The interaction of thrombospondin with platelet glycoprotein GPIIb-IIIa
نویسندگان
چکیده
منابع مشابه
Interaction of thrombospondin with platelet glycoproteins GPIa-IIa and GPIIb-IIIa.
The interaction of human thrombospondin (TSP) with GPIa-IIa and GPIIb-IIIa was studied. The binding for both proteins became time-independent after 60 min. A 7-fold excess concentration of unlabelled GPIa-IIa added either initially, or after time-dependent binding, resulted in a 50% inhibition of GPIa-IIa bound to TSP. GPIa-IIa and GPIIb-IIIa specifically bound TSP since: (a) the binding of GPI...
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Monitoring platelet GPIIb/IIIa antagonist therapy.
P latelet GP IIb/IIIa receptor antagonist therapy with abciximab (ReoPro), the Fab fragment of a mouse/ human chimeric version of the murine 7E3 antibody, is currently used to prevent ischemic complications of percutaneous coronary interventions in select cases, and the efficacy and safety of abciximab for other related indications are under study. A number of low-molecular-weight GP IIb/IIIa a...
متن کاملPlatelet membrane topography: colocalization of thrombospondin and fibrinogen with the glycoprotein IIb-IIIa complex.
The distribution of platelet thrombospondin (TSP), fibrinogen, and glycoproteins IIb-IIIa (GPIIb-IIIa) and GPIb were studied in resting and activated human platelets using frozen thin-section immunoelectron microscopy. In resting platelets, TSP and fibrinogen were found within alpha granules and not on the platelet surface. In unstimulated platelets, GPIIb-IIIa and GPIb were distributed diffuse...
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AIM To build up the structure of human fibrinogen receptor GPIIb-IIIa, subsequently combined with its antagonist decorsin, and to investigate the interaction between decorsin and its receptor GPIIb-IIIa at the molecular level. METHODS A three-dimensional (3D) molecular model of human fibrinogen receptor GPIIb-IIIa was generated by InsightII, a distance geometry-based homologous modeling packa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)30082-1