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. 1984 Aug 1;221(3):645–650. doi: 10.1042/bj2210645

Loss of fast-twitch isomyosins in skeletal muscles of the diabetic rat.

M Rutschmann, B Dahlmann, H Reinauer
PMCID: PMC1144093  PMID: 6477492

Abstract

By means of pyrophosphate electrophoresis the myosin isoenzyme pattern of two fast-twitch skeletal muscles (extensor digitorum longus, gastrocnemius) and one slow-twitch muscle (soleus) was investigated in control rats and was compared with that of rats 4 weeks after induction of diabetes mellitus by streptozotocin injection. In the fast-twitch muscles the isomyosin pattern consisting of FM1 (fast isomyosin 1), FM2 and FM3 was strongly affected by diabetes, resulting in an extensive loss of FM1 and a substantial decrease of FM2. These changes were also apparent when the light chains of the fast isomyosins were analysed by two-dimensional electrophoresis: LC3f (myosin light chain 3f) largely disappeared and LC2f was significantly diminished. In contrast, the isomyosin pattern in soleus muscle, consisting of SM1 (slow isomyosin 1) and SM2, was not affected by the diabetic state, and two-dimensional electrophoresis revealed a normal light-chain pattern of LC1sa, LC1sb and LC2s. These results indicate that the isomyosins of slow-twitch oxidative myofibres are more resistant to the hormonal and metabolic disorders during diabetes mellitus than are the isomyosins of fast-twitch fibres.

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Selected References

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

  1. Ariano M. A., Armstrong R. B., Edgerton V. R. Hindlimb muscle fiber populations of five mammals. J Histochem Cytochem. 1973 Jan;21(1):51–55. doi: 10.1177/21.1.51. [DOI] [PubMed] [Google Scholar]
  2. Armstrong R. B., Gollnick P. D., Ianuzzo C. D. Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats. Cell Tissue Res. 1975 Oct 13;162(3):387–394. doi: 10.1007/BF00220185. [DOI] [PubMed] [Google Scholar]
  3. Armstrong R. B., Ianuzzo C. D. Compensatory hypertrophy of skeletal muscle fibers in streptozotocin-diabetic rats. Cell Tissue Res. 1977 Jul 11;181(2):255–266. doi: 10.1007/BF00219985. [DOI] [PubMed] [Google Scholar]
  4. Billeter R., Heizmann C. W., Reist U., Howald H., Jenny E. Two-dimensional peptide analysis of myosin heavy chains and actin from single-typed human skeletal muscle fibers. FEBS Lett. 1982 Mar 8;139(1):45–48. doi: 10.1016/0014-5793(82)80483-3. [DOI] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  6. Carraro U., Catani C., Dalla Libera L. Myosin light and heavy chains in rat gastrocnemius and diaphragm muscles after chronic denervation or reinnervation. Exp Neurol. 1981 May;72(2):401–412. doi: 10.1016/0014-4886(81)90232-6. [DOI] [PubMed] [Google Scholar]
  7. Carraro U., Catani C., Dalla Libera L., Vascon M., Zanella G. Differential distribution of tropomyosin subunits in fast and slow rat muscles and its change in long-term denervated hemidiaphragm. FEBS Lett. 1981 Jun 15;128(2):233–236. doi: 10.1016/0014-5793(81)80088-9. [DOI] [PubMed] [Google Scholar]
  8. Carraro U., Dalla Libera L., Catani C., Danieli-Betto D. Chronic denervation of rat diaphragm: selective maintenance of adult fast myosin heavy chains. Muscle Nerve. 1982 Sep;5(7):515–524. doi: 10.1002/mus.880050706. [DOI] [PubMed] [Google Scholar]
  9. Chao T. T., Ianuzzo C. D., Armstrong R. B., Albright J. T., Anapolle S. E. Ultrastructural alterations in skeletal muscle fibers of streptozotocin-diabetic rats. Cell Tissue Res. 1976 May 6;168(2):239–246. doi: 10.1007/BF00215880. [DOI] [PubMed] [Google Scholar]
  10. Dahlmann B., Schroeter C., Herbertz L., Reinauer H. Myofibrillar protein degradation and muscle proteinases in normal and diabetic rats. Biochem Med. 1979 Feb;21(1):33–39. doi: 10.1016/0006-2944(79)90052-8. [DOI] [PubMed] [Google Scholar]
  11. Dhoot G. K., Perry S. V. Distribution of polymorphic forms of troponin components and tropomyosin in skeletal muscle. Nature. 1979 Apr 19;278(5706):714–718. doi: 10.1038/278714a0. [DOI] [PubMed] [Google Scholar]
  12. Dillmann W. H. Diabetes mellitus induces changes in cardiac myosin of the rat. Diabetes. 1980 Jul;29(7):579–582. doi: 10.2337/diab.29.7.579. [DOI] [PubMed] [Google Scholar]
  13. Fitzsimons R. B., Hoh J. F. Isomyosins in human type 1 and type 2 skeletal muscle fibres. Biochem J. 1981 Jan 1;193(1):229–233. doi: 10.1042/bj1930229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Flaim K. E., Copenhaver M. E., Jefferson L. S. Effects of diabetes on protein synthesis in fast- and slow-twitch rat skeletal muscle. Am J Physiol. 1980 Jul;239(1):E88–E95. doi: 10.1152/ajpendo.1980.239.1.E88. [DOI] [PubMed] [Google Scholar]
  15. Flink I. L., Rader J. H., Morkin E. Thyroid hormone stimulates synthesis of a cardiac myosin isozyme. Comparison of the two-two-dimensional electrophoretic patterns of the cyanogen bromide peptides of cardiac myosin heavy chains from euthyroid and thyrotoxic rabbits. J Biol Chem. 1979 Apr 25;254(8):3105–3110. [PubMed] [Google Scholar]
  16. Garlick P. J., Albertse E. C., McNurlan M. A., Pain V. M. Protein turnover in tissues of diabetic rats. Acta Biol Med Ger. 1981;40(10-11):1301–1307. [PubMed] [Google Scholar]
  17. Hoh J. F. Light chain distribution of chicken skeletal muscle myosin isoenzymes. FEBS Lett. 1978 Jun 15;90(2):297–300. doi: 10.1016/0014-5793(78)80390-1. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Hoh J. F., Yeoh G. P. Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles. Nature. 1979 Jul 26;280(5720):321–323. doi: 10.1038/280321a0. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Johnson M. A., Mastaglia F. L., Montgomery A. G., Pope B., Weeds A. G. Changes in myosin light chains in the rat soleus after thyroidectomy. FEBS Lett. 1980 Feb 11;110(2):230–235. doi: 10.1016/0014-5793(80)80080-9. [DOI] [PubMed] [Google Scholar]
  22. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  23. Pain V. M., Garlick P. J. Effect of streptozotocin diabetes and insulin treatment on the rate of protein synthesis in tissues of the rat in vivo. J Biol Chem. 1974 Jul 25;249(14):4510–4514. [PubMed] [Google Scholar]
  24. Röthig H. J., Stiller N., Dahlmann B., Reinauer H. Insulin effect on proteolytic activities in rat skeletal muscle. Horm Metab Res. 1978 Mar;10(2):101–104. doi: 10.1055/s-0028-1093452. [DOI] [PubMed] [Google Scholar]
  25. Tischler M. E. Hormonal regulation of protein degradation in skeletal and cardiac muscle. Life Sci. 1981 Jun 8;28(23):2569–2576. doi: 10.1016/0024-3205(81)90713-x. [DOI] [PubMed] [Google Scholar]
  26. Unsworth B. R., Witzmann F. A., Fitts R. H. A comparison of rat myosin from fast and slow skeletal muscle and the effect of disuse. J Biol Chem. 1982 Dec 25;257(24):15129–15136. [PubMed] [Google Scholar]
  27. Zweig S. E. The muscle specificity and structure of two closely related fast-twitch white muscle myosin heavy chain isozymes. J Biol Chem. 1981 Nov 25;256(22):11847–11853. [PubMed] [Google Scholar]
  28. 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]
  29. d'Albis A., Pantaloni C., Bechet J. J. Myosin isoenzymes in adult rat skeletal muscles. Biochimie. 1982 Jun;64(6):399–404. doi: 10.1016/s0300-9084(82)80577-4. [DOI] [PubMed] [Google Scholar]

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