Myosin light chain kinase in endothelium: molecular cloning and regulation.
作者： J G Garcia , V Lazar , L I Gilbert-McClain , P J Gallagher , A D Verin
DOI: 10.1165/AJRCMB.16.5.9160829
关键词:
摘要: The phosphorylation of myosin light chains by chain kinase (MLCK) is a key event in agonist-mediated endothelial cell gap formation and vascular permeability. We now report the cloning expression nonmuscle MLCK isoform cultured endothelium. Screening human cDNA library identified 7.7 kb with substantial (> 95%) homology to coding region rabbit bovine smooth muscle (SM) (amino acid #923-1913) as well reported avian (65-70% homology). Sequence analysis also identified, however, 5' stretch novel sequence acids #1-922) which not contained open reading frame mammalian SM MLCK, only 58% homologous fibroblast sequence. Immunoprecipitation NH2-specific antisera revealed 214 kD high molecular weight endothelium exhibits MLC properties. Amino consensus sequences for variety protein kinases including highly conserved potential sites cAMP-dependent A (PKA) CaM-binding region. Augmentation intracellular cAMP levels markedly enhanced (2.5-fold increase) reduced activity immunoprecipitates (4-fold decrease). These data suggest potentially mechanisms contraction barrier regulation.
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