Source:http://linkedlifedata.com/resource/pubmed/id/20729205
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
43
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| pubmed:dateCreated |
2010-10-18
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| pubmed:abstractText |
Although metabolic conditions associated with an increased AMP/ATP ratio are primary factors in the activation of 5'-adenosine monophosphate-activated protein kinase (AMPK), a number of recent studies have shown that increased intracellular levels of reactive oxygen species can stimulate AMPK activity, even without a decrease in cellular levels of ATP. We found that exposure of recombinant AMPK??? complex or HEK 293 cells to H(2)O(2) was associated with increased kinase activity and also resulted in oxidative modification of AMPK, including S-glutathionylation of the AMPK? and AMPK? subunits. In experiments using C-terminal truncation mutants of AMPK? (amino acids 1-312), we found that mutation of cysteine 299 to alanine diminished the ability of H(2)O(2) to induce kinase activation, and mutation of cysteine 304 to alanine totally abrogated the enhancing effect of H(2)O(2) on kinase activity. Similar to the results obtained with H(2)O(2)-treated HEK 293 cells, activation and S-glutathionylation of the AMPK? subunit were present in the lungs of acatalasemic mice or mice treated with the catalase inhibitor aminotriazole, conditions in which intracellular steady state levels of H(2)O(2) are increased. These results demonstrate that physiologically relevant concentrations of H(2)O(2) can activate AMPK through oxidative modification of the AMPK? subunit. The present findings also imply that AMPK activation, in addition to being a response to alterations in intracellular metabolic pathways, is directly influenced by cellular redox status.
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| pubmed:grant | |
| 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/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Amitrole,
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidants
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
1083-351X
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
22
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| pubmed:volume |
285
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
33154-64
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| pubmed:dateRevised |
2011-10-24
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| pubmed:meshHeading |
pubmed-meshheading:20729205-AMP-Activated Protein Kinases,
pubmed-meshheading:20729205-Acatalasia,
pubmed-meshheading:20729205-Adenosine Monophosphate,
pubmed-meshheading:20729205-Adenosine Triphosphate,
pubmed-meshheading:20729205-Amitrole,
pubmed-meshheading:20729205-Animals,
pubmed-meshheading:20729205-Catalase,
pubmed-meshheading:20729205-Catalytic Domain,
pubmed-meshheading:20729205-Cell Line,
pubmed-meshheading:20729205-Enzyme Induction,
pubmed-meshheading:20729205-Enzyme Inhibitors,
pubmed-meshheading:20729205-Glutathione,
pubmed-meshheading:20729205-Humans,
pubmed-meshheading:20729205-Hydrogen Peroxide,
pubmed-meshheading:20729205-Mice,
pubmed-meshheading:20729205-Mutation,
pubmed-meshheading:20729205-Oxidants,
pubmed-meshheading:20729205-Oxidation-Reduction,
pubmed-meshheading:20729205-Protein Processing, Post-Translational
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| pubmed:year |
2010
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| pubmed:articleTitle |
Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase.
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| pubmed:affiliation |
Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294-0012, USA. zmijewsk@uab.edu
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| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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