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Blood, Vol. 94 No. 3 (August 1), 1999:
pp. 984-993
Inhibition of In Vitro Angiogenesis by Platelet Factor-4-Derived
Peptides and Mechanism of Action
Valérie Jouan,
Xavier Canron,
Monica Alemany,
Jacques P. Caen,
Gérard Quentin,
Jean Plouet, and
Andreas Bikfalvi
From the Growth Factor and Cell Differentiation Laboratory,
University Bordeaux I, Talence; Institut des Vaisseaux et du Sang,
Paris; SERBIO, Gennevilliers; and CNRS UPR 9006, Toulouse, France.
In this study, we examined in detail the interaction of platelet
factor-4 (PF-4) with fibroblast growth factor-2 (FGF-2) and vascular
endothelial growth factor (VEGF) and the effect of PF-4-derived synthetic peptides. We show that a peptide between amino acids 47 and
70 that contains the heparin-binding lysine-rich site inhibits FGF-2 or
VEGF function. This is based on the following observations: PF-4
peptide 47-70 inhibited FGF-2 or VEGF binding to endothelial cells; it
inhibited FGF-2 or VEGF binding to FGFRs or VEGFRs in heparan
sulfate-deficient CHO cells transfected with FGFR1 (CHOFGFR1) or
VEGFR2 (CHOmVEGFR2) cDNA; it blocked proliferation or tube formation in
three-dimensional angiogenesis assays; and, finally, it competed with
the direct association of 125I-PF-4 with FGF-2 or VEGF,
respectively, and inhibited heparin-induced FGF-2 dimerization. A
shorter C-terminal peptide (peptide 58-70), which still
contained the heparin-binding lysin-rich site, had no effect. Peptide
17-58, which is located in the central part of the molecule, although
it does not inhibit FGF-2 or VEGF binding or biologic activity in
endothelial cells, inhibited heparin-dependent binding of
125I-FGF-2 or 125I-VEGF to CHOmFGFR1 or
CHOmVEGFR2 cells, respectively. Shorter peptides (peptides 34-58 and
47-58) did not show any of these effects.
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