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Neuropilin-1 mediates vascular permeability independently of vascular endothelial growth factor receptor-2 activation
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- Roth, Lise (författare)
- German Canc Res Ctr DKFZ ZMBH Alliance, Div Vasc Oncol & Metastasis, D-69120 Heidelberg, Germany.;Heidelberg Univ, Med Fac Mannheim, Dept Vasc Biol & Tumor Angiogenesis CBTM, D-68167 Mannheim, Germany.
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- Prahst, Claudia (författare)
- German Canc Res Ctr DKFZ ZMBH Alliance, Div Vasc Oncol & Metastasis, D-69120 Heidelberg, Germany.;Beth Israel Deaconess Med Ctr, Vasc Biol Res Ctr, Boston, MA 02215 USA.
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- Ruckdeschel, Tina (författare)
- German Canc Res Ctr DKFZ ZMBH Alliance, Div Vasc Oncol & Metastasis, D-69120 Heidelberg, Germany.
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- German Canc Res Ctr DKFZ ZMBH Alliance, Div Vasc Oncol & Metastasis, D-69120 Heidelberg, Germany;Heidelberg Univ, Med Fac Mannheim, Dept Vasc Biol & Tumor Angiogenesis CBTM, D-68167 Mannheim, Germany. German Canc Res Ctr DKFZ ZMBH Alliance, Div Vasc Oncol & Metastasis, D-69120 Heidelberg, Germany.;Beth Israel Deaconess Med Ctr, Vasc Biol Res Ctr, Boston, MA 02215 USA. (creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2016
- 2016
- Engelska.
- Ingår i: Science Signaling. - : American Association for the Advancement of Science (AAAS). - 1945-0877 .- 1937-9145. ; 9:425
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- Neuropilin-1 (NRP1) regulates developmental and pathological angiogenesis, arteriogenesis, and vascular permeability, acting as a coreceptor for semaphorin 3A (Sema3A) and the 165-amino acid isoform of vascular endothelial growth factor A (VEGF-A(165)). NRP1 is also the receptor for the CendR peptides, a class of cell-and tissue-penetrating peptides with a specific R-x-x-R carboxyl-terminal motif. Because the cytoplasmic domain of NRP1 lacks catalytic activity, NRP1 is mainly thought to act through the recruitment and binding to other receptors. We report here that the NRP1 intracellular domain mediates vascular permeability. Stimulation with VEGF-A(165), a ligand-blocking antibody, and a CendR peptide led to NRP1 accumulation at cell-cell contacts in endothelial cell monolayers, increased cellular permeability in vitro and vascular leakage in vivo. Biochemical analyses, VEGF receptor-2 (VEGFR-2) silencing, and the use of a specific VEGFR blocker established that the effects induced by the CendR peptide and the antibody were independent of VEGFR-2. Moreover, leakage assays in mice expressing a mutant NRP1 lacking the cytoplasmic domain revealed that this domain was required for NRP1-induced vascular permeability in vivo. Hence, these data define a vascular permeability pathway mediated by NRP1 but independent of VEGFR-2 activation.
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- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
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