| pubmed-article:17681146 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C1333572 | lld:lifeskim |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C0001038 | lld:lifeskim |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C1420071 | lld:lifeskim |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C1159884 | lld:lifeskim |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C1511737 | lld:lifeskim |
| pubmed-article:17681146 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:17681146 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17681146 | pubmed:dateCreated | 2007-8-7 | lld:pubmed |
| pubmed-article:17681146 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:abstractText | The family of mammalian Sirtuin proteins comprises seven members homologous to yeast Sir2. Here we show that SIRT2, a cytoplasmic sirtuin, is the most abundant sirtuin in adipocytes. Sirt2 expression is downregulated during preadipocyte differentiation in 3T3-L1 cells. Overexpression of SIRT2 inhibits differentiation, whereas reducing SIRT2 expression promotes adipogenesis. Both effects are accompanied by corresponding changes in the expression of PPARgamma, C/EBPalpha, and genes marking terminal adipocyte differentiation, including Glut4, aP2, and fatty acid synthase. The mechanism underlying the effects of reduced SIRT2 in 3T3-L1 adipocytes includes increased acetylation of FOXO1, with direct interaction between SIRT2 and FOXO1. This interaction enhances insulin-stimulated phosphorylation of FOXO1, which in turn regulates FOXO1 nuclear and cytosolic localization. Thus, Sirt2 acts as an important regulator of adipocyte differentiation through modulation of FOXO1 acetylation/phosphorylation and activity and may play a role in controlling adipose tissue mass and function. | lld:pubmed |
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| pubmed-article:17681146 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17681146 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17681146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17681146 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17681146 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17681146 | pubmed:issn | 1550-4131 | lld:pubmed |
| pubmed-article:17681146 | pubmed:author | pubmed-author:KahnC... | lld:pubmed |
| pubmed-article:17681146 | pubmed:author | pubmed-author:JingEnxuanE | lld:pubmed |
| pubmed-article:17681146 | pubmed:author | pubmed-author:GestaStephane... | lld:pubmed |
| pubmed-article:17681146 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17681146 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:17681146 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17681146 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17681146 | pubmed:pagination | 105-14 | lld:pubmed |
| pubmed-article:17681146 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:17681146 | pubmed:year | 2007 | lld:pubmed |
