| Up-regulation of glutathione biosynthesis in NIH3T3 cells transformed with the ETV6-NTRK3 gene fusion. | |
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MedLine Citation:
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PMID: 15750350 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The ETV6-NTRK3 gene fusion, first identified in the chromosomal translocation in congenital fibrosarcoma, encodes a chimeric protein tyrosine kinase with potent transforming activity. ETV6-NTRK3-dependent transformation involves the joint action of NTRK3 signaling pathways, and aberrant cell cycle progression resulting from activation of Mek1 and Akt. The level of glutathione (GSH) was found to be markedly increased in ETV6-NTRK3-transformed NIH3T3 cells. The activities of the two GSH biosynthetic enzymes as well as of glutathione peroxidase, together with their mRNAs, were also higher in the transformed cells. The transformed cells were able to grow in the presence of GSH-depleting agents, whereas the control cells were not. L-Buthionine-(S,R)-sulfoximine (BSO) inhibited activation of Mek1 and Akt in the transformed NIH3T3 cells. These observations imply that up-regulation of GSH biosynthesis plays a central role in ETV6-NTRK3-induced transformation. |
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Authors:
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Su-Jung Kim; Hong-Gyum Kim; Hye-Won Lim; Eun-Hee Park; Chang-Jin Lim |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecules and cells Volume: 19 ISSN: 1016-8478 ISO Abbreviation: Mol. Cells Publication Date: 2005 Feb |
Date Detail:
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Created Date: 2005-03-07 Completed Date: 2005-07-28 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9610936 Medline TA: Mol Cells Country: Korea (South) |
Other Details:
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Languages: eng Pagination: 131-6 Citation Subset: IM |
Affiliation:
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Division of Life Sciences, College of Natural Sciences, Kangwon National University, Chuncheon 200-701, Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Artificial Gene Fusion* Buthionine Sulfoximine / pharmacology Cell Transformation, Viral* DNA-Binding Proteins / genetics* Fibrosarcoma / congenital, metabolism Glutamate-Cysteine Ligase / metabolism Glutathione / biosynthesis* Glutathione Peroxidase / metabolism Glutathione Synthase / metabolism Maleates / pharmacology Mice NIH 3T3 Cells Nuclear Proteins / genetics* Proto-Oncogene Proteins c-ets Receptor, trkC / genetics* Repressor Proteins / genetics* Translocation, Genetic Up-Regulation* |
| Chemical | |
Reg. No./Substance:
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0/DNA-Binding Proteins; 0/ETS translocation variant 6 protein; 0/Maleates; 0/Nuclear Proteins; 0/Proto-Oncogene Proteins c-ets; 0/Repressor Proteins; 141-05-9/diethyl maleate; 5072-26-4/Buthionine Sulfoximine; 70-18-8/Glutathione; EC 1.11.1.9/Glutathione Peroxidase; EC 2.7.10.1/Receptor, trkC; EC 6.3.2.2/Glutamate-Cysteine Ligase; EC 6.3.2.3/Glutathione Synthase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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