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. 1986 Sep 1;103(3):977–983. doi: 10.1083/jcb.103.3.977

The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle

PMCID: PMC2114298  PMID: 3528174

Abstract

Hypertrophy was produced in the anterior latissimus dorsi (ALD) muscle of 5-wk-old chickens by application of a load to the humerus. After 4 wk, hypertrophied ALD muscles were greater than 2.5 times heavier than contralateral control ALD muscles. Two isomyosins are distinguishable in normal ALD muscles by their different electrophoretic mobilities. It is shown here that the faster migrating SM-1 isomyosin decreases in abundance with age and that the application of an overload enhances both the rate and extent of this process. Monoclonal antibodies were selected by an immunotransfer technique that were specific for the heavy chains associated with either SM-1 or SM-2, or cross-reacted with both isoforms. The cellular distribution of the SM-1 and SM-2 isomyosins was analyzed by immunofluorescent technique using these antibodies. Anti-SM-1 and anti-SM-2 antibodies reacted with separate populations of cells, whereas the third antibody reacted with all myocytes in the normal ALD muscle. These data suggest that there is an exclusive cellular distribution of myosin heavy chains associated with SM-1 and SM-2 proteins. Immunofluorescent analysis of hypertrophied muscle showed the anti-SM-2-specific antibody reacting with all myocytes, whereas the anti-SM-1-specific antibody reacted with none. This is consistent with the elimination of the SM-1 isoform in hypertrophied muscles.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ashmore C. R., Lee Y. B., Summers P., Hitchcock L. Stretch-induced growth in chicken wing muscles: nerve-muscle interaction in muscular dystrophy. Am J Physiol. 1984 May;246(5 Pt 1):C378–C384. doi: 10.1152/ajpcell.1984.246.5.C378. [DOI] [PubMed] [Google Scholar]
  2. Ashmore C. R. Stretch-induced growth in chicken wing muscles: effects on hereditary muscular dystrophy. Am J Physiol. 1982 Mar;242(3):C178–C183. doi: 10.1152/ajpcell.1982.242.3.C178. [DOI] [PubMed] [Google Scholar]
  3. Bader D., Masaki T., Fischman D. A. Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro. J Cell Biol. 1982 Dec;95(3):763–770. doi: 10.1083/jcb.95.3.763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bandman E., Matsuda R., Strohman R. C. Developmental appearance of myosin heavy and light chain isoforms in vivo and in vitro in chicken skeletal muscle. Dev Biol. 1982 Oct;93(2):508–518. doi: 10.1016/0012-1606(82)90138-5. [DOI] [PubMed] [Google Scholar]
  5. Barnett J. G., Holly R. G., Ashmore C. R. Stretch-induced growth in chicken wing muscles: biochemical and morphological characterization. Am J Physiol. 1980 Jul;239(1):C39–C46. doi: 10.1152/ajpcell.1980.239.1.C39. [DOI] [PubMed] [Google Scholar]
  6. Benfield P. A., Lowey S., LeBlanc D. D., Waller G. S. Myosin isozymes in avian skeletal muscles. II. Fractionation of myosin isozymes from adult and embryonic chicken pectoralis muscle by immuno-affinity chromatography. J Muscle Res Cell Motil. 1983 Dec;4(6):717–738. doi: 10.1007/BF00712162. [DOI] [PubMed] [Google Scholar]
  7. Bormioli S. P., Sartore S., Vitadello M., Schiaffino S. "Slow" myosins in vertebrate skeletal muscle. An immunofluorescence study. J Cell Biol. 1980 Jun;85(3):672–681. doi: 10.1083/jcb.85.3.672. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Clark W. A., Jr, Chizzonite R. A., Everett A. W., Rabinowitz M., Zak R. Species correlations between cardiac isomyosins. A comparison of electrophoretic and immunological properties. J Biol Chem. 1982 May 25;257(10):5449–5454. [PubMed] [Google Scholar]
  9. Gollnick P. D., Parsons D., Riedy M., Moore R. L. Fiber number and size in overloaded chicken anterior latissimus dorsi muscle. J Appl Physiol Respir Environ Exerc Physiol. 1983 May;54(5):1292–1297. doi: 10.1152/jappl.1983.54.5.1292. [DOI] [PubMed] [Google Scholar]
  10. Gutmann E., Hájek I., Vítek V. Compensatory hypertrophy of the latissimus dorsi posterior muscle induced by elimination of the latissimus dorsi anterior muscle of the chicken. Physiol Bohemoslov. 1970;19(6):483–489. [PubMed] [Google Scholar]
  11. Hoh J. F., McGrath P. A., Hale P. T. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol. 1978 Nov;10(11):1053–1076. doi: 10.1016/0022-2828(78)90401-7. [DOI] [PubMed] [Google Scholar]
  12. Hoh J. Y., McGrath P. A., White R. I. Electrophoretic analysis of multiple forms of myosin in fast-twitch and slow-twitch muscles of the chick. Biochem J. 1976 Jul 1;157(1):87–95. doi: 10.1042/bj1570087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laurent G. J., Sparrow M. P., Millward D. J. Turnover of muscle protein in the fowl. Changes in rates of protein synthesis and breakdown during hypertrophy of the anterior and posterior latissimus dorsi muscles. Biochem J. 1978 Nov 15;176(2):407–417. doi: 10.1042/bj1760407. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lowey S., Benfield P. A., LeBlanc D. D., Waller G. S. Myosin isozymes in avian skeletal muscles. I. Sequential expression of myosin isozymes in developing chicken pectoralis muscles. J Muscle Res Cell Motil. 1983 Dec;4(6):695–716. doi: 10.1007/BF00712161. [DOI] [PubMed] [Google Scholar]
  15. Matsuda R., Bandman E., Strohman R. C. The two myosin isoenzymes of chicken anterior latissimus dorsi muscle contain different myosin heavy chains encoded by separate mRNAs. Differentiation. 1982;23(1):36–42. doi: 10.1111/j.1432-0436.1982.tb01265.x. [DOI] [PubMed] [Google Scholar]
  16. Matsuda R., Spector D. H., Strohman R. C. Regenerating adult chicken skeletal muscle and satellite cell cultures express embryonic patterns of myosin and tropomyosin isoforms. Dev Biol. 1983 Dec;100(2):478–488. doi: 10.1016/0012-1606(83)90240-3. [DOI] [PubMed] [Google Scholar]
  17. McDonagh M. J., Davies C. T. Adaptive response of mammalian skeletal muscle to exercise with high loads. Eur J Appl Physiol Occup Physiol. 1984;52(2):139–155. doi: 10.1007/BF00433384. [DOI] [PubMed] [Google Scholar]
  18. Shafiq S. A., Shimizu T., Fischman D. A. Heterogeneity of type 1 skeletal muscle fibers revealed by monoclonal antibody to slow myosin. Muscle Nerve. 1984 Jun;7(5):380–387. doi: 10.1002/mus.880070507. [DOI] [PubMed] [Google Scholar]
  19. Sola O. M., Christensen D. L., Martin A. W. Hypertrophy and hyperplasia of adult chicken anterior latissimus dorsi muscles following stretch with and without denervation. Exp Neurol. 1973 Oct;41(1):76–100. doi: 10.1016/0014-4886(73)90182-9. [DOI] [PubMed] [Google Scholar]
  20. Sparrow M. P. Regression of skeletal muscle of chicken wing after stretch-induced hypertrophy. Am J Physiol. 1982 May;242(5):C333–C338. doi: 10.1152/ajpcell.1982.242.5.C333. [DOI] [PubMed] [Google Scholar]
  21. Sweeney L. J., Clark W. A., Jr, Umeda P. K., Zak R., Manasek F. J. Immunofluorescence analysis of the primordial myosin detectable in embryonic striated muscle. Proc Natl Acad Sci U S A. 1984 Feb;81(3):797–800. doi: 10.1073/pnas.81.3.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Vandenburgh H., Kaufman S. In vitro model for stretch-induced hypertrophy of skeletal muscle. Science. 1979 Jan 19;203(4377):265–268. doi: 10.1126/science.569901. [DOI] [PubMed] [Google Scholar]
  24. d'Albis A., Gratzer W. B. Electrophoretic examination of native myosin. FEBS Lett. 1973 Feb 1;29(3):292–296. doi: 10.1016/0014-5793(73)80042-0. [DOI] [PubMed] [Google Scholar]
  25. d'Albis A., Pantaloni C., Bechet J. J. An electrophoretic study of native myosin isozymes and of their subunit content. Eur J Biochem. 1979 Sep;99(2):261–272. doi: 10.1111/j.1432-1033.1979.tb13253.x. [DOI] [PubMed] [Google Scholar]

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