Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle

被引:53
作者
Herring, BP [1 ]
Dixon, S [1 ]
Gallagher, PJ [1 ]
机构
[1] Indiana Univ, Sch Med, Dept Physiol & Biophys, Indianapolis, IN 46202 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2000年 / 279卷 / 05期
关键词
AT1; cells; C2C12; differentiation;
D O I
10.1152/ajpcell.2000.279.5.C1656
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The purpose of this study was to characterize myosin light chain kinase (MLCK) expression in cardiac and skeletal muscle. The only classic MLCK detected in cardiac tissue, purified cardiac myocytes, and in a cardiac myocyte cell line (AT1) was identical to the 130-kDa smooth muscle MLCK (smMLCK). A complex pattern of MLCK expression was observed during differentiation of skeletal muscle in which the 220-kDa-long or "nonmuscle" form of MLCK is expressed in undifferentiated myoblasts. Subsequently, during myoblast differentiation, expression of the 220-kDa MLCK declines and expression of this form is replaced by the 130-kDa smMLCK and a skeletal muscle-specific isoform, skMLCK in adult skeletal muscle. These results demonstrate that the skMLCK is the only tissue-specific MLCK, being expressed in adult skeletal muscle but not in cardiac, smooth, or nonmuscle tissues. In contrast, the 130-kDa smMLCK is ubiquitous in all adult tissues, including skeletal and cardiac muscle, demonstrating that, although the 130-kDa smMLCK is expressed at highest levels in smooth muscle tissues, it is not a smooth muscle-specific protein.
引用
收藏
页码:C1656 / C1664
页数:9
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