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Differential bindin...
Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1.
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- Mäkinen, Taija (författare)
- Uppsala universitet,Vaskulärbiologi
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Olofsson, B (författare)
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Karpanen, T (författare)
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Hellman, U (författare)
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Soker, S (författare)
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Klagsbrun, M (författare)
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- Eriksson, U (författare)
- Karolinska Institutet
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Alitalo, K (författare)
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(creator_code:org_t)
- Elsevier BV, 1999
- 1999
- Engelska.
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Ingår i: Journal of Biological Chemistry. - : Elsevier BV. - 0021-9258 .- 1083-351X. ; 274:30
- Relaterad länk:
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http://www.jbc.org/c...
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https://urn.kb.se/re...
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http://kipublication...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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