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Title: The biochemical basis of the regulation of smooth-muscle contraction. Author: Allen BG, Walsh MP. Journal: Trends Biochem Sci; 1994 Sep; 19(9):362-8. PubMed ID: 7985229. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]