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. 1985 Sep 1;101(3):1001–1008. doi: 10.1083/jcb.101.3.1001

The presence of two skeletal muscle alpha-actinins correlates with troponin-tropomyosin expression and Z-line width

PMCID: PMC2113711  PMID: 4030889

Abstract

Two species of alpha-actinin from rabbit fast skeletal muscles were identified with a monospecific antisera. Designated alpha-actinin1f and alpha-actinin2f, their distribution in muscles does not correlate with histochemically defined fast fiber type. Rather, the presence of each correlates with Z-line width and with the expression of different thin filament Ca2+-regulatory complexes. alpha-Actinin1f is expressed with troponin T 1f-alpha beta tropomyosin, and alpha-actinin2f with troponin T 2f-alpha 2 tropomyosin. CNBr peptide maps show that the fast alpha- actinin species differ in primary structure. In contrast, the slow alpha-actinin is indistinguishable from alpha-actinin1f. Further evidence for the similarity of alpha-actinin1f and slow alpha-actinin comes from electron microscopic studies which show that fibers that express these species exhibit thick Z-lines. So, unlike other contractile proteins, the multiple forms of alpha-actinin do not reflect the distinction between fast- and slow-twitch muscles.

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Selected References

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  1. Briggs M. M., Klevit R. E., Schachat F. H. Heterogeneity of contractile proteins. Purification and characterization of two species of troponin T from rabbit fast skeletal muscle. J Biol Chem. 1984 Aug 25;259(16):10369–10375. [PubMed] [Google Scholar]
  2. Bronson D. D., Schachat F. H. Heterogeneity of contractile proteins. Differences in tropomyosin in fast, mixed, and slow skeletal muscles of the rabbit. J Biol Chem. 1982 Apr 10;257(7):3937–3944. [PubMed] [Google Scholar]
  3. Busch W. A., Stromer M. H., Goll D. E., Suzuki A. Ca 2+ -specific removal of Z lines from rabbit skeletal muscle. J Cell Biol. 1972 Feb;52(2):367–381. doi: 10.1083/jcb.52.2.367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Callaway J. E., Bechtel P. J. C-protein from rabbit soleus (red) muscle. Biochem J. 1981 May 1;195(2):463–469. doi: 10.1042/bj1950463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dhoot G. K., Frearson N., Perry S. V. Polymorphic forms of troponin T and troponin C and their localization in striated muscle cell types. Exp Cell Res. 1979 Sep;122(2):339–350. doi: 10.1016/0014-4827(79)90310-0. [DOI] [PubMed] [Google Scholar]
  6. Ebashi S., Kodama A., Ebashi F. Troponin. I. Preparation and physiological function. J Biochem. 1968 Oct;64(4):465–477. doi: 10.1093/oxfordjournals.jbchem.a128918. [DOI] [PubMed] [Google Scholar]
  7. Eisenberg B. R., Kuda A. M. Discrimination between fiber populations in mammalian skeletal muscle by using ultrastructural parameters. J Ultrastruct Res. 1976 Jan;54(1):76–88. doi: 10.1016/s0022-5320(76)80010-x. [DOI] [PubMed] [Google Scholar]
  8. Frearson N., Perry S. V. Phosphorylation of the light-chain components of myosin from cardiac and red skeletal muscles. Biochem J. 1975 Oct;151(1):99–107. doi: 10.1042/bj1510099. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gauthier G. F. Ultrastructural identification of muscle fiber types by immunocytochemistry. J Cell Biol. 1979 Aug;82(2):391–400. doi: 10.1083/jcb.82.2.391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kobayashi R., Itoh H., Tashima Y. Different muscle-specific forms of rabbit skeletal muscle alpha-actinin. Eur J Biochem. 1984 Aug 15;143(1):125–131. doi: 10.1111/j.1432-1033.1984.tb08351.x. [DOI] [PubMed] [Google Scholar]
  11. Kobayashi R., Itoh H., Tashima Y. Polymorphism of alpha-actinin. Electrophoretic and immunological studies of rabbit skeletal muscle alpha-actinins. Eur J Biochem. 1983 Jul 1;133(3):607–611. doi: 10.1111/j.1432-1033.1983.tb07505.x. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Lazarides E., Burridge K. Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell. 1975 Nov;6(3):289–298. doi: 10.1016/0092-8674(75)90180-4. [DOI] [PubMed] [Google Scholar]
  14. Matsuda R., Obinata T., Shimada Y. Types of troponin components during development of chicken skeletal muscle. Dev Biol. 1981 Feb;82(1):11–19. doi: 10.1016/0012-1606(81)90424-3. [DOI] [PubMed] [Google Scholar]
  15. Matsuda R., Spector D., Strohman R. C. Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins. Proc Natl Acad Sci U S A. 1984 Feb;81(4):1122–1125. doi: 10.1073/pnas.81.4.1122. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Peter J. B., Barnard R. J., Edgerton V. R., Gillespie C. A., Stempel K. E. Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits. Biochemistry. 1972 Jul 4;11(14):2627–2633. doi: 10.1021/bi00764a013. [DOI] [PubMed] [Google Scholar]
  17. Reddy M. K., Etlinger J. D., Rabinowitz M., Fischman D. A., Zak R. Removal of Z-lines and alpha-actinin from isolated myofibrils by a calcium-activated neutral protease. J Biol Chem. 1975 Jun 10;250(11):4278–4284. [PubMed] [Google Scholar]
  18. Reedy M. K. Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice. J Mol Biol. 1968 Jan 28;31(2):155–176. doi: 10.1016/0022-2836(68)90437-3. [DOI] [PubMed] [Google Scholar]
  19. Reinach F. C., Masaki T., Fischman D. A. Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere. J Cell Biol. 1983 Jan;96(1):297–300. doi: 10.1083/jcb.96.1.297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sato T. A modified method for lead staining of thin sections. J Electron Microsc (Tokyo) 1968;17(2):158–159. [PubMed] [Google Scholar]
  21. Schachat F. H., Bronson D. D., McDonald O. B. Heterogeneity of contractile proteins. A continuum of troponin-tropomyosin expression in mammalian skeletal muscle. J Biol Chem. 1985 Jan 25;260(2):1108–1113. [PubMed] [Google Scholar]
  22. Schachat F. H., Bronson D. D., McDonald O. B. Two kinds of slow skeletal muscle fibers which differ in their myosin light chain complements. FEBS Lett. 1980 Dec 15;122(1):80–82. doi: 10.1016/0014-5793(80)80406-6. [DOI] [PubMed] [Google Scholar]
  23. Suzuki A., Goll D. E., Singh I., Allen R. E., Robson R. M., Stromer M. H. Some properties of purified skeletal muscle alpha-actinin. J Biol Chem. 1976 Nov 10;251(21):6860–6870. [PubMed] [Google Scholar]
  24. Suzuki A., Goll D. E., Stromer M. H., Temple J. -actinin from red and white porcine muscle. Biochim Biophys Acta. 1973 Jan 25;295(1):188–207. doi: 10.1016/0005-2795(73)90087-1. [DOI] [PubMed] [Google Scholar]
  25. 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]

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