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@ARTICLE{Roth:130443,
      author       = {L. Roth$^*$ and C. Prahst$^*$ and T. Ruckdeschel$^*$ and S.
                      Savant$^*$ and S. Weström$^*$ and A. Fantin and M.
                      Riedel$^*$ and M. Héroult$^*$ and C. Ruhrberg and H.
                      Augustin$^*$},
      title        = {{N}europilin-1 mediates vascular permeability independently
                      of vascular endothelial growth factor receptor-2
                      activation.},
      journal      = {Science signaling},
      volume       = {9},
      number       = {425},
      issn         = {1937-9145},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {DKFZ-2017-05522},
      pages        = {ra42 - ra42},
      year         = {2016},
      abstract     = {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-A165). 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-A165, 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.},
      cin          = {A190},
      ddc          = {500},
      cid          = {I:(DE-He78)A190-20160331},
      pnm          = {321 - Basic Concepts (POF3-321)},
      pid          = {G:(DE-HGF)POF3-321},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27117252},
      doi          = {10.1126/scisignal.aad3812},
      url          = {https://inrepo02.dkfz.de/record/130443},
}