pubmed-article:19417140 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0042172 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0929301 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0006141 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0694888 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0026559 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0237477 | lld:lifeskim |
pubmed-article:19417140 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:19417140 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:19417140 | pubmed:dateCreated | 2009-5-18 | lld:pubmed |
pubmed-article:19417140 | pubmed:abstractText | Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a dual-function phosphatase with tumor suppressor function compromised in a wide spectrum of cancers. Because tissue polarity and architecture are crucial modulators of normal and malignant behavior, we postulated that PTEN may play a role in maintenance of tissue integrity. We used two nonmalignant human mammary epithelial cell lines that form polarized, growth-arrested structures (acini) when cultured in three-dimensional laminin-rich extracellular matrix gels (lrECM). As acini begin to form, PTEN accumulates both in the cytoplasm and at cell-cell contacts where it colocalizes with the E-cadherin/beta-catenin complex. Reduction of PTEN levels by shRNA in lrECM prevents formation of organized breast acini and disrupts growth arrest. Importantly, disruption of acinar polarity and cell-cell contact by E-cadherin function-blocking antibodies reduces endogenous PTEN protein levels and inhibits its accumulation at cell-cell contacts. Conversely, in Skbr-3 breast cancer cells lacking endogenous E-cadherin expression, exogenous introduction of E-cadherin gene causes induction of PTEN expression and its accumulation at sites of cell interactions. These studies provide evidence that E-cadherin regulates both the PTEN protein levels and its recruitment to cell-cell junctions in three-dimensional lrECM, indicating a dynamic reciprocity between architectural integrity and the levels and localization of PTEN. This interaction thus seems to be a critical integrator of proliferative and morphogenetic signaling in breast epithelial cells. | lld:pubmed |
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pubmed-article:19417140 | pubmed:language | eng | lld:pubmed |
pubmed-article:19417140 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19417140 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19417140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19417140 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19417140 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19417140 | pubmed:month | May | lld:pubmed |
pubmed-article:19417140 | pubmed:issn | 1538-7445 | lld:pubmed |
pubmed-article:19417140 | pubmed:author | pubmed-author:BissellMina... | lld:pubmed |
pubmed-article:19417140 | pubmed:author | pubmed-author:FournierMarci... | lld:pubmed |
pubmed-article:19417140 | pubmed:author | pubmed-author:YaswenPaulP | lld:pubmed |
pubmed-article:19417140 | pubmed:author | pubmed-author:MartinKatheri... | lld:pubmed |
pubmed-article:19417140 | pubmed:author | pubmed-author:FataJimmie... | lld:pubmed |
pubmed-article:19417140 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19417140 | pubmed:day | 15 | lld:pubmed |
pubmed-article:19417140 | pubmed:volume | 69 | lld:pubmed |
pubmed-article:19417140 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19417140 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19417140 | pubmed:pagination | 4545-52 | lld:pubmed |
pubmed-article:19417140 | pubmed:dateRevised | 2011-4-11 | lld:pubmed |
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