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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1992-3-27
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pubmed:abstractText |
We have stably expressed the cDNA encoding the 165 amino-acid long form of human vascular endothelial growth factor (VEGF) in BHK-21 cells. VEGF was partially purified from the conditioned medium of transfected cells using heparin-sepharose affinity chromatography. The partially purified VEGF was mitogenic for various types of endothelial cells and inhibited the binding of pure [125I]VEGF to its receptors. Western blot analysis, using anti-VEGF antibodies, revealed a 47 kDa VEGF homodimer in the partially purified VEGF fraction. Preincubation of the transfected cells with the N-glycosylation inhibitor tunicamycin resulted in the conversion of the 47 kDa VEGF homodimer into a smaller, deglycosylated form of 42 kDa. Partially purified preparations of the deglycosylated VEGF displayed a mitogenic activity that was similar to that of the glycosylated form and efficiently inhibited the binding of native [125I]VEGF to the VEGF receptors of bovine aortic arch derived endothelial cells.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
182
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1340-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1540178-Animals,
pubmed-meshheading:1540178-Blotting, Western,
pubmed-meshheading:1540178-Cattle,
pubmed-meshheading:1540178-Cell Division,
pubmed-meshheading:1540178-Cell Line,
pubmed-meshheading:1540178-Cells, Cultured,
pubmed-meshheading:1540178-DNA,
pubmed-meshheading:1540178-Endothelial Growth Factors,
pubmed-meshheading:1540178-Endothelium, Vascular,
pubmed-meshheading:1540178-Glycosylation,
pubmed-meshheading:1540178-Humans,
pubmed-meshheading:1540178-Lymphokines,
pubmed-meshheading:1540178-Mitogens,
pubmed-meshheading:1540178-Plasmids,
pubmed-meshheading:1540178-Recombinant Proteins,
pubmed-meshheading:1540178-Restriction Mapping,
pubmed-meshheading:1540178-Transfection,
pubmed-meshheading:1540178-Vascular Endothelial Growth Factor A,
pubmed-meshheading:1540178-Vascular Endothelial Growth Factors
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pubmed:year |
1992
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pubmed:articleTitle |
Glycosylation of vascular endothelial growth factor is not required for its mitogenic activity.
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pubmed:affiliation |
Department of Biology, Israel Institute of Technology, Technion City, Haifa.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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