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Antibodies against platelet membrane glycoproteins
Author(s) -
Jenkins C. S. P.,
Clemetson K. J.,
AliBriggs Elizabeth F.
Publication year - 1983
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.1365-2141.1983.tb02051.x
Subject(s) - chemistry , glycoprotein , platelet membrane glycoprotein , platelet , glycoprotein ib , thrombin , platelet glycoprotein gpib ix complex , ristocetin , receptor , antibody , biochemistry , microbiology and biotechnology , platelet aggregation , medicine , immunology , biology
S ummary . Glycocalicin has been proposed as the common platelet receptor for both ristocetin‐human VIIIR:WF and thrombin‐induced platelet aggregation. Platelets which have lost glycocalicin do not respond to either ristocetin‐human VIIIR:WF or bovine VIIIR:WF. Using antibodies to the platelet membrane glycoproteins la and lb, lib and Ilia, and glycocalicin we show that the Fab'fragments of anti‐glycoproteins la and lb and anti‐glycocalicin IgG totally inhibited bovine VIIIR:WF‐induced platelet aggregation, while those from anti‐glycoproteins lib and Ilia IgG were without effect. Thrombin‐induced platelet aggregation was strongly inhibited by the Fab'fragments of anti‐glycoproteins la and lb IgG and anti‐glycocalicin IgG, indicating that these glycoproteins play a major role in thrombin‐platelet interaction. Fab'fragments of antiglycoproteins lib and Ilia IgG inhibited thrombin‐induced platelet aggregation to a lesser extent implying that these glycoproteins are also somehow involved in the platelet response to thrombin perhaps as fibrinogen receptors. The data presented here give further support to the proposal that ristocetin‐human VIIIR:WF and bovine VIIIR:WF share a common receptor on the platelet surface and indicate that this structure plays an important role in thrombin‐induced platelet responses.