Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1984 Apr 1;98(4):1514–1522. doi: 10.1083/jcb.98.4.1514

Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies

PMCID: PMC2113215  PMID: 6546932

Abstract

Monoclonal antibodies (McAbs) specific for the fast (MF-1) and slow (ALD-66) isoforms of C-protein from chicken skeletal muscle have been produced and characterized. Using these antibodies it was possible to demonstrate that skeletal muscles of varying fiber type express different isoforms of this protein and that in the posterior latissimus dorsi muscle both isoforms are co-expressed in the same myofiber (17, 18). Since we had shown that both isoforms were present in all sarcomeres, it was feasible to test whether the two isoforms co- distributed in the same 43-nm repeat within the A-band, thereby establishing a minimum number of C-proteins per repeat in the thick filaments. Here we describe the ultrastructural localization of C- protein in myofibers from three muscle types of the chicken using these same McAbs. We observed that although C-protein was present in a 43-nm repeat along the filaments in all three muscles, there were marked differences in the absolute number and position occupied by the different isoforms. Since McAbs MF-1 and ALD-66 decorated the same 43- nm repeats in the A-bands of the posterior latissimus dorsal muscle, we suggest that at least two C-proteins can co-localize at binding sites 43 nm apart along thick filaments of this muscle.

Full Text

The Full Text of this article is available as a PDF (1.3 MB).

Selected References

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

  1. 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]
  2. Craig R., Offer G. The location of C-protein in rabbit skeletal muscle. Proc R Soc Lond B Biol Sci. 1976 Mar 16;192(1109):451–461. doi: 10.1098/rspb.1976.0023. [DOI] [PubMed] [Google Scholar]
  3. Craig R. Structure of A-segments from frog and rabbit skeletal muscle. J Mol Biol. 1977 Jan 5;109(1):69–81. doi: 10.1016/s0022-2836(77)80046-6. [DOI] [PubMed] [Google Scholar]
  4. HUXLEY H. E. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. J Mol Biol. 1963 Sep;7:281–308. doi: 10.1016/s0022-2836(63)80008-x. [DOI] [PubMed] [Google Scholar]
  5. Haselgrove J. C. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J Mol Biol. 1975 Feb 15;92(1):113–143. doi: 10.1016/0022-2836(75)90094-7. [DOI] [PubMed] [Google Scholar]
  6. Huxley H. E., Brown W. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J Mol Biol. 1967 Dec 14;30(2):383–434. doi: 10.1016/s0022-2836(67)80046-9. [DOI] [PubMed] [Google Scholar]
  7. Koretz J. F. Effects of C-protein on synthetic myosin filament structure. Biophys J. 1979 Sep;27(3):433–446. doi: 10.1016/S0006-3495(79)85227-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Moos C., Mason C. M., Besterman J. M., Feng I. N., Dubin J. H. The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J Mol Biol. 1978 Oct 5;124(4):571–586. doi: 10.1016/0022-2836(78)90172-9. [DOI] [PubMed] [Google Scholar]
  9. Moos C., Offer G., Starr R., Bennett P. Interaction of C-protein with myosin, myosin rod and light meromyosin. J Mol Biol. 1975 Sep 5;97(1):1–9. doi: 10.1016/s0022-2836(75)80017-9. [DOI] [PubMed] [Google Scholar]
  10. Offer G., Moos C., Starr R. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J Mol Biol. 1973 Mar 15;74(4):653–676. doi: 10.1016/0022-2836(73)90055-7. [DOI] [PubMed] [Google Scholar]
  11. PAGE S. G., HUXLEY H. E. FILAMENT LENGTHS IN STRIATED MUSCLE. J Cell Biol. 1963 Nov;19:369–390. doi: 10.1083/jcb.19.2.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pepe F. A., Drucker B. The myosin filament. III. C-protein. J Mol Biol. 1975 Dec 25;99(4):609–617. doi: 10.1016/s0022-2836(75)80175-6. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Reinach F. C., Masaki T., Shafiq S., Obinata T., Fischman D. A. Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies. J Cell Biol. 1982 Oct;95(1):78–84. doi: 10.1083/jcb.95.1.78. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sjöström M., Squire J. M. Fine structure of the A-band in cryo-sections. The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J Mol Biol. 1977 Jan 5;109(1):49–68. doi: 10.1016/s0022-2836(77)80045-4. [DOI] [PubMed] [Google Scholar]
  16. Starr R., Offer G. The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem J. 1978 Jun 1;171(3):813–816. doi: 10.1042/bj1710813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Whalen R. G., Sell S. M., Butler-Browne G. S., Schwartz K., Bouveret P., Pinset-Härstöm I. Three myosin heavy-chain isozymes appear sequentially in rat muscle development. Nature. 1981 Aug 27;292(5826):805–809. doi: 10.1038/292805a0. [DOI] [PubMed] [Google Scholar]
  18. Wilson F. J., Irish M. J. The structure of segments of the anisotropic band of muscle. II. Preparation and properties of A segments from vertebrate skeletal muscle. Cell Tissue Res. 1980;212(2):213–223. doi: 10.1007/BF00233956. [DOI] [PubMed] [Google Scholar]
  19. Yamamoto K., Moos C. The C-proteins of rabbit red, white, and cardiac muscles. J Biol Chem. 1983 Jul 10;258(13):8395–8401. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES