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Thromb Haemost 1985; 53(03): 360-365
DOI: 10.1055/s-0038-1661315
Original Article
Schattauer GmbH Stuttgart

Studies on the Binding of Proteins to the Human Platelet Surface: Relation to Platelet Activation

Gerhard K M Endresen
1   The Institute for Surgical Research, Rikshospitalet, National Hospital, Oslo, Norway
,
Øystein Førre
2   Oslo Sanitetsforening Rheumatism Hospital, Oslo, Norway
› Author Affiliations
Further Information

Publication History

Received 29 October 1984

Accepted 14 March 1985

Publication Date:
18 July 2018 (online)

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Summary

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, alpha1-acid glycoprotein, alpha1-antitrypsin, beta2-micro- globulin and isoantigens A and B, as well as fibronectin and plasminogen were found on the platelet surface. Only antibodies to C1q, C1s and beta2-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. These 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.

Keywords

Human platelets - Protein binding - Immune complexes - Platelet autoantibodies - Aggregation - Immunofluorescence - Autoimmune diseases
 

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