Peptide LSARLAF activates αIIIbβ3 on resting platelets and causes resting platelet aggregate formation without platelet shape change

被引：14

作者：

Derrick, JM ^{[1
]}

Loudon, RG ^{[1
]}

Gartner, TK ^{[1
]}

机构：

[1] Univ Memphis, Dept Microbiol & Mol Cell Sci, Memphis, TN 38152 USA

来源：

THROMBOSIS RESEARCH | 1998年 / 89卷 / 01期

关键词：

platelet agonist; GPIIb IIIa; alpha(IIb)beta(3); fibrinogen receptor;

D O I：

10.1016/S0049-3848(97)00289-2

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Adhesion of resting platelets to fibrinogen was enhanced by a peptide which was designed to bind near the presumptive fibrinogen gamma-chain binding site of the alpha subunit of the integrin alpha(IIb)beta(3). This peptide, but not a scrambled control peptide, induced adhesion of resting platelets to fibronectin, vitronectin, von Willebrand factor, and monovalent (lacks one functional gamma-chain) fibrinogen. Resting platelets not treated with the agonist peptide did not adhere to these ligands. Agonist peptide induced adhesion of resting platelets to Fg was not secretion dependent and was inhibited by the monoclonal antibody 7E3. The agonist peptide caused aggregation of resting platelets on resting platelets adherent to immobilized Fg without causing platelet shape change. Therefore, the agonist peptide may activate alpha(IIb)beta(3) by directly inducing a conformation change in the receptor on resting platelets. (C) 1998 Elsevier Science Ltd.

引用

页码：31 / 40

页数：10

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