Publications by authors named "Ya A Naimushin"
The ability of different ligands of glycoprotein (GP) IIb-IIIa (alphaIIb/beta3-integrin) to support platelet aggregation stimulated by activating anti-GP IIb-IIIa monoclonal antibody (monoAB) CRC54 has been investigated. Antibody CRC54 stimulated aggregation of washed platelets not only in the presence of fibrinogen, the main GP IIb-IIIa ligand, but also in the presence of von Willebrand factor (vWF). Unlike these ligands, fibronectin failed to support CRC54-induced aggregation.
View Article and Find Full Text PDFIn this study we investigated mechanisms of platelet interaction with von Willebrand factor (vWF) induced by activating anti-glycoprotein (GP)IIb-IIIa antibody CRC54 directed against LIBS (ligand-induced binding site epitope) in GPIIIa. It was demonstrated that aggregation of washed platelets (measured in Born aggregometer) could be stimulated by CRC54 not only in the presence of fibrinogen but vWF as well. The level of aggregation induced in the presence of saturating concentrations of vWF (approximately 80 microg/ml) was even higher than that in the presence of 1 mg/ml of fibrinogen.
View Article and Find Full Text PDFRole of glycoprotein IIb-IIIa (alpha IIb beta 3-integrin) in stimulation of secretion from platelet granules.
Biochemistry (Mosc)
February 2003
Article Synopsis
- The study focused on the role of glycoprotein IIb-IIIa (GP IIb-IIIa) in platelet secretion from dense and alpha-granules.
- Monoclonal antibodies that block GP IIb-IIIa activity significantly inhibited serotonin release upon platelet activation, especially with ADP, while showing varying effects with other activators.
- The findings suggest that the binding of GP IIb-IIIa to fibrinogen is crucial for stimulating granule secretion, but other mechanisms may also be involved, particularly in cases of platelet activation by concanavalin A.