Inhibition of platelet aggregation with monoclonal antibodies to the glycoprotein IIb-IIIa complex
Byzova, T.V.; Vlasik, T.N.; Mazurov, A.V.
Biulleten' Eksperimental'noi Biologii i Meditsiny 118(10): 402-405
1994
ISSN/ISBN: 0365-9615 PMID: 7865820 Document Number: 423483
Monoclonal antibodies CRC64 to calcium-dependent glycoprotein complex IIb-IIIa from murine platelet membranes were obtained. The antibodies were capable of inhibiting fibrinogen-dependent platelet aggregation. The activity of CRC64 is directed at epitope formed by the glycoprotein complex. CRC64 does not interact with individual proteins after platelet treatment with EDTA. Complete, reproduced blockage of ADP-induced platelet aggregation was observed when monoclonal antibody concentration was 3 microgram/ml. When a stronger inhibitor thrombin was used, platelet aggregation inhibition took place in the concentration of 5 microgram/ml. F(ab')-2-fragments were also able to fully inhibit platelet aggregation in concentrations lower than those of the native monoclonal antibodies.