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- W2020179073 abstract "Platelet aggregation requires cell activation and the binding of fibrinogen to the platelet integrin GP IIb-IIIa. PAC1 is a monoclonal antibody that is specific for GP IIb-IIIa on activated platelets. PAC1 binding to GP IIb-IIIa is very similar to fibrinogen binding. In particular, the binding of both ligands is dependent on a change in the conformation of GP IIb-IIIa during platelet activation, and binding requires divalent cations and is inhibited by RGD-containing peptides. These common binding properties appear to be due to similarities in primary amino acid sequence and, presumably, in three-dimensional structure between a hypervariable region of PAC1 (H-CDR3) and GP IIb-IIIa recognition sites in fibrinogen. This conclusion is supported by the finding that certain anti-PAC1 monoclonal antibodies that recognize H-CDR3 also inhibit the binding of fibrinogen to platelet GP IIb-IIIa. Furthermore, these antibodies bind at or near three distinct regions in fibrinogen previously implicated as GP IIb-IIIa recognition sites (Aα95−98, or RGDF; Aα572−575, or RGDS; and γ400−411, or HHLGGAKQAGDV). These findings imply that the γ400−411 region of the fibrinogen molecule may assume a conformation similar to that of one or both AαRGD regions of the molecule. Thus, the PAC1-anti-PAC1 antibody system has proven in formative in defining the interactions between fibrinogen and an integrin receptor on platelets." @default.
- W2020179073 created "2016-06-24" @default.
- W2020179073 creator A5060459487 @default.
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- W2020179073 date "1992-08-01" @default.
- W2020179073 modified "2023-09-26" @default.
- W2020179073 title "Use of monoclonal antibodies to study the interaction between an integrin adhesion receptor, GP IIb-IIIa, and its physiological ligand, fibrinogen" @default.
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- W2020179073 doi "https://doi.org/10.1016/s1058-6687(05)80028-2" @default.
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