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. 1988 May 15;252(1):297–300. doi: 10.1042/bj2520297

Platelet adenylate cyclase and phospholipase C are affected differentially by ADP-ribosylation. Effects on thrombin-mediated responses.

H S Banga 1, R K Walker 1, L K Winberry 1, S E Rittenhouse 1
PMCID: PMC1149138  PMID: 3138970

Abstract

Thrombin stimulates phospholipase C and inhibits adenylate cyclase in human platelets. We have studied the effect of purified S1 monomer, the ADP-ribosylating subunit of pertussis toxin, on these receptor-coupled G-protein-dependent activities. ADP-ribosylation of a 41 kDa protein is associated with a marked decrease in the ability of thrombin to inhibit cyclic AMP formation, but has little effect on phospholipase C. Therefore adenylate cyclase and phospholipase C appear to be modulated by different G-proteins.

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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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