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. 1985 May;75(5):1600–1607. doi: 10.1172/JCI111866

(-)-Adrenaline-induced, calcium-dependent phosphorylation of proteins in human platelets.

L H Block, H Jaksche, P Erne, P Bolli, F R Bühler
PMCID: PMC425501  PMID: 2860127

Abstract

In human platelets, adrenaline stimulated, approximately four-fold, as compared with controls, the phosphorylation of primarily two proteins of apparent molecular weights of 20,000 and 40,000, respectively. Maximum phosphorylation occurred after incubation for 1 min and was inhibited by the addition of either yohimbine, prostaglandin E1, or EGTA. Phosphorylation of the two proteins was accompanied by diacylglycerol formation. The (-)-adrenaline-induced phosphorylation of proteins corresponds to the activation of a calcium-dependent protein kinase partially purified by DEAE-cellulose and Sephadex G150 column chromatography. The enzymatic activity was modulated by addition of (-)-adrenaline and CaCl2, by diolein, and in the presence of membranes or phosphatidylinositol but not phosphatidylethanolamine and phosphatidylcholine. A phospholipid-dependent reaction appears to be involved in the molecular mechanism of action of adrenaline.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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