Tert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes
Language English Country Czech Republic Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Enzyme Activation drug effects MeSH
- Digitonin MeSH
- Hepatocytes drug effects metabolism MeSH
- Indicators and Reagents MeSH
- Mitochondria, Liver drug effects enzymology MeSH
- Rats MeSH
- NAD metabolism MeSH
- Rats, Wistar MeSH
- Oxygen Consumption drug effects MeSH
- Substrate Specificity MeSH
- In Vitro Techniques MeSH
- tert-Butylhydroperoxide pharmacology MeSH
- Electron Transport drug effects MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Digitonin MeSH
- Indicators and Reagents MeSH
- NAD MeSH
- tert-Butylhydroperoxide MeSH
Sensitivity of various mitochondrial enzymes to oxidative damage was tested on isolated rat liver hepatocytes permeabilized by digitonin. In permeabilized hepatocytes normal respiratory control values were obtained and mitochondrial membranes remained intact. Respiratory rates of NADH-dependent (glutamate + malate, palmitylcarnitine + malate) and flavoprotein-dependent (succinate) substrates were determined in hepatocytes exposed for 5 min to 0.5-3 mM tert-butyl hydroperoxide before addition of digitonin. Our data showed that oxidation of NADH-dependent substrates is much more sensitive to oxidative stress than oxidation of flavoprotein-dependent ones, evidently due to the modification of iron-sulfur clusters or SH groups in the NADH dehydrogenase enzyme complex (Complex I).
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