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

B. Paul Herring, Shelley Dixon, Patricia J. Gallagher

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)C1656-C1664
JournalAmerican Journal of Physiology - Cell Physiology
Volume279
Issue number5 48-5
StatePublished - Dec 7 2000

Keywords

  • AT1 cells
  • CC cells
  • Differentiation

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology
  • Physiology (medical)

Fingerprint Dive into the research topics of 'Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle'. Together they form a unique fingerprint.

  • Cite this