THE BIOCHEMICAL BASIS OF THE REGULATION OF SMOOTH-MUSCLE CONTRACTION

被引：162

作者：

ALLEN, BG

WALSH, MP

机构：

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1994年 / 19卷 / 09期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0968-0004(94)90112-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The primary signal for smooth-muscle contraction is an increase in sarcoplasmic free Ca2+ concentration ([Ca2+](i)). This triggers activation of calmodulin-dependent myosin light-chain kinase, which catalyses myosin phosphorylation, thereby activating crossbridge cycling and the development of force or contraction of the muscle cell. Restoration of resting [Ca2+](i) deactivates the kinase; myosin is dephosphorylated by myosin light-chain phosphatase and the muscle relaxes. Recent evidence suggests that other signal-transduction pathways can modulate the contractile state of a smooth-muscle cell by affecting specific steps in the myosin phosphorylation-dephosphorylation mechanism.

引用

页码：362 / 368

页数：7

共 33 条

[1]

IDENTIFICATION OF MITOGEN-ACTIVATED PROTEIN-KINASE PHOSPHORYLATION SEQUENCES IN MAMMALIAN H-CALDESMON [J].