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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2006-6-5
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pubmed:abstractText |
14-3-3sigma is an epithelial marker whose expression is induced by DNA damage through a p53-dependent pathway. 14-3-3sigma functions sequesters cyclin B1-CDC2 complexes outside the nucleus and thereby contributes to a G2 arrest. Down-regulation or lack of 14-3-3sigma is a frequent event in breast and prostate cancers. Epigenetic silencing by CpG methylation, p53 inactivation, and proteasome-dependent proteolysis leads to loss of 14-3-3sigma. Hypermethylation of the 14-3-3sigma gene is often observed in precancerous lesions and likely to be causally linked to the onset of cancer. Proteolytic inactivation of 14-3-3sigma has been recently found in breast and prostate cancers. In breast cancer, the estrogen-responsive E3 ubiquitin ligase Efp specifically targets 14-3-3sigma for degradation. The E2 ubiquitin conjugating enzyme UBC8 and Efp also mediates ISG15 modification of 14-3-3sigma. Detection of 14-3-3sigma inactivation on the protein or DNA methylation level may be used for cancer prognosis. Furthermore, 14-3-3sigma may be a potential therapeutic target in breast and prostate cancer.
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/ISG15 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/SFN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TRIM25 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1044-579X
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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 |
235-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16682214-14-3-3 Proteins,
pubmed-meshheading:16682214-Breast Neoplasms,
pubmed-meshheading:16682214-Cytokines,
pubmed-meshheading:16682214-DNA Damage,
pubmed-meshheading:16682214-DNA Methylation,
pubmed-meshheading:16682214-DNA-Binding Proteins,
pubmed-meshheading:16682214-Epigenesis, Genetic,
pubmed-meshheading:16682214-Exonucleases,
pubmed-meshheading:16682214-Female,
pubmed-meshheading:16682214-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:16682214-Gene Silencing,
pubmed-meshheading:16682214-Humans,
pubmed-meshheading:16682214-Male,
pubmed-meshheading:16682214-Neoplasm Proteins,
pubmed-meshheading:16682214-Prostatic Neoplasms,
pubmed-meshheading:16682214-Proteasome Endopeptidase Complex,
pubmed-meshheading:16682214-Transcription Factors,
pubmed-meshheading:16682214-Tumor Markers, Biological,
pubmed-meshheading:16682214-Tumor Suppressor Protein p53,
pubmed-meshheading:16682214-Ubiquitin-Protein Ligases,
pubmed-meshheading:16682214-Ubiquitins
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pubmed:year |
2006
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pubmed:articleTitle |
Epigenetic and proteolytic inactivation of 14-3-3sigma in breast and prostate cancers.
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pubmed:affiliation |
Research Center for Genomic Medicine and Department of Molecular Biology, Saitama Medical School, Hidaka-shi, Japan.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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