Source:http://linkedlifedata.com/resource/pubmed/id/17016429
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0012860,
umls-concept:C0031715,
umls-concept:C0752312,
umls-concept:C0871261,
umls-concept:C1334497,
umls-concept:C1370600,
umls-concept:C1424650,
umls-concept:C1428048,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704632,
umls-concept:C1705376,
umls-concept:C1706817,
umls-concept:C2911692
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| pubmed:issue |
16
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| pubmed:dateCreated |
2007-4-5
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| pubmed:abstractText |
We discovered a novel oncogene in a T-cell lymphoma cell line, multiple copies in T-cell lymphoma-1 (MCT-1), that has been shown to decrease cell-doubling time, shorten the duration of G(1) transit time and/or G(1)-S transition, and transform NIH3T3 fibroblasts. We subsequently demonstrated that there were significantly increased levels of MCT-1 protein in a subset of primary diffuse large B-cell lymphomas. Levels of MCT-1 protein were shown to be increased after exposure to DNA damaging agents. This increase did not require new protein synthesis, suggesting that post-translational mechanisms were involved. Phosphorylation is one potential mechanism by which the activity of molecules involved in cell cycle/survival is rapidly modulated. The RAS/mitogen-activated/extracellular-regulated kinase (MEK)/extracellular signal-regulated kinases (ERK) pathway plays a prominent role in the regulation of cell growth and proliferation through phosphorylation-dependent regulation of several substrates. The MCT-1 protein is predicted to have numerous putative phosphorylation sites. Using a combination of genetic and pharmacological approaches, we established that phosphorylation of MCT-1 protein by p44/p42 mitogen-activated protein kinases is critical for stabilization of MCT-1 protein and for its ability to promote cell proliferation. Our data suggests that targeting the RAS/MEK/ERK signal transduction cascade may provide a potential therapeutic approach in lymphomas and related malignancies that exhibit high levels of MCT-1 protein.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MCTS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0950-9232
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
5
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| pubmed:volume |
26
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2283-9
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:17016429-3T3 Cells,
pubmed-meshheading:17016429-Amino Acid Sequence,
pubmed-meshheading:17016429-Animals,
pubmed-meshheading:17016429-Cell Cycle,
pubmed-meshheading:17016429-Cell Cycle Proteins,
pubmed-meshheading:17016429-Cell Division,
pubmed-meshheading:17016429-Cell Line, Tumor,
pubmed-meshheading:17016429-Cell Survival,
pubmed-meshheading:17016429-DNA Damage,
pubmed-meshheading:17016429-Humans,
pubmed-meshheading:17016429-Jurkat Cells,
pubmed-meshheading:17016429-Kinetics,
pubmed-meshheading:17016429-Lymphoma, T-Cell,
pubmed-meshheading:17016429-Mice,
pubmed-meshheading:17016429-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:17016429-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:17016429-Molecular Sequence Data,
pubmed-meshheading:17016429-Oncogene Proteins,
pubmed-meshheading:17016429-Phosphorylation
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| pubmed:year |
2007
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| pubmed:articleTitle |
Phosphorylation of MCT-1 by p44/42 MAPK is required for its stabilization in response to DNA damage.
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| pubmed:affiliation |
Department of Medicine, University of California, San Diego, La Jolla, CA, USA.
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| pubmed:publicationType |
Journal Article
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