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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3-4
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pubmed:dateCreated |
2011-4-7
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pubmed:abstractText |
Mitochondrial dysfunction plays important roles in the development of diabetes. Elevated nitric oxide (NO) synthase inhibitor asymmetric dimethylarginine (ADMA) has been shown to be closely related to diabetes. But the relationship between them in diabetes has not been determined. This study was to explore the role of ADMA in hepatic mitochondrial dysfunction and its potential mechanisms in diabetic rats and hepatocytes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Malondialdehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N,N-dimethylarginine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Ppargc1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial uncoupling protein 2
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pubmed:status |
MEDLINE
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pubmed:issn |
1421-9778
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 S. Karger AG, Basel.
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pubmed:issnType |
Electronic
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
341-52
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pubmed:meshHeading |
pubmed-meshheading:21471723-Adenosine Triphosphate,
pubmed-meshheading:21471723-Animals,
pubmed-meshheading:21471723-Arginine,
pubmed-meshheading:21471723-Cell Line, Tumor,
pubmed-meshheading:21471723-Diabetes Mellitus, Experimental,
pubmed-meshheading:21471723-Enzyme Inhibitors,
pubmed-meshheading:21471723-Hepatocytes,
pubmed-meshheading:21471723-Ion Channels,
pubmed-meshheading:21471723-Liver,
pubmed-meshheading:21471723-Male,
pubmed-meshheading:21471723-Malondialdehyde,
pubmed-meshheading:21471723-Membrane Potential, Mitochondrial,
pubmed-meshheading:21471723-Mitochondria, Liver,
pubmed-meshheading:21471723-Mitochondrial Proteins,
pubmed-meshheading:21471723-Nitric Oxide,
pubmed-meshheading:21471723-Nitric Oxide Synthase,
pubmed-meshheading:21471723-Oxidative Stress,
pubmed-meshheading:21471723-RNA-Binding Proteins,
pubmed-meshheading:21471723-Rats,
pubmed-meshheading:21471723-Rats, Sprague-Dawley,
pubmed-meshheading:21471723-Superoxide Dismutase,
pubmed-meshheading:21471723-Transcription Factors
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pubmed:year |
2011
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pubmed:articleTitle |
Contribution of endogenous inhibitor of nitric oxide synthase to hepatic mitochondrial dysfunction in streptozotocin-induced diabetic rats.
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pubmed:affiliation |
Department of Pharmacology, Guangzhou Medical University, Guangzhou, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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