rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-2-23
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pubmed:abstractText |
Activation-induced cytidine deaminase (AID) is an inducible gene that plays an important role in class switch recombination, somatic hypermutation and gene conversion in B cells. We examined the regulation of AID gene expression in human and mouse B cells by IL-4 and CD40 ligation. IL-4 by itself and, to a much lesser extent, CD40 ligation induced AID mRNA expression in primary B cells. The two stimuli strongly synergized in inducing AID mRNA and protein expression. IL-4 induced STAT6 binding to a site in the 5' upstream region of the AID gene, while CD40 ligation induced NFkappaB binding to two sites in that region. B cells from STAT6-/- mice failed to up-regulate AID in response to IL-4, while B cells from p50-/- mice were impaired in their ability to up-regulate AID in response to CD40 ligation and IL-4. These results suggest that signals delivered via CD40 that activate NFkappaB synergize with signals delivered via the IL-4 receptor that activate STAT6 to induce optimal AID gene expression.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AICDA (activation-induced cytidine...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD40,
http://linkedlifedata.com/resource/pubmed/chemical/Cytidine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/STAT6 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Stat6 protein, mouse,
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 |
0953-8178
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
395-404
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:14978013-Animals,
pubmed-meshheading:14978013-Antigens, CD40,
pubmed-meshheading:14978013-B-Lymphocytes,
pubmed-meshheading:14978013-Binding Sites,
pubmed-meshheading:14978013-Cell Culture Techniques,
pubmed-meshheading:14978013-Cell Line,
pubmed-meshheading:14978013-Cytidine Deaminase,
pubmed-meshheading:14978013-DNA-Binding Proteins,
pubmed-meshheading:14978013-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:14978013-Enzyme Induction,
pubmed-meshheading:14978013-Humans,
pubmed-meshheading:14978013-Interleukin-4,
pubmed-meshheading:14978013-Mice,
pubmed-meshheading:14978013-Mice, Inbred BALB C,
pubmed-meshheading:14978013-NF-kappa B,
pubmed-meshheading:14978013-Promoter Regions, Genetic,
pubmed-meshheading:14978013-RNA, Messenger,
pubmed-meshheading:14978013-STAT6 Transcription Factor,
pubmed-meshheading:14978013-Trans-Activators
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pubmed:year |
2004
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pubmed:articleTitle |
Induction of activation-induced cytidine deaminase gene expression by IL-4 and CD40 ligation is dependent on STAT6 and NFkappaB.
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pubmed:affiliation |
Division of Immunology, Children's Hospital and Department of Pediatrics, Harvard Medical School, Harvard Medical School, Boston, MA 02115, 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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