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Thromb Haemost 1985; 54(03): 603-606
DOI: 10.1055/s-0038-1660079
Original Article
Schattauer GmbH Stuttgart

Studies on Platelets of Patients with Inherited Platelet Disorders Suggest that Collagen-Induced Fibrinogen Binding to Membrane Receptors Requires Secreted ADP but Not Released α-Granule Proteins[*]

Chantal Legrand
The Laboratoire d’Hémostase et de Thrombose Expérimentale, Hôpital Lariboisière, Paris, France
,
Alan T Nurden
The Laboratoire d’Hémostase et de Thrombose Expérimentale, Hôpital Lariboisière, Paris, France
› Author Affiliations
Further Information

Publication History

Received 05 May 1985

Accepted 02 July 1985

Publication Date:
19 July 2018 (online)

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Summary

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 α-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 α-granule release.

Keywords

Platelet aggregation - Fibrinogen - Collagen - Platelet secretion - Inherited platelet disorders

* This work was presented in part at the American Society of Hematology and has been published in abstract form (Blood 64, 248a, 1984).


 

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