Wijetunge S, Hughes A D
Department of Clinical Pharmacology, St. Mary's Hospital Medical School, Imperial College of Science Technology & Medicine, London, England.
Biochem Biophys Res Commun. 1995 Dec 26;217(3):1039-44. doi: 10.1006/bbrc.1995.2874.
Intracellular application of pp60c-src, a nonreceptor tyrosine kinase present in large amounts in smooth muscle cells increased voltage-operated calcium channel currents in rabbit ear artery cells. Intracellular peptide-A, an inhibitor of pp60c-src, reduced calcium channel currents and abolished the action of pp60c-src. Selective tyrosine kinase inhibitors, tyrphostin-23 and genistein also abolished the effect of pp60c-src, but inhibition of protein kinase C did not prevent the action of pp60c-src. These results suggest that endogenous pp60c-src modulates voltage-operated calcium channels by a mechanism dependent on tyrosine phosphorylation but not involving activation of protein kinase C.
在平滑肌细胞中大量存在的非受体酪氨酸激酶pp60c-src在细胞内的应用增加了兔耳动脉细胞中的电压门控钙通道电流。细胞内肽A是pp60c-src的一种抑制剂,它可降低钙通道电流并消除pp60c-src的作用。选择性酪氨酸激酶抑制剂曲磷胺-23和染料木黄酮也消除了pp60c-src的作用,但抑制蛋白激酶C并不能阻止pp60c-src的作用。这些结果表明,内源性pp60c-src通过一种依赖酪氨酸磷酸化但不涉及蛋白激酶C激活的机制来调节电压门控钙通道。