The action of PKA on smooth muscle myosin phosphorylation |
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Authors: | Yang Jing Xian Lin Yuan |
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Affiliation: | Department of Pharmacology, Dalian Medical University, 465 Zhongshan Road, Dalian 116027, PR China. xiayang9999@sina.com |
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Abstract: | The aim of the study is to reveal the characterization of PKA acting on myosin. We found: (a) in the absence of Ca(2+)/CaM, PKA slightly phosphorylated MLC(20) and stimulated the Mg(2+)-ATPase activity of myosin, which was strengthened significantly by arachidonic acid (ACAD); (b) Ca(2+)-independent phosphorylation of myosin by PKA was obviously less efficient than both Ca(2+)-dependent and independent phosphorylation of myosin by MLCK; (c) micro-amount of calponin could not increase the precipitation of myosin phosphorylated by PKA, but it increased the precipitation of myosin phosphorylated by MLCK, suggesting the presence of conformational differences between the myosins phosphorylated by PKA and by MLCK. |
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