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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0019643,
umls-concept:C0035696,
umls-concept:C0077063,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0220802,
umls-concept:C0439662,
umls-concept:C0443199,
umls-concept:C0871261,
umls-concept:C1326205,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911684,
umls-concept:C2911692
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pubmed:issue |
3
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pubmed:dateCreated |
1998-7-31
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pubmed:abstractText |
The reversible acetylation of histones by histone deacetylases (HDACs) and acetyltransferases (HATs) plays a fundamental role in gene transcription. We previously showed that HDAC mRNA is upregulated in immune cells upon PHA-induced activation. Little is known, however, about the differential regulation of HDAC mRNAs by the HDAC inhibitors Trichostatin A (TSA) and butyrate, agents known to block proliferation and induce apoptosis. We report that apoptosis-inducing concentrations of TSA and butyrate upregulate the expression of HDAC mRNAs in a differential manner and act synergistically with PHA to induce HDAC expression, suggesting the presence of independent HDAC regulatory mechanisms. Moreover, we show that HDAC inhibitor-induced apoptosis is associated with early abrogation of gamma-IFN production by Th1 lymphocytes and with p53 mRNA downregulation. Our findings highlight the dynamic interplay of cell cycle-, activation- and apoptosis-related proteins in association with time-dependent expression of HDACs and are suggestive of different specific roles for these enzymes.
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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/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Butyric Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Butyric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxamic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phytohemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/trichostatin A
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
833-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9647779-Acetyltransferases,
pubmed-meshheading:9647779-Apoptosis,
pubmed-meshheading:9647779-Butyric Acid,
pubmed-meshheading:9647779-Butyric Acids,
pubmed-meshheading:9647779-CD4-Positive T-Lymphocytes,
pubmed-meshheading:9647779-Cell Cycle,
pubmed-meshheading:9647779-Cell Division,
pubmed-meshheading:9647779-Down-Regulation,
pubmed-meshheading:9647779-Flow Cytometry,
pubmed-meshheading:9647779-Gene Expression Regulation,
pubmed-meshheading:9647779-Genes, p53,
pubmed-meshheading:9647779-Histone Acetyltransferases,
pubmed-meshheading:9647779-Histone Deacetylases,
pubmed-meshheading:9647779-Humans,
pubmed-meshheading:9647779-Hydroxamic Acids,
pubmed-meshheading:9647779-Interferon-gamma,
pubmed-meshheading:9647779-Isoenzymes,
pubmed-meshheading:9647779-Phytohemagglutinins,
pubmed-meshheading:9647779-RNA, Messenger,
pubmed-meshheading:9647779-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9647779-Thymidine,
pubmed-meshheading:9647779-Up-Regulation
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pubmed:year |
1998
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pubmed:articleTitle |
Differential expression of human histone deacetylase mRNAs in response to immune cell apoptosis induction by trichostatin A and butyrate.
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pubmed:affiliation |
Department of Neurology, Harvard Institutes of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusettes 02115, USA. dangond@cnd.bwh.harvard.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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