Angiogenesis in vitro inhibition of platelet factor-4-derived peptides and mechanism of action

In this study, detailed study of the interaction of platelet factor -4 (PF-4), and fibroblast growth factor -2 (FGF-2) and vascular endothelial growth factor (VEGF) and the synthetic peptides derived from PF-4effect. We show that between 47 and 70 amino acid peptide to inhibit the function of FGF-2, or vascular endothelial growth factor, which contains a heparin-binding site of the lysine-rich. This is based on the following observations: PF-4 peptide 47-70 to inhibit the FGF-2 or VEGF binding to vascular endothelial cells, it inhibits the binding of FGF-2 or VEGF heparan sulfate - deficient CHO cells FGFRs or VEGFRs transfection of-FGFR1 (CHOFGFR1) or VEGFR2 (CHOmVEGFR2) gene, to prevent the diffusion tube to form a three-dimensional angiogenesis detection Finally, it is directly associated 125I-PF-4, FGF-2, VEGF, and competition, inhibit heparin-induced FGF-2 dimers. A short C-terminal peptide (peptide 58-70), still contains a heparin-binding lysin-rich Web site, there is no effect. Peptide 17-58, which is in the central part of the molecule, although it does not inhibit the FGF-2 or VEGF binding or the biological activity in the vascular endothelial cells, inhibition of the heparin-dependent binding of125I-FGF-2 or the 125 I-VEGF CHOmFGFR1 or CHOmVEGFR2 cells, respectively. Short peptides (peptide 34-58 and 47-58) does not have any impact.

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inhibition of the heparin-dependent binding of125I-FGF-2 or the 125 I-VEGF CHOmFGFR1 or CHOmVEGFR2 cells, respectively.



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