PUBLICATION

N-tert-butyloxycarbonyl-Phe-Leu-Phe-Leu-Phe (BOC2) inhibits the angiogenic activity of heparin-binding growth factors

Authors
Nawaz, I.M., Chiodelli, P., Rezzola, S., Paganini, G., Corsini, M., Lodola, A., Di Ianni, A., Mor, M., Presta, M.
ID
ZDB-PUB-191029-16
Date
2018
Source
Angiogenesis   21: 47-59 (Journal)
Registered Authors
Presta, Marco
Keywords
Angiogenesis, BOC2, FGF2, Heparin binding, VEGF
MeSH Terms
  • Animals
  • CHO Cells
  • Cattle
  • Cell Line, Tumor
  • Chick Embryo
  • Cricetulus
  • Fibroblast Growth Factor 2*/antagonists & inhibitors
  • Fibroblast Growth Factor 2*/chemistry
  • Fibroblast Growth Factor 2*/metabolism
  • Human Umbilical Vein Endothelial Cells/cytology
  • Human Umbilical Vein Endothelial Cells/metabolism*
  • Humans
  • Neovascularization, Physiologic/drug effects*
  • Neovascularization, Physiologic/physiology
  • Oligopeptides*/chemistry
  • Oligopeptides*/pharmacology
  • Receptors, Formyl Peptide/metabolism
  • Signal Transduction/drug effects
  • Surface Plasmon Resonance
  • Vascular Endothelial Growth Factor A*/antagonists & inhibitors
  • Vascular Endothelial Growth Factor A*/chemistry
  • Vascular Endothelial Growth Factor A*/metabolism
  • Vascular Endothelial Growth Factor Receptor-2/metabolism
  • Zebrafish
PubMed
29030736 Full text @ Angiogenesis
Abstract
The peptides N-tert-butyloxycarbonyl-Phe-Leu-Phe-Leu-Phe (BOC2) and BOC-Met-Leu-Phe (BOC1) are widely used antagonists of formyl peptide receptors (FPRs), BOC2 acting as an FPR1/FPR2 antagonist whereas BOC1 inhibits FPR1 only. Extensive investigations have been performed by using these FPR antagonists as a tool to assess the role of FPRs in physiological and pathological conditions. Based on previous observations from our laboratory, we assessed the possibility that BOC2 may exert also a direct inhibitory effect on the angiogenic activity of vascular endothelial growth factor-A (VEGF-A). Our data demonstrate that BOC2, but not BOC1, inhibits the angiogenic activity of heparin-binding VEGF-A165 with no effect on the activity of the non-heparin-binding VEGF-A121 isoform. Endothelial cell-based bioassays, surface plasmon resonance analysis, and computer modeling indicate that BOC2 may interact with the heparin-binding domain of VEGF-A165, thus competing for heparin interaction and preventing the binding of VEGF-A165 to tyrosine kinase receptor VEGFR2, its phosphorylation and downstream signaling. In addition, BOC2 inhibits the interaction of a variety of heparin-binding angiogenic growth factors with heparin, including fibroblast growth factor 2 (FGF2) whose angiogenic activity is blocked by the compound. Accordingly, BOC2 suppresses the angiogenic potential of human tumor cell lines that co-express VEGF-A and FGF2. Thus, BOC2 appears to act as a novel multi-heparin-binding growth factor antagonist. These findings caution about the interpretation of FPR-focusing experimental data obtained with this compound and set the basis for the design of novel BOC2-derived, FPR independent multi-target angiogenesis inhibitors.
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