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pubmed-article:9529250pubmed:abstractTextVascular endothelial growth factor (VEGF), a major regulator of angiogenesis, binds to two receptor tyrosine kinases, KDR/Flk-1 and Flt-1. We now describe the purification and the expression cloning from tumor cells of a third VEGF receptor, one that binds VEGF165 but not VEGF121. This isoform-specific VEGF receptor (VEGF165R) is identical to human neuropilin-1, a receptor for the collapsin/semaphorin family that mediates neuronal cell guidance. When coexpressed in cells with KDR, neuropilin-1 enhances the binding of VEGF165 to KDR and VEGF165-mediated chemotaxis. Conversely, inhibition of VEGF165 binding to neuropilin-1 inhibits its binding to KDR and its mitogenic activity for endothelial cells. We propose that neuropilin-1 is a novel VEGF receptor that modulates VEGF binding to KDR and subsequent bioactivity and therefore may regulate VEGF-induced angiogenesis.lld:pubmed
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pubmed-article:9529250pubmed:articleTitleNeuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor.lld:pubmed
pubmed-article:9529250pubmed:affiliationDepartment of Surgery, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.lld:pubmed
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pubmed-article:9529250pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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