Journal article

Distinct roles of ligand affinity and cytoskeletal anchorage in alpha(IIb)beta(3) (GP IIb/IIIa)-mediated cell aggregation and adhesion

K Peter, I Ahrens, M Schwarz, C Bode, J Ylanne

PLATELETS | TAYLOR & FRANCIS INC | Published : 2004

Abstract

Platelet integrin alphaIIbbeta3 (GP IIb/IIla) is functionally modulated by changes in ligand affinity or in cytoskeletal anchorage. CHO cells transfected with wild-type/mutated alphaIIbbeta3 allow the dissection of the relative contributions of the two regulatory mechanisms in alphaIIbbeta3-mediated adhesion and aggregation. Mutations included a truncation of the cytoplasmic domain of the beta-subunit, resulting in a loss of cytoskeletal anchorage of alphaIIbbeta3, and a VGFFK-deletion of the alpha-subunit, resulting in a permanent high affinity state. alphaIIbbeta3-mediated cell aggregation is dependent on the high affinity state but only partially on the cytoskeletal anchorage of alphaIIbb..

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