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PMID: 9712843 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Neuropilin-1 is a placenta growth factor-2 receptor.

The Journal of biological chemistry ·Vol. 273 ·No. 35 ·1998-08-28 ·Pages 22272-8

Migdal M, Huppertz B, Tessler S, Comforti A, Shibuya M, Reich R, Baumann H, Neufeld G

Abstract

Placenta growth factor (PlGF) belongs to the family of vascular endothelial growth factors (VEGFs). It binds to the flt-1 VEGF receptor but not to the KDR/flk-1 receptor which is thought to mediate most of the angiogenic and proliferative effects of VEGF. Three PlGF isoforms are produced by alternative splicing. PlGF-1 and PlGF-3 differ from PlGF-2 since they lack the exon 6 encoded peptide which bestows upon PlGF-2 its heparin binding properties. Cross-linking experiments revealed that 125I-PlGF-2 binds to two endothelial cell surface receptors in a heparin dependent fashion. The binding of 125I-PlGF-2 to these receptors was inhibited by an excess of PlGF-2 and by the 165-amino acid form of VEGF (VEGF165), but not at all by VEGF121 and very marginally if at all by PlGF-1. The apparent molecular weight and the binding characteristics of these receptors correspond to those of the recently identified VEGF165 specific receptor neuropilin-1, and we therefore conclude that neuropilin-1 is a receptor for PlGF-2. The binding of 125I-PlGF-2 as well as the binding of 125I-VEGF165 to these receptors was inhibited by a synthetic peptide derived from exon 6 of PlGF. Furthermore, the binding of 125I-PlGF-2, but not that of 125I-VEGF165, was also inhibited by a synthetic peptide derived from exon 7 of PlGF. These observations indicate that the peptides encoded by these exons probably participate in the formation of the domain which mediates the binding of PlGF-2 to these receptors. We have also determined, using chemically modified heparin species, that the presence of sulfate moieties on the glucosamine-O-6 and on the iduronic acid-O-2 groups of heparin was required for the potentiation of 125I-PlGF-2 binding to these receptors. To determine if PlGF-2 is able to induce biological responses that are not induced by PlGF-1, we compared the effects of PlGF-1 and PlGF-2 on the migration and proliferation of endothelial cells. Both PlGF forms induced migration of endothelial cells. However, there was no quantitative difference between the response to PlGF-2 and the response to PlGF-1. Furthermore, neither PlGF-1 nor PlGF-2 had any effect upon the proliferation of the endothelial cells.

MeSH Terms
Animals Cattle Cell Division Endothelium, Vascular/cytology,metabolism Exons Glucosamine/chemistry Heparin/chemistry,metabolism Humans Iduronic Acid/chemistry Membrane Proteins Nerve Tissue Proteins/metabolism Neuropilin-1 Peptides/pharmacology Protein Binding Proteins/antagonists & inhibitors,genetics,metabolism Receptors, Cell Surface/metabolism
Chemicals
Membrane Proteins Nerve Tissue Proteins PIGF protein, human Peptides Proteins Receptors, Cell Surface Neuropilin-1 Iduronic Acid Heparin Glucosamine
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Migdal M
Department of Biology, Technion, Israel Institute of Technology, Haifa, 32000, Israel.
Huppertz B
Tessler S
Comforti A
Shibuya M
Reich R
Baumann H
Neufeld G
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1998-08-28
Pages
22272-8
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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