Characterization of an antiglycoprotein Ib monoclonal antibody that specifically inhibits platelet-thrombin interaction
| Autor: | Michael C. Berndt, William J. Booth, Vadim S. Repin, Tatjana N. Vlasik, Mazurov Av, Dimitry V. Vinogradov |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Blood Platelets
Platelet Aggregation Receptors Cell Surface Platelet Membrane Glycoproteins Platelet membrane glycoprotein Epitopes Immunoglobulin Fab Fragments Mice chemistry.chemical_compound Thrombin Von Willebrand factor hemic and lymphatic diseases von Willebrand Factor medicine Animals Humans Platelet Binding site Ristocetin Mice Inbred BALB C Binding Sites biology Antibodies Monoclonal Hematology Molecular biology Adenosine Diphosphate chemistry Biochemistry Glycoprotein Ib biology.protein Platelet aggregation inhibitor Receptors Thrombin Collagen Platelet Aggregation Inhibitors circulatory and respiratory physiology medicine.drug |
| Zdroj: | Thrombosis Research. 62:673-684 |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/0049-3848(91)90371-3 |
| Popis: | Platelet glycoprotein Ib (GPIb) acts as a high-affinity thrombin binding site and as a receptor for von Willebrand Factor (vWF). A new anti-GPIb monoclonal antibody (mAB) VM16d was produced that specifically inhibited platelet-thrombin but not platelet-vWF interaction. The epitope for VM16d was located within the 45 kDa N-terminal region of the alpha-chain of GPIb. VM16d inhibited platelet aggregation induced by low dose thrombin (0.05 U/ml) but did not affect platelet aggregation induced by ristocetin, bovine vWF, ADP or collagen. The same inhibitory effects on thrombin-induced platelet aggregation were observed with the whole IgG molecule of VM16d and its F(ab')2 and F(ab') fragments. VM16d also inhibited 14C-serotonin secretion induced by low dose thrombin and binding of 125I-thrombin but not ristocetin-dependent binding of 125I-vWF to platelets. These data indicate that the high-affinity thrombin binding site is located on the N-terminal 45 kDa domain of GPIb and that it is topographically separated from the vWF binding site. |
| Databáze: | OpenAIRE |
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