Effect of HGF-like basic hexapeptides on angiogenesis

K. Fazekas, A. Janovics, B. Döme, P. Koska, A. Albini, J. Tímár

Research output: Contribution to journalArticlepeer-review


The interaction of glycosaminoglycans (GAG) with peptides relies on noncovalent binding to basic amino acid sequences, for which a minimal requirement is a pentapeptide region in the protein and the sulfated and carboxyl region in the GAG. Since such sequences are present in the heparin-binding angiogenic cytokines, including hepatocyte growth factor (HGF), we have postulated that such small peptides may have biological activity. Two basic peptide regions of the β chain of HGF (RYRNKH512-516, HHRGK645-649) exhibited significant anti-angiogenic activity in viva in the chorioallantoic membrane assay and showed some antiproliferative activity in vitro on normal human brain microvessel endothelial - but not on anchorage-independent endothelial - cells (Kaposi sarcoma). Basic HIV-TAT peptides and scrambled hexapeptides did not show similar activity, except for KRKRKR, indicating sequence specificity of the phenomena. An HGF-derived basic peptide, HHRGK, modulated tumor-induced angiogenesis in viva by interfering with the morphogenic, but not with the proliferative, phase of the process. These observations suggest small basic peptides as a new class of angiogenesis modulators.

Original languageEnglish
Pages (from-to)440-444
Number of pages5
JournalMicrovascular Research
Issue number3
Publication statusPublished - 2001


  • Basic peptides
  • CAM assay
  • Endothelial cells
  • HGF β-chain
  • Tumor-induced angiogenesis

ASJC Scopus subject areas

  • Biochemistry
  • Cardiology and Cardiovascular Medicine


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