| pubmed-article:7638205 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0023487 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0035339 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0162768 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:7638205 | lifeskim:mentions | umls-concept:C2346501 | lld:lifeskim |
| pubmed-article:7638205 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:7638205 | pubmed:dateCreated | 1995-9-11 | lld:pubmed |
| pubmed-article:7638205 | pubmed:abstractText | The t(15;17) chromosomal translocation, specific for acute promyelocytic leukemia (APL), fuses the PML gene to the retinoic acid receptor alpha (RAR alpha) gene, resulting in expression of a PML-RAR alpha hybrid protein. In this report, we analyzed the nature of PML-RAR alpha-containing complexes in nuclear protein extracts of t(15;17)-positive cells. We show that endogenous PML-RAR alpha can bind to DNA as a homodimer, in contrast to RAR alpha that requires the retinoid X receptor (RXR) dimerization partner. In addition, these cells contain oligomeric complexes of PML-RAR alpha and endogenous RXR. Treatment with retinoic acid results in a decrease of PML-RAR alpha protein levels and, as a consequence, of DNA binding by the different complexes. Using responsive elements from various hormone signaling pathways, we show that PML-RAR alpha homodimers have altered DNA-binding characteristics when compared to RAR alpha-RXR alpha heterodimers. In transfected Drosophila SL-3 cells that are devoid of endogenous retinoid receptors PML-RAR alpha inhibits transactivation by RAR alpha-RXR alpha heterodimers in a dominant fashion. In addition, we show that both normal retinoid receptors and the PML-RAR alpha hybrid bind and activate the peroxisome proliferator-activated receptor responsive element from the Acyl-CoA oxidase gene, indicating that retinoids and peroxisome proliferator receptors may share common target genes. These properties of PML-RAR alpha may contribute to the transformed phenotype of APL cells. | lld:pubmed |
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| pubmed-article:7638205 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7638205 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7638205 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7638205 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7638205 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:WahliWW | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:MahfoudiAA | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:JansenJ HJH | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:DejeanAA | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:RambaudSS | lld:pubmed |
| pubmed-article:7638205 | pubmed:author | pubmed-author:LavauCC | lld:pubmed |
| pubmed-article:7638205 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7638205 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7638205 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:7638205 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7638205 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7638205 | pubmed:pagination | 7401-5 | lld:pubmed |
| pubmed-article:7638205 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7638205 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7638205 | pubmed:articleTitle | Multimeric complexes of the PML-retinoic acid receptor alpha fusion protein in acute promyelocytic leukemia cells and interference with retinoid and peroxisome-proliferator signaling pathways. | lld:pubmed |
| pubmed-article:7638205 | pubmed:affiliation | Unité de Recombinaison et Expression Génétique, Institut National de la Santé et de la Recherche Médicale (U.163), Institut Pasteur, Paris, France. | lld:pubmed |
| pubmed-article:7638205 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7638205 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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