Interactions of multiple heparin binding growth factors with neuropilin-1 and potentiation of the activity of fibroblast growth factor-2.
type: Dataset
contact point: Organization
  fn: CCSD
keyword: infoeu-reposemanticsarticle
keyword: mesh-neuropilin-1
keyword: mesh-polysaccharides
keyword: mesh-fibroblast-growth-factor-2
keyword: mesh-biosensing-techniques
keyword: mesh-endothelial-cells
keyword: mesh-cell-line
keyword: journal-articles
keyword: mesh-receptors-fibroblast-growth-factor
keyword: mesh-protein-isoforms
keyword: mesh-binding-sites
keyword: mesh-hepatocyte-growth-factor
keyword: mesh-receptor-fibroblast-growth-factor-type-1
keyword: mesh-protein-structure-tertiary
keyword: mesh-animals
keyword: mesh-heparin
keyword: mesh-receptor-protein-tyrosine-kinases
keyword: mesh-models-molecular
keyword: sdvbbmlife-sciences-q-biobiochemistry-molecular-biology
keyword: mesh-humans
landing page: 0021-9258
description: The hypothesis that neuropilin-1 (Npn-1) may interact with heparin-binding proteins other than vascular endothelial growth factor has been tested using an optical biosensor-based binding assay. The results show that fibroblast growth factor (FGF) 1, 2, 4, and 7, FGF receptor 1, hepatocyte growth factor/scatter factor (HGF/SF), FGF-binding protein, normal protease sensitive form of prion protein, antithrombin III, and Npn-1 itself are all able to interact with Npn-1 immobilized on the sensor surface. FGF-2, FGF-4, and HGF/SF are also shown to interact with Npn-1 in a solution assay. Moreover, these protein-protein interactions are dependent on the ionic strength of the medium and are inhibited by heparin, and the kinetics of binding of FGF-2, FGF-4 and HGF/SF to Npn-1 are characterized by fast association rate constants (270,000-1,600,000 m(-1) s(-1)). These results suggest that Npn-1 possesses a "heparin" mimetic site that is able to interact at least in part through ionic bonding with the heparin binding site on many of the proteins studied. Npn-1 was also found to potentiate the growth stimulatory activity of FGF-2 on human umbilical vein endothelial cells, indicating that Npn-1 may not just bind but also regulate the activity of heparin-binding proteins.
issued: 2026-05-09T10:00:36.211110
language: en
modified: 2026-05-09T10:00:36.211115

test_moissonnage_selune
type: Agent

Interactions of multiple heparin binding growth factors with neuropilin-1 and potentiation of the activity of fibroblast growth factor-2.
type: Distribution
access URL: https://hal.science/hal-00087200
format: HTML
issued: 2026-05-09T10:00:36.244119
modified: 2026-05-09T10:00:36.189854