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Modulation of mitogenic activity and cellular binding of basic fibroblast growth factor by basic proteins
Author(s) -
Dauchel M. C.,
Courty J.,
Mereau A.,
Barritault D.
Publication year - 1989
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240390407
Subject(s) - basic fibroblast growth factor , protamine , polylysine , heparin , fibroblast , cell surface receptor , microbiology and biotechnology , fibroblast growth factor , biochemistry , thrombin , growth factor , chemistry , biology , receptor , in vitro , immunology , platelet
Polycationic molecules were studied either for their ability to displace the binding of basic fibroblast growth factor (bFGF) to high‐ and low‐affinity membrane interaction sites and/or to modulate bFGF‐induced proliferation of fibroblasts. Heparin‐binding polypeptides, such as polylysine, protamine, histones, and thrombin‐displaced [ 125 I]bFGF bound to bovine brain membrane receptors. The most displacing polypeptides were those with the strongest affinity to heparin. Two of these polypeptides, protamine and polylysine, inhibited (at 5 μM) by more than 90% the mitogenic effect induced by bFGF on Chinese hamster lung fibroblast cells (CCL39). At the same dose, no effect was observed with basic proteins that do not bind to heparin, such as cytochrome C and lysozyme. An interesting observation was that protamine at 1 μM potentiated by 1.5‐fold the mitogenic activity of bFGF, while it acted as an inhibitor at higher concentration.