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Biochem Biophys Res Commun. 1986 Oct 15;140(1):280-7.

The modulatory role of myosin light chain phosphorylation in human platelet activation.

Erratum in

  • Biochem Biophys Res Commun 1987 Jan 15;142(1):287.

Abstract

Myosin 20 K-Da light chain phosphorylation in human platelets was found to be catalyzed by MLCK in the early phase during collagen activation. The effect of newly synthesized selective inhibitor of MLCK, ML-9, on collagen induced platelet activation was investigated. ML-9 delayed the time course of the myosin 20 K-Da light chain phosphorylation, sequentially led to a delay in aggregation, secretion and phosphorylation of the 40K-Da peptide, in a dose-dependent fashion. It is proposed that the MLCK catalyzed phosphorylation of myosin 20 K-Da light chain may be an initial response and if so may influence the sequent reactions in the activation of platelets with collagen.

PMID:
3778449
DOI:
10.1016/0006-291x(86)91087-9
[Indexed for MEDLINE]

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