The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle

doi:10.1083/jcb.103.3.977

This Article

	Full Text (PDF, 1883K)
	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 Kennedy, J. M.
	Articles by Zak, R.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Kennedy, J. M.
	Articles by Zak, R.


Social Bookmarking

	What's this?

ARTICLES

The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle

JM Kennedy, S Kamel, WW Tambone, G Vrbova and R Zak

Hypertrophy was produced in the anterior latissimus dorsi (ALD) muscle of 5-wk-old chickens by application of a load to the humerus. After 4 wk, hypertrophied ALD muscles were greater than 2.5 times heavier than contralateral control ALD muscles. Two isomyosins are distinguishable in normal ALD muscles by their different electrophoretic mobilities. It is shown here that the faster migrating SM-1 isomyosin decreases in abundance with age and that the application of an overload enhances both the rate and extent of this process. Monoclonal antibodies were selected by an immunotransfer technique that were specific for the heavy chains associated with either SM-1 or SM-2, or cross-reacted with both isoforms. The cellular distribution of the SM-1 and SM-2 isomyosins was analyzed by immunofluorescent technique using these antibodies. Anti-SM-1 and anti-SM-2 antibodies reacted with separate populations of cells, whereas the third antibody reacted with all myocytes in the normal ALD muscle. These data suggest that there is an exclusive cellular distribution of myosin heavy chains associated with SM-1 and SM-2 proteins. Immunofluorescent analysis of hypertrophied muscle showed the anti-SM-2-specific antibody reacting with all myocytes, whereas the anti-SM-1-specific antibody reacted with none. This is consistent with the elimination of the SM-1 isoform in hypertrophied muscles.
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:

Jordan, T., Jiang, H., Li, H., DiMario, J. X. (2004). Inhibition of ryanodine receptor 1 in fast skeletal muscle fibers induces a fast-to-slow muscle fiber type transition. J. Cell Sci. 117: 6175-6183 [Abstract] [Full Text]
Momken, I., Lechene, P., Ventura-Clapier, R., Veksler, V. (2004). Voluntary physical activity alterations in endothelial nitric oxide synthase knockout mice. Am. J. Physiol. Heart Circ. Physiol. 287: H914-H920 [Abstract] [Full Text]
Sacks, L. D., Cann, G. M., Nikovits, W. Jr, Conlon, S., Espinoza, N. R., Stockdale, F. E. (2003). Regulation of myosin expression during myotome formation. Development 130: 3391-3402 [Abstract] [Full Text]
Sciote, J. J., Morris, T. J. (2000). Skeletal Muscle Function and Fibre Types: the Relationship Between Occlusal Function and the Phenotype of Jaw-closing Muscles in Human. J. Orthod. 27: 15-30 [Abstract] [Full Text]
Nikovits, W. Jr., Wang, G. F., Feldman, J. L., Miller, J. B., Wade, R., Nelson, L., Stockdale, F. E. (1996). Isolation and Characterization of an Avian Slow Myosin Heavy Chain Gene Expressed during Embryonic Skeletal Muscle Fiber Formation. J. Biol. Chem. 271: 17047-17056 [Abstract] [Full Text]