http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11596
Inhibition of endothelial cell migration and angiogenesis by a vascular endothelial growth factor receptor-1 derived peptide. (Articolo in rivista)
- Type
- Label
- Inhibition of endothelial cell migration and angiogenesis by a vascular endothelial growth factor receptor-1 derived peptide. (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.ejca.2008.06.032 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lacal PM; Morea V; Ruffini F; Orecchia A; Dorio AS; Failla CM; Soro S; Tentori L; Zambruno G; Graziani G; Tramontano A; D'Atri S. (literal)
- Pagina inizio
- Pagina fine
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- http://www.sciencedirect.com/science/article/pii/S0959804908005054 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- Note
- ISI Web of Science (WOS) (literal)
- PubMe (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Laboratory of Molecular Oncology, Istituto Dermopatico dell'Immacolata-IRCCS, Via dei Monti di Creta 104, 00167 Rome, Italy; Institute of Molecular Biology and Pathology, National Research Council, Rome, Italy; INSERM U634, Faculte de Medecine, Universite Nice Sophia Antipolis, Nice cedex, France; Department of Neuroscience, University of Rome ''Tor Vergata'', Rome, Italy; Laboratory of Molecular and Cell Biology, Istituto Dermopatico dell'Immacolata-IRCCS, Rome, Italy; Department of Biochemical Sciences, University of Rome ''La Sapienza'', Rome, Italy (literal)
- Titolo
- Inhibition of endothelial cell migration and angiogenesis by a vascular endothelial growth factor receptor-1 derived peptide. (literal)
- Abstract
- Vascular endothelial growth factor receptor-1 (VEGFR-1) exists in two isoforms: a membrane-bound isoform (mVEGFR-1) and a soluble one (sVEGFR-1). mVEGFR-1 is involved in endothelial cell migration and survival supported by VEGF-A and placenta growth factor (PIGF), whereas the biologic function of sVEGFR-1 has not been fully elucidated. We previously reported that sVEGFR-1 induces endothelial cell motility and promotes endothelial cell adhesion. In this study, we tested a set of VEGFR-1-derived peptides for their ability to interfere with endothelial cell migration. Peptide B3 was found to specifically inhibit cell migration induced by sVEGFR-1 and by mVEGFR-1-specific ligands. Moreover, peptide B3 markedly hampered angiogenesis in vitro and in vivo and was found to interfere with VEGFR-1 homodimerisation. Altogether, these data demonstrate that peptide B3 might be a useful tool for the specific inhibition of VEGFR-1 function and might represent a basis for the development of new anti-angiogenic compounds. (literal)
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