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Difference between revisions of "Vrbacky 2007 Biochim Biophys Acta"

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{{Publication
{{Publication
|title=Vrbacky M, Drahota Z, Mracek T, Vojtískova A, Jesina P, Stopka P, Houstek J (2007) Respiratory chain components involved in the glycerophosphate dehydrogenase-dependent ROS production by brown adipose tissue mitochondria. Biochim Biophys Acta 1767: 989-997.
|title=Vrbacky M, Drahota Z, Mracek T, Vojtískova A, Jesina P, Stopka P, Houstek J (2007) Respiratory chain components involved in the glycerophosphate dehydrogenase-dependent ROS production by brown adipose tissue mitochondria. Biochim Biophys Acta 1767:989-97.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17560536 PMID: 17560536]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17560536 PMID: 17560536 Open Access]
|authors=Vrbacky M, Drahota Z, Mracek T, Vojtiskova A, Jesina P, Stopka P, Houstek J
|authors=Vrbacky M, Drahota Z, Mracek T, Vojtiskova A, Jesina P, Stopka P, Houstek J
|year=2007
|year=2007
|journal=Biochim Biophys Acta
|journal=Biochim Biophys Acta
|abstract=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-H<sub>2</sub> DCFDA 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.
|abstract=Involvement of mammalian [[Glycerophosphate dehydrogenase complex |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-H<sub>2</sub> DCFDA 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.
|keywords=Brown adipose tissue mitochondria, Glycerophosphate dehydrogenase, Reactive oxygen species, Fluorescent probes, Oxygraphy, EPR, Hamster
|keywords=Brown adipose tissue mitochondria, Glycerophosphate dehydrogenase, Reactive oxygen species, Fluorescent probes, Oxygraphy, EPR, Hamster
|mipnetlab=CZ_Prague_Houstek J, CZ Prague Bioenergetics
|mipnetlab=CZ Prague Houstek J, CZ Hradec Kralove Cervinkova Z
|discipline=Mitochondrial Physiology, Biomedicine
|discipline=Mitochondrial Physiology, Biomedicine
}}
}}
{{Labeling
{{Labeling
|instruments=Oxygraph-2k, Spectrofluorometry
|area=Respiration
|injuries=RONS; Oxidative Stress
|organism=Other mammals
|taxonomic group=Mammals
|tissues=Fat
|tissues=Fat
|preparations=Isolated Mitochondria
|preparations=Isolated mitochondria
|substratestates=CII, GpDH, CIII
|enzymes=Complex III
|enzymes=Complex III
|injuries=Oxidative stress;RONS
|pathways=S, Gp
|instruments=Oxygraph-2k
|discipline=Mitochondrial Physiology, Biomedicine
|discipline=Mitochondrial Physiology, Biomedicine
}}
}}

Latest revision as of 12:10, 8 November 2016

Publications in the MiPMap
Vrbacky M, Drahota Z, Mracek T, Vojtískova A, Jesina P, Stopka P, Houstek J (2007) Respiratory chain components involved in the glycerophosphate dehydrogenase-dependent ROS production by brown adipose tissue mitochondria. Biochim Biophys Acta 1767:989-97.

» PMID: 17560536 Open Access

Vrbacky M, Drahota Z, Mracek T, Vojtiskova A, Jesina P, Stopka P, Houstek J (2007) Biochim Biophys Acta

Abstract: 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-H2 DCFDA 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. Keywords: Brown adipose tissue mitochondria, Glycerophosphate dehydrogenase, Reactive oxygen species, Fluorescent probes, Oxygraphy, EPR, Hamster

O2k-Network Lab: CZ Prague Houstek J, CZ Hradec Kralove Cervinkova Z


Labels: MiParea: Respiration 

Stress:Oxidative stress;RONS  Organism: Other mammals  Tissue;cell: Fat  Preparation: Isolated mitochondria  Enzyme: Complex III 


Pathway: S, Gp  HRR: Oxygraph-2k