Studies on the interaction of platelet glycoprotein IIb-IIIa and glycoprotein IV with fibrinogen and thrombospondin: A new immunochemical approach
| Autor: | Philippe Beiso, Dominique Fournier, Dominique Pidard, Chantal Legrand, Véronique Dubernard |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.drug_class
Molecular Sequence Data Biophysics Platelet Membrane Glycoproteins Fibrinogen Platelet membrane glycoprotein Monoclonal antibody Biochemistry medicine Humans Amino Acid Sequence Immunoelectrophoresis Molecular Biology Immunosorbent Techniques chemistry.chemical_classification Membrane Glycoproteins biology Ligand binding assay Fibrinogen binding Molecular biology chemistry Polyclonal antibodies biology.protein Autoradiography Thrombospondins Glycoprotein Glycoprotein IIb/IIIa Immunoelectrophoresis Two-Dimensional medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1033:7-12 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/0304-4165(90)90186-z |
| Popis: | We have designed a new binding assay based on crossed immunoelectrophoresis that allowed us to test for the relative capacities of platelet membrane glycoprotein IIb-IIIa (GP IIb-IIIa), and glycoprotein IV (GP IV) to bind purified Arg-Gly-Asp (RGD)-containing adhesive proteins. Preformed immune complexes were made by reacting a platelet lysate with murine monoclonal antibodies to GP IV (OKM5 and FA6-152) or to GP IIb-IIIa (AP-2). Upon two-dimensional electrophoretic separation in agarose gels and immunoprecipitation by a polyclonal antibody to mouse IgG, the immobilized complexes containing the desired antigen were further probed with purified 125I-labeled TSP or fibrinogen. Under these conditions, immobilized GP IV was found to specifically bind TSP, whereas it was unreactive with fibrinogen. By contrast, immobilized GP IIb-IIIa demonstrated fibrinogen binding capacity but did not demonstrate any reactivity toward TSP. These observations suggest that the overall structure of the adhesive protein may determine the accessibility of the RGD sequence to its binding site on GP IIb-IIIa. |
| Databáze: | OpenAIRE |
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