Source:http://linkedlifedata.com/resource/pubmed/id/10692454
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
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| pubmed:dateCreated |
2000-4-3
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| pubmed:abstractText |
In follicular lymphoma, bcl-2 is translocated to the immunoglobulin heavy chain locus leading to deregulation of bcl-2 expression. We examined the role of Myb proteins in the regulation of bcl-2 expression in lymphoma cells. We showed that A-Myb up-regulates bcl-2 promoter activity. Northern and Western analyses demonstrated that A-Myb was expressed in the DHL-4 t(14;18) cell line. In t(14;18) cells and mature B cells, A-Myb up-regulated bcl-2 expression, whereas B- and c-Myb had little effect on bcl-2 gene expression. Deletion analysis of the bcl-2 5'-region identified a region responsive to A-Myb in t(14;18) cells. A potential binding site for the Cdx homeodomain proteins was located in this sequence. Analysis of the A-Myb-responsive region by UV cross-linking experiments revealed that a 32-kDa protein formed a complex with this region, but direct binding by Myb proteins could not be demonstrated. A-Myb could be recovered along with Cdx2 when nuclear extracts were passed over the Cdx site. Mutagenesis of the Cdx binding site abolished binding by the 32-kDa protein and significantly reduced the ability of A-Myb to induce bcl-2 expression. A strong induction of bcl-2 P2 promoter activity was observed in cotransfection studies of DHL-4 cells with the A-Myb and Cdx2 expression vectors, and increased endogenous Bcl-2 protein expression was observed in B cells transfected with A-Myb and/or Cdx2 expression constructs.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cdx-2-3 protein,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MYBL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
275
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6499-508
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:10692454-Animals,
pubmed-meshheading:10692454-B-Lymphocytes,
pubmed-meshheading:10692454-Binding Sites,
pubmed-meshheading:10692454-DNA-Binding Proteins,
pubmed-meshheading:10692454-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:10692454-Homeodomain Proteins,
pubmed-meshheading:10692454-Humans,
pubmed-meshheading:10692454-Lymphoma, Follicular,
pubmed-meshheading:10692454-Mutagenesis,
pubmed-meshheading:10692454-Promoter Regions, Genetic,
pubmed-meshheading:10692454-Proto-Oncogene Proteins,
pubmed-meshheading:10692454-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10692454-RNA, Messenger,
pubmed-meshheading:10692454-Rats,
pubmed-meshheading:10692454-Trans-Activators,
pubmed-meshheading:10692454-Transfection,
pubmed-meshheading:10692454-Translocation, Genetic,
pubmed-meshheading:10692454-Tumor Cells, Cultured,
pubmed-meshheading:10692454-Ultraviolet Rays,
pubmed-meshheading:10692454-Up-Regulation
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| pubmed:year |
2000
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| pubmed:articleTitle |
A-Myb up-regulates Bcl-2 through a Cdx binding site in t(14;18) lymphoma cells.
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| pubmed:affiliation |
Center for Molecular Biology in Medicine, Veterans Affairs Palo Alto Health Care System and the Department of Medicine, Stanford University School of Medicine, Stanford, California 94305, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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