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1990/09/28
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Modulation of smooth muscle calponin by protein kinase C and calmodulin.

Naka M, Kureishi Y, Muroga Y, Takahashi K, Ito M, Tanaka T.
Biochem Biophys Res Commun. 1990 Sep 28;171(3):933-7.

Abstract

When smooth muscle calponin was incubated with protein kinase C, 1 mole of phosphate was incorporated per mole of calponin. The apparent Km value for calponin of the protein kinase was about 0.4 microM. The phosphorylation of calponin by protein kinase C was inhibited markedly by calmodulin in a calcium-dependent manner. Kinetic analysis of calmodulin-induced inhibition of calponin phosphorylation by protein kinase C revealed that calmodulin inhibited the phosphorylation in a noncompetitive fashion with calponin and the determined Ki value was 0.4 microM. These results suggest that interaction of calmodulin with calponin may play a regulatory role in the phosphorylation by protein kinase C and smooth muscle contraction.

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