Respiratory chain components involved in the glycerophosphate dehydrogenase-dependent ROS production by brown adipose tissue mitochondria
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17560536
DOI
10.1016/j.bbabio.2007.05.002
PII: S0005-2728(07)00107-7
Knihovny.cz E-resources
- MeSH
- Antimycin A analogs & derivatives pharmacology MeSH
- Cell Respiration MeSH
- Electron Spin Resonance Spectroscopy MeSH
- Ethidium analogs & derivatives chemistry MeSH
- Ferricyanides pharmacology MeSH
- Glycerolphosphate Dehydrogenase metabolism MeSH
- Glycerophosphates metabolism MeSH
- Adipose Tissue, Brown drug effects enzymology ultrastructure MeSH
- Cricetinae MeSH
- Mitochondria drug effects enzymology metabolism MeSH
- Reactive Oxygen Species analysis metabolism MeSH
- Electron Transport Complex III metabolism MeSH
- Oxygen Consumption MeSH
- Electron Transport MeSH
- Ubiquinone metabolism MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antimycin A MeSH
- antimycin MeSH Browser
- dihydroethidium MeSH Browser
- Ethidium MeSH
- Ferricyanides MeSH
- Glycerolphosphate Dehydrogenase MeSH
- Glycerophosphates MeSH
- hexacyanoferrate III MeSH Browser
- Reactive Oxygen Species MeSH
- Electron Transport Complex III MeSH
- Ubiquinone MeSH
Involvement of mammalian mitochondrial glycerophosphate dehydrogenase (mGPDH, EC 1.1.99.5) in reactive oxygen species (ROS) generation was studied in brown adipose tissue mitochondria by different spectroscopic techniques. Spectrofluorometry using ROS-sensitive probes CM-H2DCFDA and Amplex Red was used to determine the glycerophosphate- or succinate-dependent ROS production in mitochondria supplemented with respiratory chain inhibitors antimycin A and myxothiazol. In case of glycerophosphate oxidation, most of the ROS originated directly from mGPDH and coenzyme Q while complex III was a typical site of ROS production in succinate oxidation. Glycerophosphate-dependent ROS production monitored by KCN-insensitive oxygen consumption was highly activated by one-electron acceptor ferricyanide, whereas succinate-dependent ROS production was unaffected. In addition, superoxide anion radical was detected as a mGPDH-related primary ROS species by fluorescent probe dihydroethidium, as well as by electron paramagnetic resonance (EPR) spectroscopy with DMPO spin trap. Altogether, the data obtained demonstrate pronounced differences in the mechanism of ROS production originating from oxidation of glycerophosphate and succinate indicating that electron transfer from mGPDH to coenzyme Q is highly prone to electron leak and superoxide generation.
References provided by Crossref.org
Pleiotropic Effects of Biguanides on Mitochondrial Reactive Oxygen Species Production
