Platelet Adenylate Cyclase and Phospholipase C Are Affected Differentially by ADP-ribosylation. Effects on Thrombin-mediated Responses

Overview

Journal Biochem J

Specialty Biochemistry

Date 1988 May 15

PMID 3138970

Citations 7

Authors

H S Banga

R K Walker

L K Winberry

S E Rittenhouse

Affiliations

Soon will be listed here.

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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