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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1998-3-6
|
| pubmed:databankReference | |
| pubmed:abstractText |
The nucleosomal histones can be modified through reversible acetylation by histone acetyltransferases (HATs) and deacetylases (HDACs). HATs induce nucleosomal relaxation and allow DNA-binding by transcriptional activators. HDACs from corepressor complexes which negatively regulate cell growth. However, the HDAC inhibitors butyrate and Trichostatin A block T cell proliferation, suggesting that not all effects of HDACs lead to repression. Using mRNA differential display and 5'RACE we isolated human HDAC3, a novel gene that is upregulated in PHA-activated T cell clones. HDAC3 is homologous to other human HDACs and yeast RPD3. In peripheral blood mononuclear cells (PBMCs), activation by PHA, PMA and alpha-CD3 increased HDAC mRNA but no effect was seen with IFN-gamma, LPS, or IL-4. In contrast, GMCSF downregulated PBMC levels of HDAC3 mRNA. All HDACs were found to be ubiquitously expressed in immune and non-immune tissues. In human myeloid leukemia THP-1 cells, HDAC3 transfection resulted in increased size, aberrant nuclear morphology and cell cycle G2/M cell accumulation. Functional activity of the expressed HDAC3 protein was confirmed in alpha-HDAC3 antibody immunoprecipitates by a histone deacetylase assay. Our study suggests the participation of HDACs in cell cycle progression and activation.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Phytohemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/histone deacetylase 3
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
26
|
| pubmed:volume |
242
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
648-52
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9464271-Amino Acid Sequence,
pubmed-meshheading:9464271-Antigens, CD3,
pubmed-meshheading:9464271-Blotting, Northern,
pubmed-meshheading:9464271-Cell Cycle,
pubmed-meshheading:9464271-Cloning, Molecular,
pubmed-meshheading:9464271-DNA,
pubmed-meshheading:9464271-Flow Cytometry,
pubmed-meshheading:9464271-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9464271-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:9464271-Histone Deacetylases,
pubmed-meshheading:9464271-Humans,
pubmed-meshheading:9464271-Molecular Sequence Data,
pubmed-meshheading:9464271-Phylogeny,
pubmed-meshheading:9464271-Phytohemagglutinins,
pubmed-meshheading:9464271-RNA, Messenger,
pubmed-meshheading:9464271-Sequence Alignment,
pubmed-meshheading:9464271-Sequence Analysis, DNA,
pubmed-meshheading:9464271-T-Lymphocytes,
pubmed-meshheading:9464271-Transfection,
pubmed-meshheading:9464271-Tumor Cells, Cultured
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells.
|
| pubmed:affiliation |
Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. dangond@cnd.bwh.harvard.edu
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|