| pubmed-article:9668119 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C1335858 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C0148199 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C1442756 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C0597360 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9668119 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9668119 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:9668119 | pubmed:dateCreated | 1998-8-20 | lld:pubmed |
| pubmed-article:9668119 | pubmed:abstractText | Kinase domain receptor (KDR) is a high affinity, endothelial cell-specific, autophosphorylating tyrosine kinase receptor for vascular endothelial growth factor. This transcriptionally regulated receptor is a critical mediator of endothelial cell (EC) growth and vascular development. In this study, we identify a DNA element modulating KDR promoter activity and evaluate the nuclear binding proteins accounting for a portion of the cell-type specificity of the region. KDR promoter luciferase activity was retained within -85/+296 and was 10-30-fold higher in EC than non-EC. Electrophoretic mobility shift assays demonstrated specific nuclear protein binding to -85/-64, and single point mutations suggested important binding nucleotides between -79/-68 with five critical bases between -74/-70 (5'-CTCCT-3'). DNA-protein complexes were displaced by Sp1 consensus sequence oligodeoxynucleotides and supershifted by Sp1- and Sp3-specific antibodies. Sp1 and Sp3 protein in EC nuclear extracts bound the -79/-68 region even when all surrounding classic Sp1 recognition sites were removed. Sp1 protein in nuclear extracts was 4-24-fold higher in EC than non-EC, whereas Sp3 was 3-7-fold higher. Sp1/Sp3 ratios in EC were 2-10-fold higher. Overexpression of Sp1 protein increased KDR promoter activity 3-fold in both EC and non-EC, whereas simultaneous co-expression of Sp3 attenuated this response. An Sp1 consensus sequence cis element "decoy" reduced EC KDR promoter activity and mRNA expression by 85 and 69%, respectively. An antisense phosphorothioate oligodeoxynucleotide to Sp1 inhibited Sp1 and KDR protein expression by 66 and 68%, respectively, without changing Sp3 protein expression. These data illustrate that Sp1 and Sp3 modulate KDR promoter activity through a novel recognition binding sequence. However, since Sp1-mediated promoter activation is attenuated by Sp3, endothelial selective KDR promoter activity may be partially regulated by variations in the Sp1/Sp3 ratio. | lld:pubmed |
| pubmed-article:9668119 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9668119 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9668119 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9668119 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9668119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9668119 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9668119 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9668119 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9668119 | pubmed:author | pubmed-author:HataYY | lld:pubmed |
| pubmed-article:9668119 | pubmed:author | pubmed-author:ZhangKK | lld:pubmed |
| pubmed-article:9668119 | pubmed:author | pubmed-author:RobinsonG SGS | lld:pubmed |
| pubmed-article:9668119 | pubmed:author | pubmed-author:AielloL PLP | lld:pubmed |
| pubmed-article:9668119 | pubmed:author | pubmed-author:DumNN | lld:pubmed |
| pubmed-article:9668119 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9668119 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:9668119 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9668119 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9668119 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9668119 | pubmed:pagination | 19294-303 | lld:pubmed |
| pubmed-article:9668119 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9668119 | pubmed:meshHeading | pubmed-meshheading:9668119-... | lld:pubmed |
| pubmed-article:9668119 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9668119 | pubmed:articleTitle | Transcription factors Sp1 and Sp3 alter vascular endothelial growth factor receptor expression through a novel recognition sequence. | lld:pubmed |
| pubmed-article:9668119 | pubmed:affiliation | Research Division, Joslin Diabetes Center, Boston, Massachusetts 02215, USA. | lld:pubmed |
| pubmed-article:9668119 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9668119 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9668119 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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