High efficiency of ROS production by glycerophosphate dehydrogenase in mammalian mitochondria
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18952046
DOI
10.1016/j.abb.2008.10.011
PII: S0003-9861(08)00476-1
Knihovny.cz E-resources
- MeSH
- Antimycin A pharmacology MeSH
- Glycerolphosphate Dehydrogenase metabolism MeSH
- Adipose Tissue, Brown metabolism MeSH
- Mitochondria, Liver drug effects metabolism MeSH
- Cricetinae MeSH
- Rats MeSH
- Succinic Acid metabolism MeSH
- Pyruvic Acid metabolism MeSH
- Mitochondria drug effects metabolism MeSH
- Brain metabolism MeSH
- Hydrogen Peroxide metabolism MeSH
- Rats, Wistar MeSH
- Reactive Oxygen Species metabolism MeSH
- Electron Transport Complex III metabolism MeSH
- Mitochondria, Heart drug effects metabolism MeSH
- In Vitro Techniques MeSH
- Electron Transport MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antimycin A MeSH
- Glycerolphosphate Dehydrogenase MeSH
- Succinic Acid MeSH
- Pyruvic Acid MeSH
- Hydrogen Peroxide MeSH
- Reactive Oxygen Species MeSH
- Electron Transport Complex III MeSH
We investigated hydrogen peroxide production in mitochondria with low (liver, heart, brain) and high (brown adipose tissue, BAT) content of glycerophosphate dehydrogenase (mGPDH). ROS production at state 4 due to electron backflow from mGPDH was low, but after inhibition of electron transport with antimycin A high rates of mGPDH-dependent ROS production were observed in liver, heart and brain mitochondria. When this ROS production was related to activity of mGPDH, many-fold higher ROS production was found in contrast to succinate- (39-, 28-, 3-fold) or pyruvate plus malate-dependent ROS production (32-, 96-, 5-fold). This specific rate of mGPDH-dependent ROS production was also exceedingly higher (28-, 66-, 22-fold) compared to that in BAT. mGPDH-dependent ROS production was localized to the dehydrogenase+CoQ and complex III, the latter being the highest in all mitochondria but BAT. Our results demonstrate high efficiency of mGPDH-dependent ROS production in mammalian mitochondria with a low content of mGPDH and suggest its endogenous inhibition in BAT.
References provided by Crossref.org
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