Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor.

Department of Surgery, Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Vascular 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.
Mesh Terms:
Antigens, Surface, Cell Line, Chemotaxis, Cloning, Molecular, Endothelial Growth Factors, Endothelium, Vascular, Exons, Gene Expression, Humans, Isomerism, Lymphokines, Molecular Sequence Data, Neovascularization, Physiologic, Nerve Tissue Proteins, Neuropilin-1, RNA, Messenger, Receptor Protein-Tyrosine Kinases, Receptors, Growth Factor, Receptors, Mitogen, Receptors, Vascular Endothelial Growth Factor, Recombinant Fusion Proteins, Umbilical Cord, Vascular Endothelial Growth Factor A, Vascular Endothelial Growth Factors
Cell Mar. 20, 1998; 92(6);735-45 [PUBMED:9529250]
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