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Monoclonal Antibody to Human Platelet Glycoprotein I II. EFFECTS ON HUMAN PLATELET FUNCTION
Author(s) -
Ruan C.,
Tobelem G.,
McMichael A. J.,
Drouet L.,
Legrand Y.,
Degos L.,
Kieffer N.,
Lee H.,
Caen J. P.
Publication year - 1981
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1981.tb07259.x
Subject(s) - platelet , chemistry , von willebrand factor , glycoprotein , ristocetin , platelet membrane glycoprotein , monoclonal antibody , platelet adhesiveness , adhesion , thrombin , platelet adhesion , glycoprotein ib , antibody , membrane glycoproteins , microbiology and biotechnology , biochemistry , immunology , platelet aggregation , biology , organic chemistry
S ummary . The effect on platelet function of a monoclonal platelet antibody to platelet membrane glycoprotein I was tested. This antibody, AN51, inhibited ristocetin or bovine factor VIII‐induced aggregation but did not modify ADP, collagen type I or type III, thrombin or arachidonic acid induced aggregations. Furthermore, the adhesion‐aggregation of platelets induced by microfibrils was also inhibited by the antibody. Platelet adhesion to rabbit aorta subendothelium was impaired by the antibody. The persistent adhesion of platelets to collagenase‐treated subendothelium was also inhibited. These findings strongly suggested that platelet membrane glycoprotein I could interact with a non‐collagenic microfibrillar component of subendothelium. The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the presence of the antibody. Platelet membrane glycoprotein I could, thus, be a binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.