Identification of placenta growth factor determinants for binding and activation of Flt-1 receptor (Articolo in rivista)

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Label
  • Identification of placenta growth factor determinants for binding and activation of Flt-1 receptor (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M401418200 (literal)
Alternative label
  • Errico M.; Riccioni T.; Iyer S.; Pisano C.; Acharya K.R.; Persico M.G.; De Falco S. (2004)
    Identification of placenta growth factor determinants for binding and activation of Flt-1 receptor
    in The Journal of biological chemistry (Print); American Society Of Biochemistry And Molecular Biology Inc. (ASBMB), Rockville (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Errico M.; Riccioni T.; Iyer S.; Pisano C.; Acharya K.R.; Persico M.G.; De Falco S. (literal)
Pagina inizio
  • 43929 (literal)
Pagina fine
  • 43939 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.jbc.org/content/279/42/43929.long (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 279 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 42 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • PUBBLICAZIONE (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR, Inst Genet & Biophys Adriano Buzzati Traverso, I-80131 Naples, Italy; Sigma Tau Pharmaceut Co, Ind Farmaceut Riunite, Res & Dev, I-00040 Pomezia, Rome, Italy; Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon, England. (literal)
Titolo
  • Identification of placenta growth factor determinants for binding and activation of Flt-1 receptor (literal)
Abstract
  • Placenta growth factor (PlGF) belongs to the vascular endothelial growth factor (VEGF) family and represents a key regulator of angiogenic events in pathological conditions. PlGF exerts its biological function through the binding and activation of the seven immunoglobulinlike domain receptor Flt-1, also known as VEGFR-1. Here, we report the first detailed mutagenesis studies that provide a basis for understanding molecular recognition between PlGF-1 and Flt-1, highlighting some of the residues that are critical for receptor recognition. Mutagenesis analysis, performed on the basis of a structural model of interaction between PlGF and the minimal binding domain of Flt-1, has led to the identification of several PlGF-1 residues involved in Flt-1 recognition. The two negatively charged residues, Asp-72 and Glu-73, located in the ?3-?4 loop, are critical for Flt-1 binding. Other mutations, which bring about a significant decrease in PlGF binding activity, are Gln-27, located in the N-terminal ?-helix, and Pro-98 and Tyr-100 on the ?6 strand. The mutation of one of the two glycosylated residues of PlGF, Asn-84, generates a PlGF variant with reduced binding activity. This indicates that, unlike in VEGF, glycosylation plays an important role in Flt-1 binding. The double mutation of residues Asp-72 and Glu-73 generates a PlGF variant unable to bind and activate the receptor molecules on the cell surface. This variant failed to induce in vitro capillary-like tube formation of primary endothelial cells or neo-angiogenesis in an in vivo chorioallantoic membrane assay. (literal)
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