Inhibition of platelet functions by a monoclonal antibody (LYP20) directed against a granule membrane glycoprotein (GMP-140/PADGEM)
| Autor: | John L. McGregor, Sophie Parmentier, Lawrence L.K. Leung, Lilian McGregor, Bruno Catimel |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Blood Platelets
Rosette Formation Platelet Aggregation Immunology Blotting Western Platelet Membrane Glycoproteins In Vitro Techniques Biochemistry chemistry.chemical_compound Humans Platelet Platelet activation Lymphocyte homing receptor biology Platelet-activating factor Cell adhesion molecule Chemistry Antibodies Monoclonal Cell Biology Hematology Molecular biology Molecular Weight Membrane glycoproteins Kinetics biology.protein Electrophoresis Polyacrylamide Gel Selectin Platelet factor 4 |
| Zdroj: | Blood. 77(8) |
| ISSN: | 0006-4971 |
| Popis: | Granule membrane protein (GMP-140), also known as platelet activation- dependent granule-external membrane (PAD-GEM) is an integral membrane glycoprotein that is expressed on the platelet surface following degranulation. GMP-140, also expressed by endothelial cells, is part of a new family of cell adhesion molecules (selectins) related to the endothelial leukocyte adhesion molecule (ELAM-1) and to the lymphocyte homing receptors in humans (Leu-8/TQ1) and in mouse (gp90MEL-14). The role of GMP-140 in platelet functions remains to be elucidated. In this study, a monoclonal antibody, LYP20, was raised against GMP-140. LYP20, directed against a disulphide bridge-dependent epitope, significantly binds to thrombin-stimulated platelets (12,200 +/- 1,184 bound molecules/platelet, kd = 5.0 +/- 0.61 nmol/L) compared with controls (2,400 +/- 266 molecules/platelet, kd = 2.3 +/- 0.54 nmol/L) and inhibits collagen or thrombin-induced aggregation of washed platelets or platelets in platelet-rich plasma. In addition, LYP20 inhibits rosetting of thrombin-activated platelets to U937 cells. These results strongly suggest that GMP-140 plays an important role in platelet aggregation and platelet interaction with other blood cells. |
| Databáze: | OpenAIRE |
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