Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2005-4-25
pubmed:abstractText
Resveratrol, a small molecule found in red wine, is reported to slow aging in simple eukaryotes and has been suggested as a potential calorie restriction mimetic. Resveratrol has also been reported to act as a sirtuin activator, and this property has been proposed to account for its anti-aging effects. We show here that resveratrol is a substrate-specific activator of yeast Sir2 and human SirT1. In particular, we observed that, in vitro, resveratrol enhances binding and deacetylation of peptide substrates that contain Fluor de Lys, a non-physiological fluorescent moiety, but has no effect on binding and deacetylation of acetylated peptides lacking the fluorophore. Consistent with these biochemical data we found that in three different yeast strain backgrounds, resveratrol has no detectable effect on Sir2 activity in vivo, as measured by rDNA recombination, transcriptional silencing near telomeres, and life span. In light of these findings, the mechanism accounting for putative longevity effects of resveratrol should be reexamined.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylase Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Niacinamide, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/SIR2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Silent Information Regulator..., http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 2, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins, http://linkedlifedata.com/resource/pubmed/chemical/Stilbenes, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53, http://linkedlifedata.com/resource/pubmed/chemical/resveratrol
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17038-45
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15684413-Antioxidants, pubmed-meshheading:15684413-Binding, Competitive, pubmed-meshheading:15684413-DNA, Ribosomal, pubmed-meshheading:15684413-Dose-Response Relationship, Drug, pubmed-meshheading:15684413-Fungal Proteins, pubmed-meshheading:15684413-Gene Silencing, pubmed-meshheading:15684413-Histone Deacetylase Inhibitors, pubmed-meshheading:15684413-Histone Deacetylases, pubmed-meshheading:15684413-Humans, pubmed-meshheading:15684413-Kinetics, pubmed-meshheading:15684413-Models, Chemical, pubmed-meshheading:15684413-Niacinamide, pubmed-meshheading:15684413-Peptides, pubmed-meshheading:15684413-Protein Binding, pubmed-meshheading:15684413-Recombination, Genetic, pubmed-meshheading:15684413-Silent Information Regulator Proteins, Saccharomyces..., pubmed-meshheading:15684413-Sirtuin 1, pubmed-meshheading:15684413-Sirtuin 2, pubmed-meshheading:15684413-Sirtuins, pubmed-meshheading:15684413-Stilbenes, pubmed-meshheading:15684413-Substrate Specificity, pubmed-meshheading:15684413-Telomere, pubmed-meshheading:15684413-Time Factors, pubmed-meshheading:15684413-Transcription, Genetic, pubmed-meshheading:15684413-Tumor Suppressor Protein p53
pubmed:year
2005
pubmed:articleTitle
Substrate-specific activation of sirtuins by resveratrol.
pubmed:affiliation
Department of Genome Sciences, University of Washington, Seattle, Washington 98195, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural