Difference between revisions of "Drahota 2005 Physiol Res"
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{{Publication | {{Publication | ||
|title=Drahota Z, Krivakova P, Cervinkova Z, Kmonickova E, Lotkova H, Kucera O, Houstek J (2005) Tert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes. Physiol | |title=Drahota Z, Krivakova P, Cervinkova Z, Kmonickova E, Lotkova H, Kucera O, Houstek J (2005) Tert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes. Physiol Res 54:67-72. | ||
|authors=Drahota | |info=[http://www.ncbi.nlm.nih.gov/pubmed/15717843 PMID: 15717843 Open Access] | ||
|authors=Drahota Zdenek, Stankova Pavla, Cervinkova Zuzana, Kmonickova E, Lotkova Halka, Kucera Otto, Houstek Josef | |||
|year=2005 | |year=2005 | ||
|journal=Physiol | |journal=Physiol Res | ||
|abstract=Sensitivity of various mitochondrial enzymes to oxidative damage was tested on isolated rat liver hepatocytes permeabilized by digitonin. In permeabilized hepatocytes normal respiratory control values were obtained and mitochondrial membranes remained intact. Respiratory rates of NADH-dependent (glutamate+malate, palmitylcarnitine + malate) and flavoprotein-dependent (succinate) substrates were determined in hepatocytes exposed for 5 min to 0.5-3 mM tert-butyl hydroperoxide before addition of digitonin. Our data showed that oxidation of NADH-dependent substrates is much more sensitive to oxidative stress than oxidation of flavoprotein-dependent ones, evidently due to the modification of iron-sulfur clusters or SH groups in the NADH dehydrogenase enzyme complex (Complex I). | |abstract=Sensitivity of various mitochondrial enzymes to oxidative damage was tested on isolated rat liver hepatocytes permeabilized by digitonin. In permeabilized hepatocytes normal respiratory control values were obtained and mitochondrial membranes remained intact. Respiratory rates of NADH-dependent (glutamate+malate, palmitylcarnitine + malate) and flavoprotein-dependent (succinate) substrates were determined in hepatocytes exposed for 5 min to 0.5-3 mM tert-butyl hydroperoxide before addition of digitonin. Our data showed that oxidation of NADH-dependent substrates is much more sensitive to oxidative stress than oxidation of flavoprotein-dependent ones, evidently due to the modification of iron-sulfur clusters or SH groups in the NADH dehydrogenase enzyme complex (Complex I). | ||
|keywords=Hepatocytes, Mitochondrial enzymes Tert-butyl hydroperoxide | |keywords=Hepatocytes, Mitochondrial enzymes Tert-butyl hydroperoxide | ||
| | |mipnetlab=CZ_Prague_Houstek J, CZ_Hradec Kralove_Cervinkova Z | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |||
|organism=Rat | |organism=Rat | ||
|tissues= | |tissues=Liver | ||
|preparations=Permeabilized | |preparations=Permeabilized cells | ||
|enzymes=TCA | |enzymes=TCA cycle and matrix dehydrogenases | ||
| | |couplingstates=OXPHOS | ||
|pathways=N | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 11:06, 18 March 2020
| Drahota Z, Krivakova P, Cervinkova Z, Kmonickova E, Lotkova H, Kucera O, Houstek J (2005) Tert-butyl hydroperoxide selectively inhibits mitochondrial respiratory-chain enzymes in isolated rat hepatocytes. Physiol Res 54:67-72. |
Drahota Zdenek, Stankova Pavla, Cervinkova Zuzana, Kmonickova E, Lotkova Halka, Kucera Otto, Houstek Josef (2005) Physiol Res
Abstract: Sensitivity of various mitochondrial enzymes to oxidative damage was tested on isolated rat liver hepatocytes permeabilized by digitonin. In permeabilized hepatocytes normal respiratory control values were obtained and mitochondrial membranes remained intact. Respiratory rates of NADH-dependent (glutamate+malate, palmitylcarnitine + malate) and flavoprotein-dependent (succinate) substrates were determined in hepatocytes exposed for 5 min to 0.5-3 mM tert-butyl hydroperoxide before addition of digitonin. Our data showed that oxidation of NADH-dependent substrates is much more sensitive to oxidative stress than oxidation of flavoprotein-dependent ones, evidently due to the modification of iron-sulfur clusters or SH groups in the NADH dehydrogenase enzyme complex (Complex I). • Keywords: Hepatocytes, Mitochondrial enzymes Tert-butyl hydroperoxide
• O2k-Network Lab: CZ_Prague_Houstek J, CZ_Hradec Kralove_Cervinkova Z
Labels: MiParea: Respiration
Organism: Rat
Tissue;cell: Liver
Preparation: Permeabilized cells
Enzyme: TCA cycle and matrix dehydrogenases
Coupling state: OXPHOS Pathway: N HRR: Oxygraph-2k
