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The isoforms of C protein and their distribution in mammalian skeletal muscle

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Summary

A monoclonal antibody that is specific for the slow skeletal muscle isoform of C protein of rabbit muscle has been prepared by immunizing mice with a crude preparation of human myosin. It reacted with the X protein fraction of rabbit skeletal muscle and stained all type I cells in this tissue. It also stained a fraction of the type II cells with varying intensities. The type II cells staining with antibody to slow C protein also stained with a polyclonal antibody prepared against rabbit fast muscle C protein. The type II cells not staining with antibody to slow C protein stained strongly with antibody to fast C protein. In the human skeletal muscle antibody to slow C protein stained all cells whereas antibody to fast C stained only type II cells. It is concluded that the distribution of the isoforms of C protein in adult vertebrate skeletal muscle is more complex than is the case with proteins such as components of the troponin complex.

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References

  1. CALLAWAY, J. E. & BECHTEL, P. J. (1981) C protein from rabbit soleus (red) muscle.Biochem. J. 195 463–9.

  2. DE BLAS, A. L. & CHERWINSKI, H. M. (1983) Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies.Analyt. Biochem. 133 214–19.

  3. DENNIS, J. E., SHIMIZU, T., REINACH, F. C. & FISCHMAN, D. A. (1984) Localization of C protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies.J. Cell Biol. 98 1514–22.

  4. DHOOT, G. K., FREARSON, N. & PERRY, S. V. (1979) Polymorphic forms of troponin T and troponin C and their localization in striated muscle cell types.Expl Cell Res. 122 339–50.

  5. DHOOT, G. K., GELL, P. G. H. & PERRY, S. V. (1978) The localisation of the different forms of troponin I in skeletal and cardiac muscle.Expl Cell Res. 117 357–70.

  6. DHOOT, G. K. & PERRY, S. V. (1982) The effect of denervation on the distribution of the polymorphic forms of troponin components in fast and slow muscles of the rat.Cell Tiss. Res. 225 201–15.

  7. DRAPER, M. H. & HODGE, A. J. (1949) Studies on muscle with the electron microscope. 1. The ultrastructure of toad striated muscle.Aust. J. Exp. Biol. Med. Sci. 37 465–503.

  8. DUBOWITZ, V. & BROOKE, M. H. (1973) Histological and histochemical stains and reactions. InMuscle Biopsy: A Modern Approach. p. 32. London, Philadelphia, Toronto: W. B. Saunders.

  9. HEELEY, D. H. DHOOT, G. K., FREARSON, N. PERRY, S. V. & VRBOVA, G. (1983) The effect of cross innervation on the tropomyosin composition of rabbit skeletal muscle.FEBS Lett. 152 282–6.

  10. KOHLER, G. & MILSTEIN, C. (1975) continuous culture of fused cells secreting specific antibody.Nature 256 495–7.

  11. LOWE, G., HARDIE, D., JEFFERIS, R., LING, N. R., DRYSDALE, P., RICHARDSON, P. RAYKUNDALIA, C., CATTY, D., APPLEBY, P., DREW, R. & MACLENNAN, I. C. M. (1981) Properties of monoclonal antibodies to human immunoglobulin kappa and lambda chains.Immunology 42 649–59.

  12. MOOS, C. & FENG, I. M. (1980) Effect of C-protein on actomyosin ATPase.biochem. biophys. Acta,632 141–9.

  13. MOOS, C., MASON, C. M., BESTERMAN, J. M., FENG, I. M. & DUBIN, J. H. (1978) The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment 1.J. molec. Biol. 124 571–86.

  14. MOOS, C., OFFER, G., STARR, R. & BENNETT, P. (1975) Interaction of C-protein with myosin, myosin rod and light meromyosin.J. molec. Biol. 97 1–9.

  15. OBINATA, T., REINACH, F. C., BADER, D. M., MASAKI, T., KITANI, S. & FISCHMAN, D. A. (1984) Immunochemical analysis of C-protein isoform transitions during the development of chicken skeletal muscle.Devl Biol. 101 116–24.

  16. OFFER, G. (1972) C protein and the periodicity in the thick filaments of vertebrate skeletal muscle.Cold Spring Harb. Symp. quant. Biol. 37 87–95.

  17. OFFER, G., MOOS, C. & STARR, R. (1973) A new protein of the thick filaments of vertebrate skeletal myofibrils.J. molec. Biol. 74 653–76.

  18. PEPE, F. A. & DRUCKER, B. (1975) The myosin filament C protein.J. Cell Biol. 99 609–17.

  19. PERRY, S. V., DHOOT, G. K. & HEELEY, D. H. (1984) Muscle protin isoforms and physiological function: role of nerve in gene expression.Symp. Biochem. Soc. 49 137–47.

  20. PERRY, S. V. & ZYDOWO, M. (1959) A ribonucleoprotein of skeletal muscle and its relation to the myofibril.Biochem. J. 72 682–90.

  21. REINACH, F. C., MASAKI, T., SHAFIQ, S., OBINATA, T. & FISCHMANN, D. A. (1982) Isoforms of C protein in adult chicken skeletal muslce. Detection with monoclonal antibodies.J. Cell Biol. 95 78–84.

  22. ROUND, J. M., Matthews, Y. & JONES, D. A. (1980) A quick, simple and reliable histochemical method for ATPase in human muscle preparations.Histochem. J. 12 707–10.

  23. RUBINSTEIN, N. A. & KELLY, A. M. (1978) Myogenic and neurogenic contributions to the development of fast and slow twitch muscles in the rat.Devl Biol. 62 473–85.

  24. SPENCER, M. (1978) Hydroxypatite for chromatography. Sources of variability and improved methods of preparation.J. Chromat. 166 435–46.

  25. STARR, R., BENNETT, P. & OFFER, G. (1980) X-Protein and its polymer.J. Musc. Res. Cell Motility 1 205–6.

  26. STARR, R. & OFFER, G. (1982) Preparation of C-protein, H-protein, X-protin and phosphofructokinase.Meth. Enzym. 85 130–8.

  27. STARR, R. & OFFER, G. (1983) H Protein and X Protein. Two new components of the thick filaments of vertebrate skeletal muslce.J. molec. Biol. 170 675–98.

  28. TOWBIN, H., STAEHELIN, T. & GORDON, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proc. natn. Acad. Sci. U.S.A. 76 4350–4.

  29. VANDEKERCKHOVE, J. & WEBER, K. (1979) The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle and rabbit slow skeletal muscle.Differentiation 14 123–33.

  30. WEEDS, A. G., HALL, R. & SPURWAY, N. C. (1975) Characterisation of myosin light chains from histochemically identified fibres of rabbit psoas muscle.FEBS Lett. 49 320–4.

  31. WILKINSON, J. M., PERRY, S. V., COLE, H. A. & TRAYER, I. P. (1972) The regulatory proteins of the myofibril. Separation and biological activity of the components of the inhibitory-factor preparations.Biochem. J. 127 215–28.

  32. WRAY, W., BOULIKAS, T., WRAY, V. P. & HANCOCK, R. (1981) Silver staining of proteins in polyacrylamide gels.Analyt. Biochem. 118 197–203.

  33. YAMAMOTO, K. & MOOS, C. (1981) A comparative study of C proteins from heart and skeletal muscles.Biophys. J. 33, 237a.

  34. YAMAMOTO, K. & MOOS, C. (1983) The C-proteins of rabbit red, white and cardiac muscles.J. biol. Chem. 258 8395–401.

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Dhoot, G.K., Hales, M.C., Grail, B.M. et al. The isoforms of C protein and their distribution in mammalian skeletal muscle. J Muscle Res Cell Motil 6, 487–505 (1985). https://doi.org/10.1007/BF00712585

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Keywords

  • Monoclonal Antibody
  • Skeletal Muscle
  • Polyclonal Antibody
  • Protein Fraction
  • Human Skeletal Muscle