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Aspirin Recapitulates Features of Caloric Restriction
F. Pietrocola, F. Castoldi, M. Markaki, S. Lachkar, G. Chen, DP. Enot, S. Durand, N. Bossut, M. Tong, SA. Malik, F. Loos, N. Dupont, G. Mariño, N. Abdelkader, F. Madeo, MC. Maiuri, R. Kroemer, P. Codogno, J. Sadoshima, N. Tavernarakis, G. Kroemer,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
Grantová podpora
P40 OD010440
NIH HHS - United States
NLK
Cell Press Free Archives
od 2012
Directory of Open Access Journals
od 2012
Free Medical Journals
od 2012
Freely Accessible Science Journals
od 2012-01-26
Open Access Digital Library
od 2012-01-26
Open Access Digital Library
od 2012-01-01
- MeSH
- acetylkoenzym A metabolismus MeSH
- Aspirin farmakologie MeSH
- autofagie účinky léků genetika MeSH
- kalorická restrikce * MeSH
- lidé MeSH
- metabolom účinky léků MeSH
- metabolomika MeSH
- myši inbrední C57BL MeSH
- nádorové buněčné linie MeSH
- protein p300 asociovaný s E1A metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
The age-associated deterioration in cellular and organismal functions associates with dysregulation of nutrient-sensing pathways and disabled autophagy. The reactivation of autophagic flux may prevent or ameliorate age-related metabolic dysfunctions. Non-toxic compounds endowed with the capacity to reduce the overall levels of protein acetylation and to induce autophagy have been categorized as caloric restriction mimetics (CRMs). Here, we show that aspirin or its active metabolite salicylate induce autophagy by virtue of their capacity to inhibit the acetyltransferase activity of EP300. While salicylate readily stimulates autophagic flux in control cells, it fails to further increase autophagy levels in EP300-deficient cells, as well as in cells in which endogenous EP300 has been replaced by salicylate-resistant EP300 mutants. Accordingly, the pro-autophagic activity of aspirin and salicylate on the nematode Caenorhabditis elegans is lost when the expression of the EP300 ortholog cpb-1 is reduced. Altogether, these findings identify aspirin as an evolutionary conserved CRM.
BioTechMed Graz Humboldtstraße 50 8010 Graz Austria
Department of Basic Sciences Faculty of Medicine University of Crete Heraklion 70013 Crete Greece
Department of Biochemistry Sargodha Medical College Sargodha Pakistan
Department of Cell Biology and Molecular Medicine Rutgers New Jersey Medical School Newark NJ USA
Gustave Roussy Cancer Campus Villejuif France
Institut Necker Enfants Malades Paris France
Institute of Molecular Biosciences NAWI Graz University of Graz Humboldtstraße 50 8010 Graz Austria
Instituto de Investigación Sanitaria del Principado de Asturias Oviedo Spain
Metabolomics and Cell Biology Platforms Gustave Roussy Cancer Campus Villejuif France
Pôle de Biologie Hôpital Européen Georges Pompidou AP HP Paris France
Scientific Computing LGCR Sanofi R and D 94403 Vitry sur Seine France
Sotio a c Prague Czech Republic
Structure Design and Informatics LGCR Sanofi R and D 94403 Vitry sur Seine France
Université Paris Descartes Paris 5 Sorbonne Paris Cité Paris France
Université Paris Sud Paris XI Faculté de Médecine Kremlin Bicêtre France Paris France
Citace poskytuje Crossref.org
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