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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5 Pt 1
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pubmed:dateCreated |
1991-6-24
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pubmed:abstractText |
Although nitric oxide (.N = O) biosynthesis is inducible in rat hepatocytes (HC), the physiological significance of .N = O production by these cells is unknown. Short exposure of HC to authentic .N = O led to a concentration-dependent inhibition of mitochondrial aconitase, NADH-ubiquinone oxidoreductase, and succinate-ubiquinone oxidoreductase (complexes I and II of the mitochondrial electron transport chain). Most susceptible to .N = O inhibition was mitochondrial aconitase, in which a reduction in enzyme activity to 20.2 +/- 1.6% of control was observed. In contrast to mitochondrial aconitase, cytosolic aconitase activity was not inhibited by .N = O. After exposure to a maximal inhibitory concentration of .N = O, mitochondrial aconitase activity recovered completely within 6 h. Complex I did not fully recover within this incubation period. Endogenous .N = O biosynthesis was induced in HC by a specific combination of cytokines and lipopolysaccharide. After 18 h of incubation with these stimuli, a significant inhibition of mitochondrial aconitase activity to 70.8 +/- 2.4% of controls was detected. However, this was due only in part to the action of .N = O. A non- .N = O-dependent inhibition of mitochondrial function appeared to be mediated by tumor necrosis factor.
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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/Electron Transport Complex II,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinone Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Succinate Dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C910-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1903597-Animals,
pubmed-meshheading:1903597-Cells, Cultured,
pubmed-meshheading:1903597-Electron Transport Complex II,
pubmed-meshheading:1903597-Kinetics,
pubmed-meshheading:1903597-Male,
pubmed-meshheading:1903597-Mitochondria, Liver,
pubmed-meshheading:1903597-Multienzyme Complexes,
pubmed-meshheading:1903597-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:1903597-Nitric Oxide,
pubmed-meshheading:1903597-Oxidoreductases,
pubmed-meshheading:1903597-Oxygen Consumption,
pubmed-meshheading:1903597-Protein Biosynthesis,
pubmed-meshheading:1903597-Quinone Reductases,
pubmed-meshheading:1903597-Rats,
pubmed-meshheading:1903597-Rats, Inbred Strains,
pubmed-meshheading:1903597-Succinate Dehydrogenase
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pubmed:year |
1991
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pubmed:articleTitle |
Effect of exogenous and endogenous nitric oxide on mitochondrial respiration of rat hepatocytes.
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pubmed:affiliation |
Department of Surgery, University of Pittsburgh, Pennsylvania 15261.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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