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

doi:10.1083/jcb.98.4.1514

This Article

	Full Text (PDF, 1339K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Dennis, J. E.
	Articles by Fischman, D. A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Dennis, J. E.
	Articles by Fischman, D. A.


Social Bookmarking

	What's this?

ARTICLES

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

JE Dennis, T Shimizu, FC Reinach and DA Fischman

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.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Matsumoto, Y., Park, I.-K., Kohyama, K. (2009). Matrix Metalloproteinase (MMP)-9, but Not MMP-2, Is Involved in the Development and Progression of C Protein-Induced Myocarditis and Subsequent Dilated Cardiomyopathy. J. Immunol. 183: 4773-4781 [Abstract] [Full Text]
Katsumata, Y., Harigai, M., Sugiura, T., Kawamoto, M., Kawaguchi, Y., Matsumoto, Y., Kohyama, K., Soejima, M., Kamatani, N., Hara, M. (2007). Attenuation of Experimental Autoimmune Myositis by Blocking ICOS-ICOS Ligand Interaction. J. Immunol. 179: 3772-3779 [Abstract] [Full Text]
McGrath, M. J., Cottle, D. L., Nguyen, M.-A., Dyson, J. M., Coghill, I. D., Robinson, P. A., Holdsworth, M., Cowling, B. S., Hardeman, E. C., Mitchell, C. A., Brown, S. (2006). Four and a Half LIM Protein 1 Binds Myosin-binding Protein C and Regulates Myosin Filament Formation and Sarcomere Assembly. J. Biol. Chem. 281: 7666-7683 [Abstract] [Full Text]
Welikson, R. E., Fischman, D. A. (2002). The C-terminal IgI domains of myosin-binding proteins C and H (MyBP-C and MyBP-H) are both necessary and sufficient for the intracellular crosslinking of sarcomeric myosin in transfected non-muscle cells. J. Cell Sci. 115: 3517-3526 [Abstract] [Full Text]
Winegrad, S. (1999). Cardiac Myosin Binding Protein C. Circ. Res. 84: 1117-1126 [Abstract] [Full Text]
Gilbert, R, Cohen, J., Pardo, S, Basu, A, Fischman, D. (1999). Identification of the A-band localization domain of myosin binding proteins C and H (MyBP-C, MyBP-H) in skeletal muscle. J. Cell Sci. 112: 69-79 [Abstract]
Bonne, G., Carrier, L., Richard, P., Hainque, B., Schwartz, K. (1998). Familial Hypertrophic Cardiomyopathy : From Mutations to Functional Defects. Circ. Res. 83: 580-593 [Abstract] [Full Text]
Gautel, M., Furst, D. O., Cocco, A., Schiaffino, S. (1998). Isoform Transitions of the Myosin Binding Protein C Family in Developing Human and Mouse Muscles : Lack of Isoform Transcomplementation in Cardiac Muscle. Circ. Res. 82: 124-129 [Abstract] [Full Text]
Alyonycheva, T. N., Mikawa, T., Reinach, F. C., Fischman, D. A. (1997). Isoform-specific Interaction of the Myosin-binding Proteins (MyBPs) with Skeletal and Cardiac Myosin Is a Property of the C-terminal Immunoglobulin Domain. J. Biol. Chem. 272: 20866-20872 [Abstract] [Full Text]
Alyonycheva, T., Cohen-Gould, L., Siewert, C., Fischman, D. A., Mikawa, T. (1997). Skeletal Muscle�Specific Myosin Binding Protein-H Is Expressed in Purkinje Fibers of the Cardiac Conduction System. Circ. Res. 80: 665-672 [Abstract] [Full Text]
Gilbert, R, Kelly, M., Mikawa, T, Fischman, D. (1996). The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle. J. Cell Sci. 109: 101-111 [Abstract]
Vinkemeier, U, Obermann, W, Weber, K, Furst, D. (1993). The globular head domain of titin extends into the center of the sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins. J. Cell Sci. 106: 319-330 [Abstract]
Epstein, H., Fischman, D. (1991). Molecular analysis of protein assembly in muscle development. Science 251: 1039-1044 [Abstract]
Cooper, T., Ordahl, C. (1984). A single troponin T gene regulated by different programs in cardiac and skeletal muscle development. Science 226: 979-982 [Abstract]
Witt, C. C., Gerull, B., Davies, M. J., Centner, T., Linke, W. A., Thierfelder, L. (2001). Hypercontractile Properties of Cardiac Muscle Fibers in a Knock-in Mouse Model of Cardiac Myosin-binding Protein-C. J. Biol. Chem. 276: 5353-5359 [Abstract] [Full Text]