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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2000-7-20
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pubmed:abstractText |
Neuropilin-1 (np-1) and neuropilin-2 (np-2) are receptors for axon guidance factors belonging to the class 3 semaphorins. np-1 also binds to the 165-amino acid heparin-binding form of VEGF (VEGF(165)) but not to the shorter VEGF(121) form, which lacks a heparin binding ability. We report that human umbilical vein-derived endothelial cells express the a17 and a22 splice forms of the np-2 receptor. Both np-2 forms bind VEGF(165) with high affinity in the presence of heparin (K(D) 1.3 x 10(-10) m) but not VEGF(121). np-2 also binds the heparin-binding form of placenta growth factor. These binding characteristics resemble those of np-1. VEGF(145) is a secreted heparin binding VEGF form that contains the peptide encoded by exon 6 of VEGF but not the peptide encoded by exon 7, which is present in VEGF(165). VEGF(145) binds to np-2 with high affinity (K(D) 7 x 10(-10) m). Surprisingly, VEGF(145) did not bind to np-1. Indeed, VEGF(145) does not bind to MDA-MB-231 breast cancer cells, which predominantly express np-1. By contrast, VEGF(145) binds to human umbilical vein-derived endothelial cells, which express both np-1 and np-2. The binding of VEGF(165) to porcine aortic endothelial cells expressing recombinant np-2 did not affect the proliferation or migration of the cells. Nevertheless, it is possible that VEGF-induced np-2-mediated signaling will take place only in the presence of other VEGF receptors such as VEGF receptor-1 or VEGF receptor-2.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endothelial Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphokines,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropilin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Pregnancy Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/VEGFA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factors,
http://linkedlifedata.com/resource/pubmed/chemical/placenta growth factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18040-5
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pubmed:dateRevised |
2009-11-25
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pubmed:meshHeading |
pubmed-meshheading:10748121-Animals,
pubmed-meshheading:10748121-Baculoviridae,
pubmed-meshheading:10748121-Breast Neoplasms,
pubmed-meshheading:10748121-Cells, Cultured,
pubmed-meshheading:10748121-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10748121-Endothelial Growth Factors,
pubmed-meshheading:10748121-Endothelium,
pubmed-meshheading:10748121-Female,
pubmed-meshheading:10748121-Growth Substances,
pubmed-meshheading:10748121-Humans,
pubmed-meshheading:10748121-Lymphokines,
pubmed-meshheading:10748121-Nerve Tissue Proteins,
pubmed-meshheading:10748121-Neuropilin-1,
pubmed-meshheading:10748121-Placenta,
pubmed-meshheading:10748121-Pregnancy Proteins,
pubmed-meshheading:10748121-Protein Binding,
pubmed-meshheading:10748121-Protein Isoforms,
pubmed-meshheading:10748121-Receptors, Cell Surface,
pubmed-meshheading:10748121-Spodoptera,
pubmed-meshheading:10748121-Structure-Activity Relationship,
pubmed-meshheading:10748121-Tumor Cells, Cultured,
pubmed-meshheading:10748121-Vascular Endothelial Growth Factor A,
pubmed-meshheading:10748121-Vascular Endothelial Growth Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected].
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pubmed:affiliation |
Department of Biology, Technion, Israel Institute of Technology, Haifa 32000, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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