Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12018887
DOI
10.1023/a:1015123908918
Knihovny.cz E-zdroje
- MeSH
- biologické modely MeSH
- ferrikyanidy farmakologie MeSH
- glycerolfosfátdehydrogenasa antagonisté a inhibitory izolace a purifikace metabolismus MeSH
- glycerolfosfáty metabolismus MeSH
- hnědá tuková tkáň účinky léků metabolismus MeSH
- inhibitory enzymů farmakologie MeSH
- katalasa metabolismus farmakologie MeSH
- křečci praví MeSH
- křeček rodu Mesocricetus MeSH
- luminiscenční měření MeSH
- mitochondrie účinky léků metabolismus MeSH
- peroxid vodíku metabolismus MeSH
- reaktivní formy kyslíku metabolismus MeSH
- techniky in vitro MeSH
- ubichinon metabolismus farmakologie MeSH
- zvířata MeSH
- Check Tag
- křečci praví MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- ferrikyanidy MeSH
- glycerolfosfátdehydrogenasa MeSH
- glycerolfosfáty MeSH
- inhibitory enzymů MeSH
- katalasa MeSH
- peroxid vodíku MeSH
- potassium ferricyanide MeSH Prohlížeč
- reaktivní formy kyslíku MeSH
- ubichinon MeSH
Oxidation of glycerophosphate (GP) by brown adipose tissue mitochondria in the presence of antimycin A was found to be accompanied by significant production of hydrogen peroxide. GP-dependent hydrogen peroxide production could be detected by p-hydroxyphenylacetate fluorescence changes or as an antimycin A-insensitive oxygen consumption. One-electron acceptor, potassium ferricyanide, highly stimulated the rate of GP-dependent antimycin A-insensitive oxygen uptake, which was prevented by inhibitors of mitochondrial GP dehydrogenase (mGPDH) or by coenzyme Q (CoQ). GP-dependent ferricyanide-induced peroxide production was also determined luminometrically, using mitochondria or partially purified mGPDH. Ferricyanide-induced peroxide production was negligible, when succinate or NADH was used as a substrate. These results indicate that hydrogen peroxide is produced directly by mGPDH and reflect the differences in the transport of reducing equivalents from mGPDH and succinate dehydrogenase to the CoQ pool. The data suggest that more intensive production of reactive oxygen species may be present in mammalian cells with active mGPDH.
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