Title : Evidence for two GTPases activated by thrombin in membranes of human platelets.

Pub. Date : 1986 Aug 1

PMID : 3026330






6 Functional Relationships(s)
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1 Thrombin inhibits adenylate cyclase and stimulates GTP hydrolysis by high-affinity GTPase(s) in membranes of human platelets at almost identical concentrations. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens
2 However, stimulation of GTP hydrolysis caused by adrenaline (alpha 2-adrenoceptor agonist) and by thrombin at maximally effective concentrations was partially additive, whereas with regard to adenylate cyclase inhibition no additive response was observed. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens
3 Additionally, the thiol reagent N-ethylmalemide (NEM) at rather low concentrations abolished thrombin- and adrenaline-induced stimulation of GTP hydrolysis was decreased by only 30-40% by treatment of platelet membranes with even high concentrations of NEM. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens
4 The data suggest that thrombin interaction with its receptor sites in platelet membranes leads to stimulation of two GTP-hydrolysing enzymes. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens
5 The other GTP-hydrolysing enzyme activated by thrombin may represent a guanine nucleotide-binding protein apparently involved in the coupling of thrombin receptors to the phosphoinositide phosphodiesterase. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens
6 The other GTP-hydrolysing enzyme activated by thrombin may represent a guanine nucleotide-binding protein apparently involved in the coupling of thrombin receptors to the phosphoinositide phosphodiesterase. Guanosine Triphosphate coagulation factor II, thrombin Homo sapiens