| STAT-1-independent upregulation of FADD and procaspase-3 and -8 in cancer cells treated with cytotoxic drugs. | |
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MedLine Citation:
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PMID: 10080945 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have previously shown that treatment by anticancer drugs sensitized tumor cells to Fas (APO-1/CD95)-mediated cell death. The present study demonstrates that the cytotoxic drugs cisplatin, doxorubicin and mitomycin C induce the accumulation of the Fas receptor, the FADD adaptor molecule, the procaspases-8, -3 and -2L and the proapoptotic molecule Bax in several human colon cancer cells. This upregulation is also observed in U3A myeloblastoma cells that do not express STAT-1, a transcription factor involved in the constitutive expression of procaspases. We conclude that anticancer drugs sensitize tumor cells to Fas-mediated cell death by a STAT-1-independent upregulation of molecules involved in this apoptotic pathway. |
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Authors:
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O Micheau; A Hammann; E Solary; M T Dimanche-Boitrel |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 256 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 1999 Mar |
Date Detail:
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Created Date: 1999-04-19 Completed Date: 1999-04-19 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 603-7 Citation Subset: IM |
Copyright Information:
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Copyright 1999 Academic Press. |
Affiliation:
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Department of Biology and Therapy of Cancer (JE 515), Faculty of Medicine and Pharmacy, 7 boulevard Jeanne d'Arc, Dijon Cédex, 21033, France. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing* Antigens, CD95 Antineoplastic Agents / pharmacology* Apoptosis / drug effects Carrier Proteins / genetics, metabolism* Caspase 2 Caspase 3 Caspase 8 Caspase 9 Caspases / metabolism* Cisplatin / pharmacology Colonic Neoplasms / drug therapy, enzymology, genetics, metabolism* DNA-Binding Proteins / genetics, physiology* Dactinomycin / pharmacology Doxorubicin / pharmacology Enzyme Precursors / metabolism* Fas-Associated Death Domain Protein Gene Expression Regulation, Neoplastic / drug effects Humans Isoenzymes / metabolism Mitomycin / pharmacology Poly(ADP-ribose) Polymerases / metabolism Proto-Oncogene Proteins / metabolism Proto-Oncogene Proteins c-bcl-2* RNA, Messenger / metabolism Receptors, Tumor Necrosis Factor / physiology STAT1 Transcription Factor Trans-Activators / genetics, physiology* Transcription, Genetic Tumor Cells, Cultured Up-Regulation / drug effects* bcl-2-Associated X Protein |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/Antigens, CD95; 0/Antineoplastic Agents; 0/BAX protein, human; 0/Carrier Proteins; 0/DNA-Binding Proteins; 0/Enzyme Precursors; 0/FADD protein, human; 0/Fas-Associated Death Domain Protein; 0/Isoenzymes; 0/Proto-Oncogene Proteins; 0/Proto-Oncogene Proteins c-bcl-2; 0/RNA, Messenger; 0/Receptors, Tumor Necrosis Factor; 0/STAT1 Transcription Factor; 0/STAT1 protein, human; 0/Trans-Activators; 0/bcl-2-Associated X Protein; 15663-27-1/Cisplatin; 23214-92-8/Doxorubicin; 50-07-7/Mitomycin; 50-76-0/Dactinomycin; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/CASP8 protein, human; EC 3.4.22.-/CASP9 protein, human; EC 3.4.22.-/Caspase 2; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspase 8; EC 3.4.22.-/Caspase 9; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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