ROS generation and multiple forms of mammalian mitochondrial glycerol-3-phosphate dehydrogenase
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
23999537
DOI
10.1016/j.bbabio.2013.08.007
PII: S0005-2728(13)00144-8
Knihovny.cz E-zdroje
- Klíčová slova
- 2,6-dichlorophenolindophenol, 2-n-heptyl-4-hydroxyquinoline N-oxide, AA, BAT, CoQ, DCPIP, E.C. 1.1.5.3, FeCN, GP, HAR, HQNO, HRP, In-gel ROS detection, MXT, Mitochondrial glycerol-3-phosphate dehydrogenase, OXPHOS, ROS, ROS production, SDH, Supercomplex, antimycin A, brown adipose tissue, coenzyme Q, ferricyanide, potassium hexacyanoferrate(III), hexaammineruthenium(III) chloride, horseradish peroxidase, mGPDH, mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase, myxothiazol, oxidative phosphorylation, reactive oxygen species, sn-glycerol-3-phosphate, succinate dehydrogenase,
- MeSH
- ferrikyanidy metabolismus MeSH
- glycerolfosfátdehydrogenasa chemie metabolismus MeSH
- glycerolfosfáty metabolismus MeSH
- krysa rodu Rattus MeSH
- mitochondrie enzymologie metabolismus MeSH
- peroxid vodíku metabolismus MeSH
- reaktivní formy kyslíku metabolismus MeSH
- savci MeSH
- sukcinátdehydrogenasa chemie metabolismus MeSH
- transport elektronů * MeSH
- ubichinon metabolismus MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- ferrikyanidy MeSH
- glycerolfosfátdehydrogenasa MeSH
- glycerolfosfáty MeSH
- peroxid vodíku MeSH
- reaktivní formy kyslíku MeSH
- sukcinátdehydrogenasa MeSH
- ubichinon MeSH
Overproduction of reactive oxygen species (ROS) has been implicated in a range of pathologies. Mitochondrial flavin dehydrogenases glycerol-3-phosphate dehydrogenase (mGPDH) and succinate dehydrogenase (SDH) represent important ROS source, but the mechanism of electron leak is still poorly understood. To investigate the ROS production by the isolated dehydrogenases, we used brown adipose tissue mitochondria solubilized by digitonin as a model. Enzyme activity measurements and hydrogen peroxide production studies by Amplex Red fluorescence, and luminol luminescence in combination with oxygraphy revealed flavin as the most likely source of electron leak in SDH under in vivo conditions, while we propose coenzyme Q as the site of ROS production in the case of mGPDH. Distinct mechanism of ROS production by the two dehydrogenases is also apparent from induction of ROS generation by ferricyanide which is unique for mGPDH. Furthermore, using native electrophoretic systems, we demonstrated that mGPDH associates into homooligomers as well as high molecular weight supercomplexes, which represent native forms of mGPDH in the membrane. By this approach, we also directly demonstrated that isolated mGPDH itself as well as its supramolecular assemblies are all capable of ROS production.
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