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Titolo:
IDENTIFICATION OF A HEPARIN-BINDING PEPTIDE ON THE EXTRACELLULAR DOMAIN OF THE KDR VEGF RECEPTOR
Autore:
DOUGHER AM; WASSERSTROM H; TORLEY L; SHRIDARAN L; WESTDOCK P; HILEMAN RE; FROMM JR; ANDERBERG R; LYMAN S; LINHARDT RJ; KAPLAN J; TERMAN BI;
Indirizzi:
WYETH AYERST RES,ONCOL PEARL RIVER NY 10965 WYETH AYERST RES,ONCOL PEARL RIVER NY 10965 UNIV IOWA,COLL PHARM,DIV MED & NAT PROD CHEM IOWA CITY IA 52242 IMMUNEX RES & DEV CORP,DEPT MOL GENET SEATTLE WA 98101
Titolo Testata:
Growth factors
fascicolo: 4, volume: 14, anno: 1997,
pagine: 257 - 268
SICI:
0897-7194(1997)14:4<257:IOAHPO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOTHELIAL GROWTH-FACTOR; VASCULAR-PERMEABILITY FACTOR; TYROSINE KINASE; FACTOR FAMILY; CELLS; PLACENTA; OLIGOSACCHARIDES; ELECTROPHORESIS; SPECIFICITY; EXPRESSION;
Keywords:
VEGF; KDR RECEPTOR SUBTYPE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
A.M. Dougher et al., "IDENTIFICATION OF A HEPARIN-BINDING PEPTIDE ON THE EXTRACELLULAR DOMAIN OF THE KDR VEGF RECEPTOR", Growth factors, 14(4), 1997, pp. 257-268

Abstract

Vascular endothelial growth factor (VEGF), a potent and specific activator of endothelial cells, is expressed as multiple homodimeric formsresulting from alternative RNA splicing, VEGF(121) does not bind heparin while the other three isoforms do, and it has been documented thatthe binding of VEGF(165) to its receptor is dependent upon cell surface heparan sulfate proteoglycans, Little is known about the biochemical mechanism that allows for heparin regulation of growth factor binding, For example, it is not clear whether heparin interactions with growth factor or with cell surface receptors or both are essential for VEGF binding to its receptor, In this manuscript we provide results whichare consistent with the hypothesis that an interaction between heparin and a site on the KDR receptor subtype is essential for VEGF(165) binding, First, we demonstrate that expression of KDR into a CHO cell Line deficient in heparan sulfate biosynthesis does not allow VEGF(165) binding unless heparin is exogenously added during the binding assay, Secondly, we show that a ten amino acid synthetic peptide, corresponding to a sequence from the extracellular domain of the KDR, both inhibits VEGF(165) binding to the receptor and also binds heparin with high avidity, Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresisand polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin, Taken together, these results are consistent with the hypothesis that interactions between cell surface heparan sulfate proteoglycans and the VEGF receptor contribute to allowing maximal VEGF binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:30:43