Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells

Patricia Gallagher, J. G N Garcia, B. Herring

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

A novel, 208-kDa myosin light chain kinase (MLCK) distinct from smooth muscle and non-muscle MLCK has been identified by cross-reaction to two antibodies raised against smooth muscle MLCK. Additional antibodies directed against the amino and carboxyl termini of the smooth muscle MLCK do not react with the 208-kDa MLCK, suggesting these regions are distinct. 208-kDa MLCK phosphorylates 20-kDa myosin light chains in a Ca2+/calmodulin-dependent manner, consistent with it being a member of the MLCK family. Expression of 208-kDa MLCK and smooth muscle MLCK appears to be inversely regulated, with 208-kDa MLCK being most abundant during early development and declining at birth. In contrast, expression of smooth muscle MLCK is relatively low early during development and increases to become the predominant MLCK detected in all adult smooth and non-muscle tissues. The developmental expression pattern of the 208-kDa MLCK suggests this form be named, embryonic MLCK.

Original languageEnglish
Pages (from-to)29090-29095
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number49
DOIs
StatePublished - 1995

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Myosin-Light-Chain Kinase
Cultured Cells
Cells
Tissue
Smooth Muscle Myosins
Smooth Muscle
Myosin Light Chains
Antibodies
Cross Reactions
Calmodulin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. / Gallagher, Patricia; Garcia, J. G N; Herring, B.

In: Journal of Biological Chemistry, Vol. 270, No. 49, 1995, p. 29090-29095.

Research output: Contribution to journalArticle

Gallagher, Patricia ; Garcia, J. G N ; Herring, B. / Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 49. pp. 29090-29095.
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