C., Lionikas, A., Hedin, G., & Henriksson, J. (2000). Influence of exercise intensity on
ERK / MAP kinase signalling in human skeletal muscle. Pflugers Archiv European Journal of Physiology, 441(2-3), 317-322.
Williamson, D., Gallagher, P., Harber, M., Hollon, C., & Trappe, S. (2003). Mitogen-activated protein kinase (MAPK)
pathway activation: effects of age and acute exercise on human skeletal muscle. The Journal of Physiology, 547
(3), 977-987.
Wortzel, I., Hanoch, T., Porat, Z., Hausser, A., & Seger, R. (2015). Mitotic Golgi translocation of ERK1c is mediated by a
PI4KIIIβ–14-3-3γ shuttling complex. Journal Cell Science, 128(22), 4083-4095.
Wretman, C., Lionikas, A., Widegren, U., Lännergren, J., Westerblad, H., & Henriksson, J. (2001). Effects of concentric
and eccentric contractions on phosphorylation of MAPKerk1 / 2 and MAPKp38 in isolated rat skeletal muscle.
The Journal of physiology, 535(1), 155-164.
Yu, M., Stepto, N. K., Chibalin, A. V., Fryer, L. G., Carling, D., Krook, A., … & Zierath, J. R. (2003). Metabolic and mitogenic
signal transduction in human skeletal muscle after intense cycling exercise. The Journal of Physiology, 546(2), 327-335.
Zhu, J. H., Gusdon, A. M., Cimen, H., Van Houten, B., Koc, E., & Chu, C. T. (2012). Impaired mitochondrial biogenesis
contributes to depletion of functional mitochondria in chronic MPP+ toxicity: dual roles for ERK1 / 2. Cell Death &
Disease, 3(5), e312.
)