[摘要] Phosphorylation of myosin light chain kinase by a Ca2+-dependent protein kinase increases the concentration of Ca2+/calmodulin required for half-maximal activation. The Ca2+ concentrations required for myosin light chain kinase phosphorylation in permeable smooth muscle are similar to those required for myosin light chain phosphorylation. Both GTPγS and carbachol increase the Ca2+ sensitivity of myosin light chain kinase phosphorylation as well as light chain phosphorylation. It is proposed that a similar G-protein mediated mechanism regulates the Ca2+-dependent phosphorylation of these two contractile proteins in smooth muscle.
[发布日期] [发布机构]
[效力级别] [学科分类] 生物化学/生物物理
[关键词] Smooth muscle contraction;Myosin light chain;Myosin light chain kinase;GTPγS;Protein phosphatase;[Ca2*]i;free intracellular Ca2+ concentration;KN-62;1-[N-O-Bis(5-isoquinolinesulfonyl)-N+-methyl-l-tyrosyl]-4-phenylpiperazine;G-protein;guanine nucleotide-binding protein;PSS;physiological salt solution;PAGE;polyacrylamide gel electrophoresis;PMSF;phenylmethylsulfonyl fluoride;EDTA;ethylenediamine-tetraacetic acid;MOPS;3-[N-morpholino]propane-sulfonic acid;EGTA;ethyleneglycol-bis (β-aminoethylether)N;N;N';N';-tetraacetic acid;k cam;concentration of Ca2+/calmodulin required for half-maximal activation;PIPES;piperazine-N;N-bis[2-ethane-sulfonic acid] [时效性]