| pubmed-article:15579439 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C0205266 | lld:lifeskim |
| pubmed-article:15579439 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:15579439 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15579439 | pubmed:dateCreated | 2004-12-6 | lld:pubmed |
| pubmed-article:15579439 | pubmed:abstractText | Injury of the tubular epithelium and TGF-beta1-induced conversion of epithelial cells to alpha-smooth muscle actin (SMA)-expressing myofibroblasts are key features of kidney fibrosis. Since injury damages intercellular junctions and promotes fibrosis, we hypothesized that cell contacts are critical regulators of TGF-beta 1-triggered epithelial-to-mesenchymal transition (EMT). Here we show that TGF-beta 1 was unable to induce EMT in intact confluent monolayers, but three different models of injury-induced loss of epithelial integrity (subconfluence, wounding, and contact disassembly by Ca(2+)-removal) restored its EMT-inducing effect. This manifested in loss of E-cadherin, increased fibronectin production and SMA expression. TGF-beta 1 or contact disassembly alone only modestly stimulated the SMA promoter in confluent layers, but together exhibited strong synergy. Since beta-catenin is a component of intact adherens junctions, but when liberated from destabilized contacts may act as a transcriptional co-activator, we investigated its role in TGF-beta 1-provoked EMT. Contact disassembly alone induced degradation of E-cadherin and beta-catenin, but TGF-beta1 selectively rescued beta-catenin and stimulated the beta-catenin-driven reporter TopFLASH. Moreover, chelation of free beta-catenin with the N-cadherin cytoplasmic tail suppressed the TGF-beta1 plus contact disassembly-induced SMA promoter activation and protein expression. These results suggest a beta-catenin-dependent two-hit mechanism in which both an initial epithelial injury and TGF-beta 1 are required for EMT. | lld:pubmed |
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| pubmed-article:15579439 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15579439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579439 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:15579439 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15579439 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:15579439 | pubmed:issn | 0002-9440 | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:RotsteinOri... | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:KapusAndrásA | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:RosivallLászl... | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:MucsiIstvánI | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:McCullochChri... | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:FanLingzhiL | lld:pubmed |
| pubmed-article:15579439 | pubmed:author | pubmed-author:MassziAndrásA | lld:pubmed |
| pubmed-article:15579439 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15579439 | pubmed:volume | 165 | lld:pubmed |
| pubmed-article:15579439 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15579439 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15579439 | pubmed:pagination | 1955-67 | lld:pubmed |
| pubmed-article:15579439 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15579439 | pubmed:meshHeading | pubmed-meshheading:15579439... | lld:pubmed |
| pubmed-article:15579439 | pubmed:meshHeading | pubmed-meshheading:15579439... | lld:pubmed |
| pubmed-article:15579439 | pubmed:meshHeading | pubmed-meshheading:15579439... | lld:pubmed |
