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Evidence for two functionally different fibrinogen receptors on hemopoietic cells: The glycoprotein IIb–IIIa and the mitogenic fibrinogen receptor
Author(s) -
Levesque JeanPierre,
Hatzfeld Antoinette,
HudryClergeon Gilbert,
Wilner George D.,
Hatzfeld Jacques
Publication year - 1987
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041320215
Subject(s) - fibrinogen , receptor , plasmin , glycoprotein , microbiology and biotechnology , biology , platelet , protease activated receptor , monoclonal antibody , cell surface receptor , chemistry , biochemistry , antibody , immunology , thrombin , enzyme
We have previously established that the mitogenic effect of fibrinogen on hemopoietic cell lines Raji and JM is mediated via a specific receptor (Levesque, J.‐P. et al.: Proc. Natl. Acad. Sci. USA 83: 6494–6498, 1986). In this study, we have further characterized the fibrinogen domain involved in the binding to the mitogenic receptor. This binding was not inhibited either by a monoclonal antibody against the C‐terminal sequence of the fibrinogen γchains or by synthetic peptides containing the Arg‐Gly‐Asp sequence. Such inhibition is specific of the platelet fibrinogen receptor, the glycoprotein IIb‐IIIa complex. Fragments containing the fibrinogen D domain were the only plasmin degradation products of fibrinogen which mitogenic. These fragments acted via direct binding on the mitogenic receptor with a Kd of 2.24 × 10 −6 M. This value was similar to the K 1 value of unlabeled fragments D (2.47 × 10 −6 M). Our results suggest the presence of two different functional types of fibrinogen receptors: the glycoprotein IIb–IIIa receptor responsible both for platelet aggregation and leukocyte adhesion and killing, and the mitogenic receptor involved in proliferation control of hemopoietic cells.