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(Received for publication, April 23, 1996, and in revised form, July 22, 1996)
From the Abteilung für Gastroenterologie und Hepatologie,
Universitätsklinikum Benjamin Franklin, Freie
Universität Berlin, Hindenburgdamm 30, 12200 Berlin, Germany
The biological activities of several growth
factors/cytokines have been shown to be modulated by binding to
molecules of the extracellular matrix. Here, the interactions of PDGF
(isoforms AA, BB, and AB), a potent mitogen for mesenchymal cells, with
collagens were investigated. All radiolabeled PDGF isoforms
specifically interacted with type I, II, III, IV, V, and VI collagens
(preferential binding to types III, I, VI, and IV) and their
constituent chains, either when immobilized on polystyrene or blotted
to nitrocellulose. PDGF-collagen interactions were of medium affinity
(KD between 4 and 22 nM) and were
inhibited by different soluble collagen chains suggesting a collagenous
consensus binding site(s) for the PDGF isoforms investigated. Scatchard
analysis revealed molar ratios of up to 3-4 PDGF molecules
bound/triple-helical (native) collagen. Biological activity of
collagen-bound PDGF was demonstrated by a 1.5-3-fold stimulation of
proliferation of human fibroblasts and mouse 3T3 cells. Furthermore, a
preferential association of PDGF with the collagenous extracellular
matrix of cirrhotic liver could be shown by immunostaining. Our data
are in accord with previous studies that localized PDGF in the
extracellular matrix of fibroproliferative lesions and suggest that
binding of PDGF to collagens may localize and modulate its biological
activities.
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26884-26891
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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