Source:http://linkedlifedata.com/resource/pubmed/id/17825817
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
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pubmed:dateCreated |
2007-10-1
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pubmed:abstractText |
Changes to the translational machinery that occur during apoptosis have been described in the last few years. The two principal ways in which translational factors are modified during apoptosis are: (i) changes in protein phosphorylation and (ii) specific proteolytic cleavages. Taxol, a member of a new class of anti-tubulin drugs, is currently used in chemotherapeutic treatments of different types of cancers. We have previously demonstrated that taxol induces calpain-mediated apoptosis in NIH3T3 cells [Piñeiro et al., Exp. Cell Res., 2007, 313:369-379]. In this study we found that translation was significantly inhibited during taxol-induced apoptosis in these cells. We have studied the phosphorylation status and expression levels of eIF2a, eIF4E, eIF4G and the regulatory protein 4E-BP1, all of which are implicated in translation regulation. We found that taxol treatment did not induce changes in eIF2alpha phosphorylation, but strongly decreased eIF4G, eIF4E and 4E-BP1 expression levels. MDL28170, a specific inhibitor of calpain, prevented reduction of eIF4G, but not of eIF4E or 4E-BP1 levels. Moreover, the calpain inhibitor did not block taxol-induced translation inhibition. All together these findings demonstrated that none of these factors are responsible for the taxol-induced protein synthesis inhibition. On the contrary, taxol treatment increased elongation factor eEF2 phosphorylation in a calpain-independent manner, supporting a role for eEF2 in taxol-induced translation inhibition.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, Phytogenic,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Eif4ebp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4E,
http://linkedlifedata.com/resource/pubmed/chemical/Paclitaxel,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
313
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3694-706
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pubmed:meshHeading |
pubmed-meshheading:17825817-Adenosine Triphosphate,
pubmed-meshheading:17825817-Animals,
pubmed-meshheading:17825817-Antineoplastic Agents, Phytogenic,
pubmed-meshheading:17825817-Apoptosis,
pubmed-meshheading:17825817-Calpain,
pubmed-meshheading:17825817-Carrier Proteins,
pubmed-meshheading:17825817-Caspase 3,
pubmed-meshheading:17825817-Eukaryotic Initiation Factor-4E,
pubmed-meshheading:17825817-Mice,
pubmed-meshheading:17825817-NIH 3T3 Cells,
pubmed-meshheading:17825817-Paclitaxel,
pubmed-meshheading:17825817-Peptide Elongation Factor 2,
pubmed-meshheading:17825817-Phosphoproteins,
pubmed-meshheading:17825817-Phosphorylation,
pubmed-meshheading:17825817-Protein Biosynthesis,
pubmed-meshheading:17825817-RNA, Messenger
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pubmed:year |
2007
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pubmed:articleTitle |
Translation regulation after taxol treatment in NIH3T3 cells involves the elongation factor (eEF)2.
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pubmed:affiliation |
Departamento de Bioquímica-Investigación, Hospital Ramón y Cajal, 28034 Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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