Source:http://linkedlifedata.com/resource/pubmed/id/20497424
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2010-8-27
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pubmed:abstractText |
1. The purpose of the present study was to evaluate differences in the AMP-activated protein kinase (AMPK) phosphorylation sites in cardiac hypertrophy induced by L-thyroxine and angiotensin (Ang) II. 2. Cardiac hypertrophy was induced in wild-type and AMPKalpha2-knockout mice by treatment with 1 mg/kg, i.p., thyroxine or 1.44 mg/kg per day AngII for 14 days. The phenotype of the hypertrophy was evaluated using echocardiographic measurements and histological analyses. The phosphorylation of AMPK at alpha-Ser(485/491) and alpha-Thr(172) was determined by western blot analysis. 3. In wild-type mice, the phosphorylation of AMPKalpha-Ser(485/491) was significantly elevated in the AngII-treated group, but not in the thyroxine-treated group, compared with the vehicle control group. In contrast, the phosphorylation of AMPKalpha-Thr(172) was significantly increased by thyroxine, but not AngII, treatment compared with the vehicle control group. Furthermore, knockout of the AMPKalpha2 subunit abolished phosphorylation at the alpha-Ser(485/491) site and significantly suppressed phosphorylation at the alpha-Thr(172) site, resulting in alleviation of thyroxine- but not AngII-induced hypertrophy. 4. In conclusion, L-thyroxine and AngII induce the phosphorylation of distinct sites of AMPK in cardiac hypertrophy. Phosphorylation of AMPK alpha-Thr(172) may contribute to thyroxine-induced cardiac hypertrophy.
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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/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroxine,
http://linkedlifedata.com/resource/pubmed/chemical/Vasoconstrictor Agents
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1440-1681
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
919-25
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pubmed:meshHeading |
pubmed-meshheading:20497424-AMP-Activated Protein Kinases,
pubmed-meshheading:20497424-Angiotensin II,
pubmed-meshheading:20497424-Animals,
pubmed-meshheading:20497424-Cardiomegaly,
pubmed-meshheading:20497424-Cells, Cultured,
pubmed-meshheading:20497424-Male,
pubmed-meshheading:20497424-Mice,
pubmed-meshheading:20497424-Mice, Inbred C57BL,
pubmed-meshheading:20497424-Mice, Knockout,
pubmed-meshheading:20497424-Myocytes, Cardiac,
pubmed-meshheading:20497424-Phosphorylation,
pubmed-meshheading:20497424-Polymerase Chain Reaction,
pubmed-meshheading:20497424-RNA,
pubmed-meshheading:20497424-Thyroxine,
pubmed-meshheading:20497424-Vasoconstrictor Agents
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pubmed:year |
2010
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pubmed:articleTitle |
A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by L-thyroxine and angiotensin II.
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pubmed:affiliation |
Institute of Vascular Medicine, Peking University Third Hospital and Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Beijing, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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