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Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1.
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1999 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 274, no 30Article in journal (Refereed) Published
Abstract [en]

Vascular endothelial growth factor B (VEGF-B) is expressed in various tissues, especially strongly in the heart, and binds selectively to one of the VEGF receptors, VEGFR-1. The two splice isoforms, VEGF-B(167) and VEGF-B(186), have identical NH(2)-terminal cystine knot growth factor domains but differ in their COOH-terminal domains which give these forms their distinct biochemical properties. In this study, we show that both splice isoforms of VEGF-B bind specifically to Neuropilin-1 (NRP1), a receptor for collapsins/semaphorins and for the VEGF(165) isoform. The NRP1 binding of VEGF-B could be competed by an excess of VEGF(165). The binding of VEGF-B(167) was mediated by the heparin binding domain, whereas the binding of VEGF-B(186) to NRP1 was regulated by exposure of a short COOH-terminal proline-rich peptide upon its proteolytic processing. In immunohistochemistry, NRP1 distribution was found to be overlapping or adjacent to known sites of VEGF-B expression in several tissues, in particular in the developing heart, suggesting the involvement of VEGF-B in NRP1-mediated signaling.

Place, publisher, year, edition, pages
1999. Vol. 274, no 30
National Category
Basic Medicine
Identifiers
URN: urn:nbn:se:uu:diva-287179PubMedID: 10409677OAI: oai:DiVA.org:uu-287179DiVA: diva2:922290
Available from: 2016-04-22 Created: 2016-04-22 Last updated: 2017-11-30

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