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Antibodies against Platelet Membrane Glycoproteins II. INFLUENCE ON ADP‐ AND COLLAGEN‐INDUCED PLATELET AGGREGATION, CROSSED IMMUNOELECTROPHORESIS STUDIES AND RELEVANCE TO GLANZMANN'S THROMBASTHENIA
Author(s) -
Jenkins C. S. P.,
AliBriggs ELIZABETH F.,
Clemetson K. J.
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.tb07247.x
Subject(s) - thrombasthenia , platelet , platelet membrane glycoprotein , glanzmann's thrombasthenia , glycoprotein , chemistry , antibody , immunoprecipitation , biochemistry , immunoelectrophoresis , microbiology and biotechnology , immunology , platelet aggregation , medicine , biology , gene
S ummary . In Glanzmann's thrombasthenia glycoproteins IIb and IIIa are missing or strongly reduced and aggregation to ADP, collagen and thrombin is impaired. Antibodies against glycoproteins IIb and IIIa did not entirely induce a thrombasthenia‐like state in normal platelets. However, they did strongly inhibit collagen‐induced aggregation and inhibited the second wave of aggregation induced by ADP. Crossed immunoelectrophoresis studies using Triton X‐100 extracts of whole platelets with these antibodies gave a single immunoprecipitate. This immuno‐precipitate was absent when similar studies were carried out with thrombasthenic platelets. Platelet antibodies gave a number of immunoprecipitates with normal platelets and differences were observed with thrombasthenic platelets, the most notable of which was a marked reduction in one of the major immunoprecipitates. These results provide further evidence that glycoproteins IIb and IIIa are involved in the later stages of platelet aggregation.