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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-2-23
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pubmed:abstractText |
The activation of microsomal glutathione (GSH) S-transferase in isolated rat liver by oxidative stress was investigated using both ischemia/reperfusion and perfusion with hydrogen peroxide. When the isolated liver was reperfused for 30 min and 60 min after 90 min ischemia, microsomal GSH S-transferase activity, but not cytosolic transferase activity, was increased 1.2-fold and 1.3-fold, respectively. In addition, microsomal GSH peroxidase activity was also significantly increased after 60 min reperfusion following ischemia. The increase in microsomal GSH S-transferase activity by ischemia/reperfusion was reversed by dithiothreitol. When N-ethylmaleimide, which activates microsomal GSH S-transferase by covalent binding to the cysteine residue of the enzyme, was incubated with microsomes, transferase activity was increased to 526% in control microsomes and to 399% in liver that underwent ischemia/reperfusion liver. These data indicate that microsomal GSH S-transferase is activated by ischemia/reperfusion of the liver by means of disulfide bond formation. When rats were pretreated with a catalase inhibitor 3-amino-1,2,4-triazole for 6 weeks, microsomal GSH S-transferase activity was increased 1.4-fold by ischemia/reperfusion, corresponding to a 1.8-fold increase as compared to the non-perfused liver of untreated rats. Perfusion of the isolated liver with hydrogen peroxide (1 mM, 15 min) also caused a significant increase in microsomal GSH S-transferase activity with a concomitant decrease in GSH content, confirming that liver microsomal GSH S-transferase in rats was activated in vivo by oxidative stress.
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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/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37-42
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8424821-Animals,
pubmed-meshheading:8424821-Dithiothreitol,
pubmed-meshheading:8424821-Enzyme Activation,
pubmed-meshheading:8424821-Ethylmaleimide,
pubmed-meshheading:8424821-Free Radicals,
pubmed-meshheading:8424821-Glutathione Transferase,
pubmed-meshheading:8424821-Hydrogen Peroxide,
pubmed-meshheading:8424821-Ischemia,
pubmed-meshheading:8424821-Liver,
pubmed-meshheading:8424821-Male,
pubmed-meshheading:8424821-Oxidation-Reduction,
pubmed-meshheading:8424821-Perfusion,
pubmed-meshheading:8424821-Rats,
pubmed-meshheading:8424821-Rats, Sprague-Dawley,
pubmed-meshheading:8424821-Stress, Physiological
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pubmed:year |
1993
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pubmed:articleTitle |
Oxidative stress-induced activation of microsomal glutathione S-transferase in isolated rat liver.
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pubmed:affiliation |
Laboratory of Physiology and Pharmacology, School of Health Sciences, University of the Ryukyus, Okinawa, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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