| pubmed-article:15121858 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0245382 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0887840 | lld:lifeskim |
| pubmed-article:15121858 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15121858 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:15121858 | pubmed:dateCreated | 2004-5-3 | lld:pubmed |
| pubmed-article:15121858 | pubmed:abstractText | Galectin-3 (Gal-3), a member of the beta-galactoside binding protein family containing the NWGR antideath motif of the Bcl-2 protein family, is involved in various aspects of cancer progression. Previously, it has been shown that the antiapoptotic activity of Gal-3 is regulated by the phosphorylation at Ser(6) by casein kinase 1 (CK1). Here we questioned how phosphorylation at Ser(6) regulates Gal-3 function. We have generated serine-to-alanine (S6A) and serine-to-glutamic acid (S6E) Gal-3 mutants and transfected them into the BT-549 human breast carcinoma cell line, which does not express Gal-3. BT-549 cell clones expressing wild-type (wt) and mutant Gal-3 were exposed to chemotherapeutic anticancer drugs. In response to the apoptotic insults, phosphorylated wt Gal-3 was exported from the nucleus to the cytoplasm and protected the BT-549 cells from drug-induced apoptosis while nonphosphorylated mutant Gal-3 neither was exported from the nucleus nor protected BT-549 cells from drug-induced apoptosis. Furthermore, leptomycin B, a nuclear export inhibitor, increased the cisplatin-induced apoptosis of Gal-3 expressing BT-549 cells. These results suggest that Ser(6) phosphoryaltion acts as a molecular switch for its cellular translocation from the nucleus to the cytoplasm and, as a result, regulates the antiapoptotic activity of Gal-3. | lld:pubmed |
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| pubmed-article:15121858 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15121858 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15121858 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15121858 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15121858 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15121858 | pubmed:month | May | lld:pubmed |
| pubmed-article:15121858 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:YoshiiTadashi... | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:FukumoriTomoh... | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:InoharaHideno... | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:KimHyeong-Reh... | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:RazAvrahamA | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:BresalierRobe... | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:OkaNatsuoN | lld:pubmed |
| pubmed-article:15121858 | pubmed:author | pubmed-author:TakenakaYukin... | lld:pubmed |
| pubmed-article:15121858 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15121858 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:15121858 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15121858 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15121858 | pubmed:pagination | 4395-406 | lld:pubmed |
| pubmed-article:15121858 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
