Faculty Collaboration Database

Glycoprotein V hydrolysis by thrombin. Lack of correlation with secretion. Thromb Res 1985 Jun 15;38(6):641-8

Date

06/15/1985

Pubmed ID

3161210

DOI

10.1016/0049-3848(85)90207-5

Scopus ID

2-s2.0-0022254372 (requires institutional sign-in at Scopus site)   9 Citations

Abstract

Platelet membrane glycoprotein V (GPV) was hydrolyzed during thrombin-induced platelet aggregation releasing a fragment GPVfl into the supernatant. Hydrolysis of GPV required catalytically active thrombin and was diminished by chemical modification of the fibrinogen binding site of thrombin. Half-maximal liberation of GPVfl occurred at a 10-fold higher concentration of thrombin than was required for half-maximal release. Time course studies at several thrombin concentrations showed disparate release of GPVfl and thrombospondin. These results emphasize the complexity of the initial events in thrombin-induced platelet activation.

Author List

White GC 2nd, Knupp CL

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
Chymotrypsin
Cytoplasmic Granules
Fibrinogen
Glycoproteins
Humans
Hydrolysis
Membrane Proteins
Platelet Membrane Glycoproteins
Thrombin
Thrombospondins