Neuropilin-1 Is Expressed by Endothelial and Tumor Cells as an Isoform-Specific Receptor for Vascular Endothelial Growth Factor

@article{Soker1998Neuropilin1IE,
  title={Neuropilin-1 Is Expressed by Endothelial and Tumor Cells as an Isoform-Specific Receptor for Vascular Endothelial Growth Factor},
  author={Shay Soker and Seiji Takashima and Hua Miao and Gera Neufeld and Michael Klagsbrun},
  journal={Cell},
  year={1998},
  volume={92},
  pages={735-745}
}

Figures from this paper

Neuropilin-1-mediated Vascular Permeability Factor/Vascular Endothelial Growth Factor-dependent Endothelial Cell Migration*

This study constructed a chimeric receptor, EGNP-1, by fusing the extracellular domain of epidermal growth factor receptor to the transmembrane and intracellular domains of NRP-1 and transduced it into HUVECs with a retroviral expression vector and showed for the first time that N RP-1 can independently promote cell signaling in endothelial cells.

Selective induction of neuropilin-1 by vascular endothelial growth factor (VEGF): A mechanism contributing to VEGF-induced angiogenesis

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The results suggest that VEGF cannot only activate endothelial cells directly but also can contribute to robust angiogenesis in vivo by a mechanism that involves up-regulation of its cognate receptor expression.

Vascular Endothelial Growth Factor Receptor-2 and Neuropilin-1 Form a Receptor Complex That Is Responsible for the Differential Signaling Potency of VEGF165 and VEGF121 *

It is demonstrated that although VEGFR-2 and Npn-1 form a complex, this complex does not result in an increase in VEGF165 binding affinity, and data suggest a receptor-clustering role for NPN-1, as opposed to Npn -1 behaving as an affinity-converting subunit.

Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration.

The data indicate that NRP2 acts as a coreceptor that enhances human endothelial cell biological responses induced by VEGF-A and VEGf-C, and is correlated with an enhancement of the VEGFR-2 phosphorylation threshold.

Neuropilin-1 regulates attachment in human endothelial cells independently of vascular endothelial growth factor receptor-2.

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Neuropilin-1 Binds to VEGF121 and Regulates Endothelial Cell Migration and Sprouting*

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Structural Basis for Selective Vascular Endothelial Growth Factor-A (VEGF-A) Binding to Neuropilin-1*

The structural basis for selective VEGF-A splice form binding to neuropilin is established and it is demonstrated that the exon 8-encoded C-terminal arginine is essential for the interaction of VEGf-A with Nrp1 and mediates high affinity NrP binding.

A VEGF-A splice variant defective for heparan sulfate and neuropilin-1 binding shows attenuated signaling through VEGFR-2

VEGF-A165b has attenuated signaling potential through VEGF receptor 2 defining this new member of the V EGF family as a partial receptor agonist.

The splice variants of vascular endothelial growth factor (VEGF) and their receptors.

Vascular endothelial growth factor (VEGF) is a secreted mitogen highly specific for cultured endothelial cells and plays a central role in both angiogenesis and vasculogenesis, most notably the neovascularisation of growing tumours.

Neuropilin-1 Regulates Vascular Endothelial Growth Factor–Mediated Endothelial Permeability

A critical role for Npn-1 is supported in regulating endothelial barrier dysfunction in response to VEGF and activation of distinct receptor complexes may determine specificity of cellular response toVEGF is suggested.
...

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