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The Effects of Thrombin on Adenyl Cyclase Activity and a Membrane Protein from Human Platelets
G. N. Brodie, … , Lewis R. Chase, Philip W. Majerus
G. N. Brodie, … , Lewis R. Chase, Philip W. Majerus
Published January 1, 1972
Citation Information: J Clin Invest. 1972;51(1):81-88. https://doi.org/10.1172/JCI106800.
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Research Article

The Effects of Thrombin on Adenyl Cyclase Activity and a Membrane Protein from Human Platelets

Abstract

Washed human platelets were incubated with 0.1-1.0 U/ml human thrombin and the effects on adenyl cyclase activity and on a platelet membrane protein (designated thrombin-sensitive protein) were studied. Adenyl cyclase activity was decreased 70-90% when intact platelets were incubated with thrombin. The T½ for loss of adenyl cyclase activity was less than 15 sec at 1 U/ml thrombin. There was no decrease of adenyl cyclase activity when sonicated platelets or isolated membranes were incubated with these concentrations of thrombin. Loss of adenyl cyclase activity was relatively specific since the activities of other platelet membrane enzymes were unaffected by thrombin. Prior incubation of platelets with dibutyryl cyclic adenosine monophosphate (AMP), prostaglandin E1, or theophylline protected adenyl cyclase from inhibition by thrombin.

Authors

G. N. Brodie, Nancy Lewis Baenziger, Lewis R. Chase, Philip W. Majerus

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