| Activation of heat-shock transcription factor 1 in heated Chinese hamster ovary cells is dependent on the cell cycle and is inhibited by sodium vanadate. | |
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MedLine Citation:
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PMID: 10073666 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Inducible heat-shock protein 70 (HSP72) is expressed in a cell cycle-specific manner in Chinese hamster ovary (CHO) cells after heating for 15 min at 45.0 degrees C, with the highest level in S-phase cells. Since heat shock induces the transcription of heat-shock proteins through the transactivation of heat-shock elements (HSEs) by heat-shock factor HSF1, we wished to determine whether the cell cycle-specific expression of HSP72 was regulated at the level of transcription. The levels of HSF1 did not vary through the cell cycle, as measured by polyclonal antibodies and flow cytometry. The binding of HSF1 to the heat-shock element was measured with the gel mobility shift assay using cell extracts from Hoechst 33342-labeled heated cells sorted from G1, S and G2/M phases. The HSF1-HSE binding activity was twofold higher in S phase than in G1 or G2/M phase. When CHO cells were exposed to 10 microM sodium vanadate, an inhibitor of tyrosine phosphatase, for 24 h before heat shock, the binding of HSF1 to HSE was reduced by a factor of 2 and the level of HSP72 was greatly reduced. The HSF1 binding to HSE was completely eliminated by using anti-HSF1 antibody in the gel mobility shift assays. Antibodies against HSP73 did not reduce the HSF1-HSE binding activity, but antibodies against HSP40 actually increased the binding activity. These results support the hypothesis that cell cycle-dependent binding of HSF1 to HSE is the cause of the cell cycle-specific expression of HSP72 in heated CHO cells and is regulated by phosphorylation. |
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Authors:
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L He; M H Fox |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Radiation research Volume: 151 ISSN: 0033-7587 ISO Abbreviation: Radiat. Res. Publication Date: 1999 Mar |
Date Detail:
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Created Date: 1999-03-25 Completed Date: 1999-03-25 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0401245 Medline TA: Radiat Res Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 283-92 Citation Subset: IM; S |
Affiliation:
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Department of Radiological Health Sciences, Colorado State University, Fort Collins 80523, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Base Sequence CHO Cells Cell Cycle / physiology* Cricetinae DNA-Binding Proteins / metabolism* HSP72 Heat-Shock Proteins Heat-Shock Proteins / metabolism* Hela Cells Hot Temperature Humans Oligodeoxyribonucleotides / genetics, metabolism Transcription Factors / metabolism* Vanadates / pharmacology |
| Grant Support | |
ID/Acronym/Agency:
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CA25636/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/DNA-Binding Proteins; 0/HSP72 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Oligodeoxyribonucleotides; 0/Transcription Factors; 0/Vanadates; 0/heat shock transcription factor |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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