Source:http://linkedlifedata.com/resource/pubmed/id/16377306
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-12-26
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pubmed:abstractText |
AMP-activated protein kinase (AMPK) is a metabolic master switch regulating glucose and lipid metabolism. Recently, AMPK has been implicated in the control of adipose tissue content. Yet, the nature of this action is controversial. We examined the effect on F442a adipocytes of the AMPK activator-AICAR. Activation of AMPK induced dose-dependent apoptotic cell death, inhibition of lipolysis, and downregulatation key adipogenic genes, such as peroxisome proliferator-activated receptor (PPARgamma) and CCAAT/enhancer-binding protein alpha (C/EBPalpha). We have identified the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) as a target gene which is phosphorylated following AICAR treatment. Such phosphorylation is one of the best-characterized mechanisms for downregulating protein synthesis. 2-Aminopurine (2-AP), an inhibitor of eIF2alpha kinases, could overcome the apoptotic effect of AICAR, abolishing the reduction of PPARgamma and C/EBPalpha and the lipolytic properties of AMPK. Thus, AMPK may diminish adiposity via reduction of fat cell number through eIF2alpha-dependent translation shutdown.
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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/AICA ribonucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminoimidazole Carboxamide,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
340
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43-7
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16377306-AMP-Activated Protein Kinases,
pubmed-meshheading:16377306-Adipocytes,
pubmed-meshheading:16377306-Adipogenesis,
pubmed-meshheading:16377306-Aminoimidazole Carboxamide,
pubmed-meshheading:16377306-Animals,
pubmed-meshheading:16377306-Apoptosis,
pubmed-meshheading:16377306-Cell Line,
pubmed-meshheading:16377306-Enzyme Activation,
pubmed-meshheading:16377306-Eukaryotic Initiation Factor-2,
pubmed-meshheading:16377306-Lipolysis,
pubmed-meshheading:16377306-Mice,
pubmed-meshheading:16377306-Multienzyme Complexes,
pubmed-meshheading:16377306-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16377306-Ribonucleotides
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pubmed:year |
2006
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pubmed:articleTitle |
AMPK activation regulates apoptosis, adipogenesis, and lipolysis by eIF2alpha in adipocytes.
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pubmed:affiliation |
Department of Human Nutrition and Metabolism, Braun School of Public Health, Faculty of Medicine, Hebrew University, Hadassah Medical School, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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