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  • Title: Studies on platelets of patients with inherited platelet disorders suggest that collagen-induced fibrinogen binding to membrane receptors requires secreted ADP but not released alpha-granule proteins.
    Author: Legrand C, Nurden AT.
    Journal: Thromb Haemost; 1985 Oct 30; 54(3):603-6. PubMed ID: 3003952.
    Abstract:
    Collagen induces a saturable 125I-fibrinogen binding to normal human platelets. A role for secreted ADP in this process is supported by studies on 2 patients with the Chédiak-Higashi syndrome. Both collagen-induced nucleotide release and 125I-fibrinogen binding were strongly reduced while ADP-induced fibrinogen binding was normal. Platelets from 2 patients with the gray platelet syndrome bound normal amounts of 125I-fibrinogen in the presence of ADP or collagen despite the severe reduction of secretable alpha-granule proteins. Binding did not occur to collagen-stimulated type I thrombasthenic platelets which lacked GPIIb-IIIa complexes but was detected in amounts which correlated with the residual concentrations of GPIIb-IIIa in the platelets of a patient with type II disease. Our results allow us to propose that collagen-induced fibrinogen binding to normal platelets requires the presence of GPIIb-IIIa complexes and secreted ADP but proceeds independently of alpha-granule release.
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