Effect of hydrogen peroxide on sugar transport in Schizosaccharomyces pombe. Absence of membrane lipid peroxidation
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
8375778
DOI
10.1007/bf02891695
Knihovny.cz E-zdroje
- MeSH
- aktivní transport účinky léků MeSH
- antimycin A farmakologie MeSH
- arabinosa metabolismus MeSH
- deoxyglukosa analogy a deriváty metabolismus MeSH
- fungální proteiny metabolismus MeSH
- karbonylkyanid-m-chlorfenylhydrazon farmakologie MeSH
- katalasa metabolismus MeSH
- membránové lipidy metabolismus MeSH
- membránové proteiny metabolismus MeSH
- metabolismus sacharidů * MeSH
- peroxid vodíku farmakologie MeSH
- peroxidace lipidů * MeSH
- protonové ATPasy metabolismus MeSH
- Schizosaccharomyces účinky léků metabolismus MeSH
- spotřeba kyslíku MeSH
- transportní proteiny metabolismus MeSH
- xylosa metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- 6-deoxyglucose MeSH Prohlížeč
- antimycin A MeSH
- arabinosa MeSH
- deoxyglukosa MeSH
- fungální proteiny MeSH
- karbonylkyanid-m-chlorfenylhydrazon MeSH
- katalasa MeSH
- membránové lipidy MeSH
- membránové proteiny MeSH
- peroxid vodíku MeSH
- protonové ATPasy MeSH
- transportní proteiny MeSH
- xylosa MeSH
Stationary unaerated cells of S. pombe containing endogenous substrates but not energized by any exogenous ones take up 2-deoxy-D-glucose, 6-deoxy-D-glucose, D-xylose and D-arabinose actively over diffusion equilibrium. The active uptake is inhibited by 20-100 mmol/L H2O2 which causes an increase in KT but has no effect on Jmax. This "competitive inhibition" indicates that H2O2 affects directly the sugar binding sites of the transporters. The ATP-binding site of the plasma membrane H(+)-ATPase is also affected by 100 mmol/L H2O2; the KT decreases 7-fold, Jmax about 2.5-fold. These effects are not likely to be mediated by membrane lipid peroxidation which appears to be lacking in S. pombe, and this lack may be one of the reasons for the high resistance of this yeast to H2O2. Because of this S. pombe represents a suitable system for studying direct effects of oxidants on membrane proteins.
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