Faculty Collaboration Database

Effect of active site-modified thrombin on the hydrolysis of platelet-associated glycoprotein V by native thrombin. Blood 1985 Mar;65(3):578-83

Date

03/01/1985

Pubmed ID

3155976

Scopus ID

2-s2.0-0021988668 (requires institutional sign-in at Scopus site)   13 Citations

Abstract

To determine the relationship between equilibrium binding of thrombin to sites on the platelet surface and the cleavage of membrane glycoprotein V (GPV) by thrombin, we examined the effect of active site-modified thrombin (1-chloro-3-tosylamido-7-amino-L-2-heptanone thrombin toslysCH2-thrombin) on the binding of native thrombin to platelets and on the hydrolysis of GPV by native thrombin. ToslysCH2-thrombin inhibited binding of native thrombin to high affinity sites on the platelet surface. In contrast, hydrolysis of GPV by native thrombin, even at threshold thrombin concentrations, was not inhibited by pretreatment with toslysCH2-thrombin at concentrations up to 210 nmol/L. ToslysCH2-thrombin also had no appreciable effect on platelet aggregation or release of 14C-serotonin induced by native thrombin. Because toslysCH2-thrombin does not inhibit platelet release, aggregation, or GPV hydrolysis by native thrombin but does inhibit high affinity surface binding by native thrombin, these results indicate that thrombin binding and hydrolysis of GPV are separate and unrelated events.

Author List

Knupp CL, White GC 2nd

Author

Gilbert C. White MD Professor in the Medicine department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Binding Sites
Blood Platelets
Glycoproteins
Humans
Hydrolysis
Membrane Proteins
Platelet Aggregation
Platelet Membrane Glycoproteins
Thrombin
Tosyllysine Chloromethyl Ketone