| Stabilization of the p53 transformation-related protein in mouse fibrosarcoma cell lines: effects of protein sequence and intracellular environment. | |
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MedLine Citation:
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PMID: 2529426 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The transformation-related protein p53 is normally very labile. The stability of p53 is significantly increased in a number of fibrosarcoma cell lines derived from mouse tumors induced by treatment with physical or chemical agents. In many instances, p53 stabilization is correlated with the ability to form a stable complex with the heat shock protein cognate hsc70. We describe a line in which p53 is very stable yet has no detectable interaction with hsc70. The inability to form such a complex probably resides in the primary structure of the endogenous p53, since introduction of other p53 variants into those cells resulted in the appearance of a p53-hsc70 complex. The factors affecting p53 stability were investigated by stable transfection experiments. The results indicated that the primary structure of the p53 protein is a major determinant of its turnover rate; different p53 variants were degraded at distinct and characteristic rates in a number of transformed cell types. However, at least one p53 variant was degraded differently in nontransformed BALB/c-3T3 than in transformed fibrosarcoma cells, demonstrating that the specific cellular environment can also affect the stability of p53. |
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Authors:
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O Halevy; A Hall; M Oren |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Molecular and cellular biology Volume: 9 ISSN: 0270-7306 ISO Abbreviation: Mol. Cell. Biol. Publication Date: 1989 Aug |
Date Detail:
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Created Date: 1989-11-21 Completed Date: 1989-11-21 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 8109087 Medline TA: Mol Cell Biol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3385-92 Citation Subset: IM |
Affiliation:
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Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Carrier Proteins / metabolism Fibrosarcoma HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins* Heat-Shock Proteins / metabolism Mice Oncogene Proteins / metabolism* Phosphoproteins / metabolism* Plasmids Protein Binding Protein Processing, Post-Translational RNA, Messenger / metabolism Recombinant Proteins / metabolism Single-Strand Specific DNA and RNA Endonucleases Transfection Tumor Cells, Cultured Tumor Suppressor Protein p53 |
| Grant Support | |
ID/Acronym/Agency:
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R01 CA 40099/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/HSC70 Heat-Shock Proteins; 0/HSP70 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Hspa8 protein, mouse; 0/Oncogene Proteins; 0/Phosphoproteins; 0/RNA, Messenger; 0/Recombinant Proteins; 0/Tumor Suppressor Protein p53; EC 3.1.30.1/Single-Strand Specific DNA and RNA Endonucleases |
| Comments/Corrections | |
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