Abstract
Protein phosphorylation may play a critical role in stimuluscoupled secretion of platelets. Some platelet proteins become phosphorylated on exposure to agents such as thrombin and collagen1–5, and the smallest of these phosphoproteins (molecular weight 20,000), has been identified as a light chain of myosin6–8. Phosphorylation of myosin light chain increases the activity of actin-activated myosin ATPase8 and the resultant contraction of the actomyosin presumably mediates the release reaction6,9. Platelet myosin light chain kinase has been identified as a calcium-dependent enzyme requiring calmodulin for its activity10,11. Calmodulin is a Ca2+-binding protein with a molecular weight of ∼18,000 which seems to be involved in a wide variety of cellular processes12. Although a growing body of evidence suggests that non-muscle actomyosin, such as that isolated from platelets, is regulated by Ca2+-calmodulin-dependent light chain phosphorylation, the precise relationship between the phosphorylation and the function of platelets is not clearly established. We now present pharmacological evidence that a calmodulin-mediated system, such as Ca2+-dependent myosin light chain phosphorylation, also plays an important role in the phenomenon of the release reaction. N-(6-aminohexyl)-5-chloro-1-napthalene-sulphonamide (W-7) (refs 13–15) is shown to bind selectively to calmodulin in vitro and inhibit its biological activity.
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Nishikawa, M., Tanaka, T. & Hidaka, H. Ca2+ -calmodulin-dependent phosphorylation and platelet secretion. Nature 287, 863–865 (1980). https://doi.org/10.1038/287863a0
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DOI: https://doi.org/10.1038/287863a0
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