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https://hdl.handle.net/2440/34690
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DC Field | Value | Language |
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dc.contributor.author | Butler, L. | - |
dc.contributor.author | Zhou, X. | - |
dc.contributor.author | Marks, P. | - |
dc.contributor.author | Rifkind, R. | - |
dc.contributor.author | Richon, V. | - |
dc.date.issued | 2002 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of USA, 2002; 99(18):11700-11705 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.issn | 1091-6490 | - |
dc.identifier.uri | http://hdl.handle.net/2440/34690 | - |
dc.description | Copyright © 2002 by the National Academy of Sciences | - |
dc.description.abstract | Suberoylanilide hydroxamic acid (SAHA) is a potent inhibitor of histone deacetylases (HDACs) that causes growth arrest, differentiation, and/or apoptosis of many tumor types in vitro and in vivo. SAHA is in clinical trials for the treatment of cancer. HDAC inhibitors induce the expression of less than 2% of genes in cultured cells. In this study we show that SAHA induces the expression of vitamin D-up-regulated protein 1/thioredoxin-binding protein-2 (TBP-2) in transformed cells. As the expression of TBP-2 mRNA is increased, the expression of a second gene, thioredoxin, is decreased. In transient transfection assays, HDAC inhibitors induce TBP-2 promoter constructs, and this induction requires an NF-Y binding site. We report here that TBP-2 expression is reduced in human primary breast and colon tumors compared with adjacent tissue. These results support a model in which the expression of a subset of genes (i.e., including TBP-2) is repressed in transformed cells, leading to a block in differentiation, and culture of transformed cells with SAHA causes re-expression of these genes, leading to induction of growth arrest, differentiation, and/or apoptosis. | - |
dc.description.statementofresponsibility | Lisa M. Butler, Xianbo Zhou, Wei-Sheng Xu, Howard I. Scher, Richard A. Rifkind, Paul A. Marks, and Victoria M. Richon | - |
dc.language.iso | en | - |
dc.publisher | Natl Acad Sciences | - |
dc.source.uri | http://dx.doi.org/10.1073/pnas.182372299 | - |
dc.subject | Tumor Cells, Cultured | - |
dc.subject | Humans | - |
dc.subject | Neoplasms | - |
dc.subject | Hydroxamic Acids | - |
dc.subject | Carrier Proteins | - |
dc.subject | RNA, Messenger | - |
dc.subject | DNA Primers | - |
dc.subject | Enzyme Inhibitors | - |
dc.subject | Cloning, Molecular | - |
dc.subject | Cell Division | - |
dc.subject | Apoptosis | - |
dc.subject | Down-Regulation | - |
dc.subject | Up-Regulation | - |
dc.subject | Base Sequence | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Thioredoxins | - |
dc.subject | Histone Deacetylase Inhibitors | - |
dc.subject | Vorinostat | - |
dc.title | The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1073/pnas.182372299 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Butler, L. [0000-0003-2698-3220] | - |
Appears in Collections: | Aurora harvest 6 Medicine publications |
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