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

First Author  Gallagher PJ Year  1995
Journal  J Biol Chem Volume  270
Issue  49 Pages  29090-5
PubMed ID  7493932 Mgi Jnum  J:30019
Mgi Id  MGI:77541 Doi  10.1074/jbc.270.49.29090
Citation  Gallagher PJ, et al. (1995) Expression of a novel myosin light chain kinase in embryonic tissues and cultured cells. J Biol Chem 270(49):29090-5
abstractText  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.
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