Counteraction of calcium-activated, phospholipid-dependent protein kinase activation by adenosine 3′,5′-monophosphate and guanosine 3′,5′-monophosphate in platelets

Yoshimi Takai, Kozo Kaibuchi, Kimihiko Sano, Yasutorni Nishizuka

Research output: Contribution to journalArticlepeer-review

66 Citations (Scopus)

Abstract

In intact human platelets activated by thrombin, diacylglycerol is produced with the concomitant disappearance of phosphatidylinositol (PI). This reaction is associated with phosphorylation of a protein having a molecular weight of about 40,000 (40 K protein) and serotonin release. All the reactions are inhibited in a parallel manner by incubation of platelets with either dibutyryl cyclic AMP or 8-bromocyclic GMP, prior to the stimulation by thrombin. The inhibition of these reactions is inversely related to phosphorylation of another group of platelet proteins. Since Ca2+-activated, phospholipid-dependent protein kinase (C-Kinase) is activated by diacylglycerol and is responsible for 40 K protein phosphorylation (Kawahara, Y., Takai, Y., Minakuchi, R., Sano, K., & Nishizuka, Y. (1980) Biochem. Biophys. Res. Commun. 97, 309-317), the results suggest that in platelets both cyclic AMP and cyclic GMP may serve as inhibitors of C-Kinase by counteracting the receptor-linked PI breakdown probably through the actions of cyclic nucleotide-dependent protein kinases.

Original languageEnglish
Pages (from-to)403-406
Number of pages4
JournalJournal of Biochemistry
Volume91
Issue number1
DOIs
Publication statusPublished - 01-1982
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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