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Platelet myosin light chain kinase is a calmodulin dependent enzyme which requires calmodulin for its activity and is intimately related to actomyosin contracting system. Platelet actomyosin contraction may cause the release reaction of platelet. N-(6-aminohexyl)-5-chloro-naphthalene sulfonamide (W-7) is one of the calmodulin interacting agents, and selectively inhibits calmodulin activity. Since platelet membrane phospholipases which are responsible for the release of arachidonic acid from membrane phospholipids may also be calmodulin-dependent enzymes, the inhibitory effects of W-7 on platelet function were examined. W-7 in a concentration as low as 10 7#x03BC;M inhibited platelet aggregation and release reaction induced by ADP, collagen, epinephrine, thrombin, arachidonic acid and Ca2+-ionophore A23187. When platelets were preincubated with W-7 before addition of an aggregating agent, the inhibition became more pronounced. In ADP-induced aggregation, only the second phase was inhibited. Arachidonate metabolites (PGG2/H2 and thromboxane A2) failed to induce aggregation and release reaction of platelets preincubated with W-7. Furthermore, release of arachidonic acid from platelet membrane phospholipids induced by A23187 in the presence of indomethacine was inhibited by W-7. W-7 had no effect on glucose metabolism in platelets. The c-AMP levels in platelets were not significantly changed by incubation with W-7. These results suggest that W-7 inhibits directly phospholipase A2 and/or phospholipase C in addition to myosin light chain kinase. These results may in turn indicate that calmodulin is involved in platelet aggregation and release reaction mechanism including membrane phospholipases and the target system of thromboxane A2 (possibly actomyosin contracting system).

Inhibition Of Platelet Aggregation And Release Reaction By A Calmodulin Interacting Agent, N-(6-Aminohexyl)-5-Chloro-1-Naphthalene Sulfonamide