| Autor: |
Bennett, Joel S., Catella-Lawson, Francesca, Rut, Andrew R., Vilaire, Gaston, Qi, Weiwei, Kapoor, Shiv C., Murphy, Scott, FitzGerald, Garret A. |
| Zdroj: |
Blood; May 2001, Vol. 97 Issue: 10 p3093-3099, 7p |
| Abstrakt: |
The polymorphism responsible for the PlA2alloantigen on the β3-component of β3-containing integrins is reported to be a risk factor for coronary thrombosis. This study examined the effect of PlA2on the function of β3-integrins using platelets from subjects homozygous and heterozygous for PlA1and PlA2. There was overlap in the distribution of the dissociation constant (Kd) and maximum fibrinogen binding (Bmax) values for fibrinogen binding to αIIbβ3on platelets from PlA1and PlA2homozygotes and PlA1/PlA2heterozygotes. However, whereas there was no statistical difference in these values for the PlA1homozygotes and PlA2heterozygotes, the Kdfor the PlA2homozygotes was significantly lower than that for the PlA1/PlA2heterozygotes, but was not statistically different from that for the PlA1homozygotes. No differences were detected in ADP sensitivity between platelets from PlA1homozygotes and PlA1/PlA2heterozygotes, in the IC50for RGDS inhibition of fibrinogen binding to αIIbβ3, in the αvβ3-mediated adhesion of platelets to osteopontin and vitronectin, and in the phorbol ester-stimulated adhesion to fibrinogen of B lymphocytes expressing αIIbβ3containing either the PlA1or the PlA2polymorphism. Finally, no differential effects of PlA2on turbidometric platelet aggregation, platelet secretion, or platelet thrombus formation were found as measured in the PFA-100. Because no differences were detected in the ability of β3-integrins to interact with ligands based on the presence or absence of the PlA2polymorphism, the results suggest that factors unrelated to β3-integrin function may account for the reported association of the PlA2allele with coronary thrombosis. |
| Databáze: |
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