Open Access
Preparation of monoclonal antibodies against glycoprotein IIIa of human platelets
Author(s) -
MELERO Jose A.,
GONZALEZRODRIGUEZ Jose
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08208.x
Subject(s) - monoclonal antibody , epitope , platelet , agglutination (biology) , antibody , glycoprotein , chemistry , antiserum , platelet membrane glycoprotein , proteolysis , antigen , biochemistry , in vitro , microbiology and biotechnology , biology , immunology , enzyme
Monoclonal antibodies against purified glycoprotein IIIa (GPIIIa) of human platelet membranes have been obtained. These antibodies, except one, are able to bind to intact platelets; the exception is M108/p98 antibody which recognizes a new epitope, unmasked after proteolysis of GPIIIa in vitro. Several antigenic areas can be delineated on the molecule, by testing the ability of different antibodies to compete in their simultaneous binding to GPIIIa. One of the monoclonal antibodies inhibits ADP‐induced platelet aggregation while others do not have an effect or induce agglutination of platelets independent of ADP. Conventional antiserum raised against purified GPIIIa also blocks the aggregation induced by ADP. These results favour the hypothesis that GPIIIa plays a direct role in the mechanism of platelet aggregation.