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| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0035339 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C1512505 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C1154382 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C2350440 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0808080 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C2261503 | lld:lifeskim |
| pubmed-article:8754749 | lifeskim:mentions | umls-concept:C1705922 | lld:lifeskim |
| pubmed-article:8754749 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8754749 | pubmed:dateCreated | 1996-12-18 | lld:pubmed |
| pubmed-article:8754749 | pubmed:abstractText | In this study we show that a breast cancer cell line (SKBR3) that expresses no E-cadherin and very low levels of beta-catenin protein and exhibits a poorly adhesive phenotype in Matrigel responds to retinoic acid (RA) by a marked increase in epithelial differentiation. Specifically, treatment of cells with all-trans-RA, 9-cis-RA, or a RA receptor alpha-specific ligand resulted in a large increase in cell-cell adhesive strength and stimulated the formation of fused cell aggregates in Matrigel. A retinoid X receptor-specific ligand was ineffective. Exposure of cells to 9-cis-RA for as little as 4 h was sufficient to maintain the adhesive phenotype for at least 4 days. The effects of 9-cis-RA required protein and RNA synthesis, but were not mediated by factors secreted by stimulated cells or by direct cell contact and did not require serum. These 9-cis-RA-induced morphological effects were completely reversed by growing cells in 50 microM Ca2+, suggesting a mechanism involving a 9-cis-RA-induced increase in Ca(2+)-dependent adhesion. Consistent with this, beta-catenin protein levels were markedly elevated in the 9-cis-RA-treated cells, and beta-catenin became localized to a Triton-insoluble pool at regions of cell-cell contact. No change could be detected in beta-catenin steady state messenger RNA levels, but 9-cis-RA did increase beta-catenin protein stability. Treatment of cells with low calcium medium did not prevent the 9-cis-RA-induced increase in total beta-catenin protein, but did prevent its movement to a Triton-insoluble pool at the cell membrane. Among several kinase inhibitors, only the broad spectrum kinase inhibitor staurosporine and the protein kinase C inhibitor bisindoylmaleimide reversed the morphological changes induced by 9-cis-RA. Like treatment with low calcium medium, these inhibitors did not prevent the 9-cis-RA-induced increase in total beta-catenin protein levels, but completely prevented the movement of beta-catenin to the cell membrane. These results point to a role for beta-catenin and serine kinase activity in mediating the action of 9-cis-RA in epithelial differentiation. | lld:pubmed |
| pubmed-article:8754749 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8754749 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8754749 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:8754749 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8754749 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8754749 | pubmed:issn | 0013-7227 | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:ByersSS | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:SpornMM | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:LechleiderRR | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:TozerenAA | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:AnzanoMM | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:PeevGG | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:CrockettCC | lld:pubmed |
| pubmed-article:8754749 | pubmed:author | pubmed-author:PishvaianMM | lld:pubmed |
| pubmed-article:8754749 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8754749 | pubmed:volume | 137 | lld:pubmed |
| pubmed-article:8754749 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8754749 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8754749 | pubmed:pagination | 3265-73 | lld:pubmed |
| pubmed-article:8754749 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:8754749 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8754749 | pubmed:articleTitle | Retinoids increase cell-cell adhesion strength, beta-catenin protein stability, and localization to the cell membrane in a breast cancer cell line: a role for serine kinase activity. | lld:pubmed |
| pubmed-article:8754749 | pubmed:affiliation | Department of Cell Biology, Georgetown University Medical Center, Washington D.C.20007, USA. | lld:pubmed |
| pubmed-article:8754749 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8754749 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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