ABSTRACT The distribution of myosin heavy (MyHC) and myosin light chain (MyLC) isoform pattern in horse, rat and human skeletal muscle was investigated to establish relations between them and the role of myosin isoform patterns in mammalian muscle with different twitch characteristics was studied. These two isoforms were separated in a SDS-PAGE gel system, stained using the coomassie and silver staining procedures, and the results were analyzed using a G:BOX system. The relative content of MyHC I isoform in muscle was 2.6 times higher than in human compared to horse muscle (p < 0.001), and 6.3 times higher than in rat muscle (p < 0.001). The relative content of MyHC IIx/d isoform in horse muscle is 2.7 times, and in rat muscle 2.2 times higher in comparison with human muscle (p < 0.001). The role of the MyLC isoform distribution in mammalian skeletal muscle seems to depend on the oxidative capacity of muscles.
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Kaasik, P. , Leisson, K. , Puhke, R. , Alev, K. and Seene, T. (2012) Characteristics of myosin isoforms in mammalian skeletal muscle. Advances in Biological Chemistry, 2, 77-83. doi: 10.4236/abc.2012.22010.
  Barany, M. (1967) ATPase activity of myosin correlated with speed of muscle shortening. The Journal of General Physiology, 50, 197-216. doi:10.1085/jgp.50.6.197
 Moss, R.L., Diffee, G.M. and Greaser, M.L. (1995) Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms. Reviews of Physiology, Biochemistry and Pharmacology, 126, 1-63.
 Schiaffino, S. and Reggiani, C. (1996) Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiological Reviews, 76, 371-423.
 Diffee, G.M., Haddad, F., Herrick, R.E. and Baldwin, K.M. (1991) Control of myosin heavy chain expression interaction of hypothyroidism and hindlimb suspension. American Journal of Physiology Cell Physiology, 261, C1099-C1106.
 Greaser, M.L., Moss, R.L. and Reiser, P.J. (1988) Variations in contractile properties of rabbit single muscle fibres in relation to troponin T isoforms and myosin light chains. The Journal of Physiology, 406, 85-98.
 Bottinelli, R., Betto, R., Schiaffino, S. and Reggiani, C. (1994) Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres. The Journal of Physiology, 478, 431-449.
 Lowey, S., Waller, G.S. and Trybus, K.M. (1993) Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. The Journal of Biological Chemistry, 268, 20414-20418.
 Lowey, S., Waller, G.S. and Trybus, K.M. (1993) Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature, 365, 454-456.
 Sweeney, H.L., Kushmerick, M.J., Mabuchi, K., Sréter, F.A. and Gergely, J. (1988) Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated muscle fibers. The Journal of Biological Chemistry, 263, 9034-9039.
 Bicer, S. and Reiser, P.J. (2004) Myosin light chain isoform expression among single mammalian skeletal muscle fibers: Species variations. Journal of Muscle Research and Cell Motility, 25, 623-633. doi:10.1007/s10974-004-5070-9
 Bicer, S. and Reiser, P.J. (2007) Variations in apparent mass of mammalian fast-type myosin light chains correlate with species body size, from shrew to elephant. American Journal of Physiology Regulatory, Integrative and Comparative Physiology, 292, R527-R534.
 Alev, K., Kaasik, P., Pehme, A., Aru, M., Parring, A.-M., Elart, A. and Seene, T. (2009) Physiological role of myosin light and heavy chain isoforms in fast- and slow-twitch muscles: Effect of exercise. Biology of Sport, 26, 215- 234.
 Hayashibara, T. and Miyanishi, T. (1994) Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin integration. Biochemistry, 33, 12821-1282.
 Stevens, L., Firinga, C., Gohlsch, B., Bastide, B., Mounier, Y. and Pette, D. (2000) Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscle of rat. American Journal Physiology Cell Physiology, 279, C1558-C1563.
 Wada, M. and Pette, D. (1993) Relationships between alkali light-chain complement and myosin heavy-chain isoforms in single fast-twitch fibers of rat and rabbit. European Journal of Biochemistry, 214, 157-161.
 Kim, J., Hinchcliff, K.W., Yamaguchi, M., Beard, L.A., Markert, C.D. and Devor, S.T. (2005) Exercise training increases oxidative capacity and attenuates exercise-induced ultrastructural damage in skeletal muscle aged horses. Journal of Applied Physiology, 98, 334-342.
 Mascarello, F., Patruno, M., Toniolo, L., Reggiani, C. and Maccatrozzo, L. (2009) Phenothypic expression of 2b myosin heavy chain isoform: a comparative study among species and different muscles. Veterinary Research Communications, 33, 105-107.
 Lucas, C.A., Kang, L.H. and Hoh, J.F. (2000) Mono- specific antibodies against the three mammalian fast limb myosin heavy chains. Biochemical and Biophysical Re- search Communications, 272, 303-308.
 Zhong, W.W., Lucas, C.A., Kang, L.H. and Hoh, J.F. (2001) Electrophoretic and immunochemical evidence showing that marsupial limb muscles express the same fast and slow myosin heavy chains as eutherians. Electrophoresis, 22, 1016-1020.
 Toniolo, L., Patruno, M., Maccatrozzo, L., Pellegrino, M., Canepari, M., Rossi, R., D’Antona, G., Bottinelli, R., Reggiani, C. and Mascarello, F. (2004) Fast fibres in a large animal: fibre types contractile properties and myosin expression in pig skeletal muscles. The Journal of Experimantal Biology, 207, 1875-1886.
 Wada, M., Inashima, S., Yamada, T. and Matsunaga S. (2003) Endurance training-induced changes in alkali light chain patterns type IIb fibers of the rat. Journal of Applied Physiology, 94, 923-929.
 Wahrmann, J.P., Winand, R. and Rieu, M. (2001) Plasticity of skeletal myosin in endurance-trained rats (I): A quantitative study. European Journal of Applied Physiology, 84, 367-372. doi:10.1007/s004210100402
 World Medical Association Declaration of Helsinki (1997) Recommendations guiding physicians in biomedical re- search involving human subjects. Cardiovascular Research, 35, 2-3. doi:10.1016/S0008-6363(97)00109-0
 Ledwith, A. and McGowan, C.M. (2004) Muscle biopsy: A routine diagnostic procedure. Equine Veterinary Education, 16, 62-67. doi:10.1111/j.2042-3292.2004.tb00268.x
 d’Albis, A., Pantaloni, C. and Bechet, J.J. (1979) An electrophoretic study of native myosin isozymes and of their subunit content. European Journal of Biochemistry/FEBS, 99, 261-272.
 H?m?l?inen, N. and Pette, D. (1996) Slow-to-fast transitions in myosin expression of rat soleus muscle by phasic high-frequency stimulation. FEBS Letters, 399, 220-222.
 Talmadge, R.J. and Roy, R.R. (1993) Electrophoretic se- paration of rat skeletal muscle myosin heavy-chain iso- forms. Journal of Applied Physiology, 75, 2337-2340.
 Kohn, T.A. and Myburgh, K.A. (2006) Electrophoretic separation of human skeletal muscle myosin heavy chain isoforms: the importance of reducing agents. The Journal of Physiological Sciences, 56, 355-360.
 Oakley, B.R., Kirsch, D.R. and Morris, N.R. (1980) A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Analytical Biochemistry, 105, 361- 363. doi:10.1016/0003-2697(80)90470-4
 Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
 Neuhoff, V., Stamm, R. and Eibl, H. (1985) Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: A systematic analysis. Electrophoresis, 6, 427-448.
 Larsson, L. and Moss, R.L. (1993) Maximum velocity of shortening in relation to myosin isoform composition in single fibres from human skeletal muscles. The Journal of Physiology, 472, 595-614.
 Reiser, P.J., Moss, R.L., Giulian, G.G. and Greaser, M.L. (1985) Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. The Journal of Biological Chemistry, 260, 9077-9080.
 Leisson, K., Alev, K., Kaasik, P., Jaakma, ü. and Seene, T. (2011) Myosin heavy chain pattern in the Akhal-Teke horses. Animal, 5, 658-662.
 Seene, T., Alev, K., Kaasik, P., Pehme, A. and Parring, A.-M. (2005) Endurance training: Volume-dependent adaptational changes in myosin. International Journal of Sports Medicine, 26, 815-821.
 Seene, T., Alev, K., Kaasik, P. and Pehme, A. (2007) Changes in fast-twitch muscle oxidative capacity and myosin isoforms modulation during endurance training. Journal of Sports Medicine and Physical Fitness, 47, 124-132.
 Bottinelli, R. (2001) Functional heterogeneity of mammalian single muscle fibres: do myosin isoforms tell the whole story? Pflügers Archiv: European Journal of Physiology, 443, 6-17.
 Eimre, M., Puhke, R., Alev, K., Seppet, E., Sikkut, A., Peet, N., Kadaja, L., Lenzner, A., Haviko, T., Seene, T., Saks, V.A. and Seppet, E.K. (2006) Altered mitochondrial apparent affinity for ADP and impaired function of mitochondrial creatine kinase in gluteus medius of patients with hip osteoarthritis. American Journal of Physiology— Regulatory, Integrative and Comparative Physiology, 290, R1271-R1275. doi:10.1152/ajpregu.00651.2005
 Neunh?userer, D., Zebedin, M., Obermoser, M., Moser, G., Tauber, M., Niebauer, J., Resch, H. and Galler, S. (2011) Human skeletal muscle: transition between fast and slow fibre types. Pflügers Archiv: European Journal of Physiology, 461, 537-543.