pubmed-article:15657439 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15657439 | lifeskim:mentions | umls-concept:C0021655 | lld:lifeskim |
pubmed-article:15657439 | lifeskim:mentions | umls-concept:C0011847 | lld:lifeskim |
pubmed-article:15657439 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
pubmed-article:15657439 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:15657439 | pubmed:dateCreated | 2005-1-19 | lld:pubmed |
pubmed-article:15657439 | pubmed:abstractText | Pten (phosphatase with tensin homology), a dual-specificity phosphatase, is a negative regulator of the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway. Pten regulates a vast array of biological functions including growth, metabolism, and longevity. Although the PI3K/Akt pathway is a key determinant of the insulin-dependent increase in glucose uptake into muscle and adipose cells, the contribution of this pathway in muscle to whole-body glucose homeostasis is unclear. Here we show that muscle-specific deletion of Pten protected mice from insulin resistance and diabetes caused by high-fat feeding. Deletion of muscle Pten resulted in enhanced insulin-stimulated 2-deoxyglucose uptake and Akt phosphorylation in soleus but, surprisingly, not in extensor digitorum longus muscle compared to littermate controls upon high-fat feeding, and these mice were spared from developing hyperinsulinemia and islet hyperplasia. Muscle Pten may be a potential target for treatment or prevention of insulin resistance and diabetes. | lld:pubmed |
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pubmed-article:15657439 | pubmed:language | eng | lld:pubmed |
pubmed-article:15657439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15657439 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15657439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15657439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15657439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15657439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15657439 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15657439 | pubmed:month | Feb | lld:pubmed |
pubmed-article:15657439 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:KahnC... | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:MakTak WTW | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:SuzukiAkiraA | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:GiaccaAdriaA | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:WooMinnaM | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:EweidaMohamed... | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:KlipAmiraA | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:KonradDanielD | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:JefferiesCrai... | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:WijesekaraNad... | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:LiadisNicoleN | lld:pubmed |
pubmed-article:15657439 | pubmed:author | pubmed-author:CrackowerMike... | lld:pubmed |
pubmed-article:15657439 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15657439 | pubmed:volume | 25 | lld:pubmed |
pubmed-article:15657439 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15657439 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15657439 | pubmed:pagination | 1135-45 | lld:pubmed |
pubmed-article:15657439 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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