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

TitleExpression of a novel myosin light chain kinase in embryonic tissues and cultured cells.
Publication TypeJournal Article
Year of Publication1995
AuthorsGallagher PJ, Garcia JG, Herring BP
JournalJ Biol Chem
Volume270
Issue49
Pagination29090-5
Date Published1995 Dec 08
ISSN Number0021-9258
KeywordsAnimals, Calcium, Cells, Cultured, Embryo, Mammalian, Female, Mice, Molecular Weight, Muscle, Smooth, Myosin-Light-Chain Kinase, Phosphorylation, Pregnancy
Abstract

<p>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.</p>

Alternate JournalJ. Biol. Chem.
PubMed ID7493932
PubMed Central IDPMC2836784
Grant ListR01 HL054118 / HL / NHLBI NIH HHS / United States
R01 HL054118-03 / HL / NHLBI NIH HHS / United States