Studies on the binding of proteins to the human platelet surface: relation to platelet activation.
Several antibody fractions and sera from patients with rheumatoid arthritis, systemic lupus erythematosus and chronic idiopathic thrombocytopenic purpura were examined for their ability to bind to normal platelets using immunofluorescent staining techniques. Platelet aggregometry was used to study the activating capacity of the samples. Both C1q, C1s, C1 inactivator, fibrinogen, factor VIII-related antigen, alpha 1-acid glycoprotein, alpha 1-antitrypsin, beta 2-microglobulin and isoantigens A and B, as well as fibronectin and plasminogen were found on the platelet surface. Only antibodies to C1q, C1s and beta 2-microglobulin were able to induce platelet aggregation. Sera containing immune complexes or platelet autoantibodies revealed positive surface staining for IgG, or for IgG and IgM. There sera also induced aggregation of platelets. Sera not containing immune complexes or autoantibodies gave negative staining and aggregation results. Thus, only some of the ligand receptor interactions were able to induce platelet aggregation.
D000906:Antibodies; D000936:Antigen-Antibody Complex; D001323:Autoantibodies; D001792:Blood Platelets / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D006801:Humans; D007106:Immune Sera; D007136:Immunoglobulins / Q000378:metabolism; D007700:Kinetics; D010974:Platelet Aggregation
D000906:Antibodies; D000936:Antigen-Antibody Complex; D001323:Autoantibodies; D001798:Blood Proteins; D007106:Immune Sera; D007136:Immunoglobulins