Am J Physiol Cell Physiol AJP: Cell Physiology
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Am J Physiol Cell Physiol 256: C399-C404, 1989;
0363-6143/89 $5.00
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AJP - Cell Physiology, Vol 256, Issue 2 C399-C404, Copyright © 1989 by American Physiological Society

ARTICLES

Molecular characterization of rat skeletal muscle myosin light chain kinase

B. P. Herring, M. H. Nunnally, P. J. Gallagher and J. T. Stull
Department of Physiology and Moss Heart Center, University of Texas, Southwestern Medical Center, Dallas 75235.

A 1.85-kilobase (kb) cDNA has been isolated that encodes the catalytic and calmodulin binding domains of rat skeletal muscle myosin light chain kinase. The cDNA hybridized to a 3.3-kb RNA present in fast- and slow-twitch skeletal muscles. The reported enzymatic activity (3-fold greater in fast- than slow-twitch skeletal muscles) reflects the relative abundance of this RNA in the two types of skeletal muscle. No hybridization of the cDNA was detected to RNA isolated from smooth or nonmuscle tissues. The clone cross hybridized to a 2.2-kb RNA present in cardiac tissue. Ribonuclease protection analysis of skeletal and cardiac muscle RNA revealed major differences in the two hybridizing RNAs. Thus rat skeletal muscle contains a single myosin light chain kinase isoform, which is distinct from the cardiac, smooth, and nonmuscle forms.


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B. P. Herring, S. Dixon, and P. J. Gallagher
Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle
Am J Physiol Cell Physiol, November 1, 2000; 279(5): C1656 - C1664.
[Abstract] [Full Text] [PDF]


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