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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2010-5-17
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pubmed:abstractText |
Carbonic anhydrase IX (CAIX) plays an important role in the growth and survival of tumor cells. MORC2 is a member of the MORC protein family. The MORC proteins contain a CW-type zinc finger domain and are predicted to have the function of regulating transcription, but no MORC2 target genes have been identified. Here we performed a DNA microarray hybridization and found CAIX mRNA to be down-regulated 8-fold when MORC2 was overexpressed. This result was further confirmed by northern and western blot analysis. Our results also showed that the protected region 4 (PR4) was important for the repression function of MORC2. Moreover, MORC2 decreased the acetylation level of histone H3 at the CAIX promoter. Meanwhile, trichostatin A (TSA) had an increasing effect on CAIX promoter activity. Among the six HDACs tested, histone deacetylase 4 (HDAC4) had a much more prominent effect on CAIX repression. ChIP and ChIP Re-IP assays showed that MORC2 and HDAC4 were assembled on the same region of the CAIX promoter. Importantly, we further confirmed that both proteins are simultaneously present in the PR4-binding complex. These results may contribute to understanding the molecular mechanisms of CAIX regulation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-10369865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-10551812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-10708480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-11156414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-11431368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-11504747,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-11672442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12137853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12384800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12454846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12532423,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12615703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-12854129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-14607086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-14712082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-15184875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-15199132,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-17608765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-18346280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-19075001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-19165203,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20110259-9230182
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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/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CA9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrases,
http://linkedlifedata.com/resource/pubmed/chemical/HDAC4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2813-24
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pubmed:dateRevised |
2010-9-28
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pubmed:meshHeading |
pubmed-meshheading:20110259-Antigens, Neoplasm,
pubmed-meshheading:20110259-Binding Sites,
pubmed-meshheading:20110259-Carbonic Anhydrases,
pubmed-meshheading:20110259-Cell Line,
pubmed-meshheading:20110259-Down-Regulation,
pubmed-meshheading:20110259-Gene Knockdown Techniques,
pubmed-meshheading:20110259-Histone Deacetylases,
pubmed-meshheading:20110259-Humans,
pubmed-meshheading:20110259-Promoter Regions, Genetic,
pubmed-meshheading:20110259-RNA, Messenger,
pubmed-meshheading:20110259-Repressor Proteins,
pubmed-meshheading:20110259-Transcription Factors
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pubmed:year |
2010
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pubmed:articleTitle |
Involvement of histone deacetylation in MORC2-mediated down-regulation of carbonic anhydrase IX.
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pubmed:affiliation |
Department of Cell Biology, Key Laboratory of Cell Biology, Ministry of Public Health, and Key Laboratory of Medical Cell Biology, Ministry of Education, China Medical University, Shenyang 110001, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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