pubmed-article:12649267 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C2325187 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C0018850 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C0920533 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C1301676 | lld:lifeskim |
pubmed-article:12649267 | lifeskim:mentions | umls-concept:C0767950 | lld:lifeskim |
pubmed-article:12649267 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:12649267 | pubmed:dateCreated | 2003-5-26 | lld:pubmed |
pubmed-article:12649267 | pubmed:abstractText | Lens epithelium-cell derived growth factor (LEDGF) is a transcriptional activator. It protects the cells by binding to cis-stress response ((A/T)GGGG(T/A)), and heat shock (HSE; nGAAn) elements in the stress genes and activating their transcription. Transforming growth factor-beta (TGF-beta) has been implicated in the control of tissue homeostasis, terminal differentiation, and apoptosis. Here we provide evidence that TGF-beta1 down-regulates LEDGF expression and diminishes its affinity for DNA during TGF-beta1-induced phenotypic changes and apoptosis in human lens epithelial cells. Surprisingly, TGF-beta1 treatment for 48 h markedly decreased the LEDGF, Hsp27, and alphaB-crystallin promoter activities with the decrease of abundance of LEDGF mRNA and protein. Deletion mutants of the LEDGF promoter showed that one TGF-beta1 inhibitory element (TIE) like sequence nnnTTGGnnn (-444 to -433) contributed to this negative regulation. Mutation of TIE (TTGG to TATT) abolished the down-regulation of the LEDGF promoter. Gel mobility and supershift assays showed that LEDGF in the nuclear extracts of TGF-beta1-treated human lens epithelial cells did not bind to stress-response elements and HSE. The TGF-beta1-induced down-regulation of LEDGF, Hsp27, and alphaB-crystallin promoters activity was reversed by cotransfection with a plasmid expressing LEDGF. Because overexpression of LEDGF was able to relieve TGF-beta1 and/or stress-induced changes, it would be a candidate molecule to postpone age-related degenerating disorders. | lld:pubmed |
pubmed-article:12649267 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:language | eng | lld:pubmed |
pubmed-article:12649267 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12649267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12649267 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12649267 | pubmed:month | May | lld:pubmed |
pubmed-article:12649267 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:ChylackLeo... | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:KuboEriE | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:ShinoharaTosh... | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:SinghDhirendr... | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:FatmaNigarN | lld:pubmed |
pubmed-article:12649267 | pubmed:author | pubmed-author:SharmaPreetiP | lld:pubmed |
pubmed-article:12649267 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12649267 | pubmed:day | 30 | lld:pubmed |
pubmed-article:12649267 | pubmed:volume | 278 | lld:pubmed |
pubmed-article:12649267 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12649267 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12649267 | pubmed:pagination | 20037-46 | lld:pubmed |
pubmed-article:12649267 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:12649267 | pubmed:meshHeading | pubmed-meshheading:12649267... | lld:pubmed |
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pubmed-article:12649267 | pubmed:meshHeading | pubmed-meshheading:12649267... | lld:pubmed |
pubmed-article:12649267 | pubmed:meshHeading | pubmed-meshheading:12649267... | lld:pubmed |
pubmed-article:12649267 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12649267 | pubmed:articleTitle | Lens epithelium-derived growth factor relieves transforming growth factor-beta1-induced transcription repression of heat shock proteins in human lens epithelial cells. | lld:pubmed |
pubmed-article:12649267 | pubmed:affiliation | Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:12649267 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12649267 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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