Difference between revisions of "Koziel 2013 Biochem J"
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{{Publication | {{Publication | ||
|title=Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P (2013) Mitochondrial respiratory chain complex I is inactivated by NADPH oxidase Nox4. Biochem J 452:231- | |title=Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P (2013) Mitochondrial respiratory chain complex I is inactivated by NADPH oxidase Nox4. Biochem J 452:231-9. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/23514110 PMID: 23514110] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/23514110 PMID: 23514110 Open Access] | ||
|authors=Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P | |authors=Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P | ||
|year=2013 | |year=2013 | ||
|journal=Biochem J | |journal=Biochem J | ||
|abstract=ROS (reactive oxygen species) generated by NADPH oxidases play an important role in cellular signal transduction regulating cell proliferation, survival and differentiation. Nox4 (NADPH oxidase 4) induces cellular senescence in human endothelial cells; however, intracellular targets for Nox4 remained elusive. In the present study, we show that Nox4 induces mitochondrial dysfunction in human endothelial cells. Nox4 depletion induced alterations in mitochondrial morphology, stabilized mitochondrial membrane potential and decreased production of H | |abstract=ROS (reactive oxygen species) generated by NADPH oxidases play an important role in cellular signal transduction regulating cell proliferation, survival and differentiation. Nox4 (NADPH oxidase 4) induces cellular senescence in human endothelial cells; however, intracellular targets for Nox4 remained elusive. In the present study, we show that Nox4 induces mitochondrial dysfunction in human endothelial cells. Nox4 depletion induced alterations in mitochondrial morphology, stabilized mitochondrial membrane potential and decreased production of H<sub>2</sub>O<sub>2</sub> in mitochondria. High-resolution respirometry in permeabilized cells combined with native PAGE demonstrated that Nox4 specifically inhibits the activity of mitochondrial electron transport chain complex I, and this was associated with a decreased concentration of complex I subunits. These data suggest a new pathway by which sustained Nox4 activity decreases mitochondrial function. | ||
|keywords= | |keywords=Complex I, Eelectron transport chain, Mitochondrion, Nox4, Oxidative stress, Senescence | ||
|mipnetlab=AT Innsbruck Jansen-Duerr P | |mipnetlab=AT Innsbruck Jansen-Duerr P | ||
}} | }} | ||
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|area=Respiration | |area=Respiration | ||
|organism=Human | |organism=Human | ||
|tissues=Endothelial; | |tissues=Endothelial;epithelial;mesothelial cell | ||
|preparations=Permeabilized cells | |preparations=Permeabilized cells | ||
|diseases=Aging; senescence | |diseases=Aging;senescence | ||
|couplingstates=OXPHOS | |couplingstates=OXPHOS | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 12:26, 28 April 2015
| Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P (2013) Mitochondrial respiratory chain complex I is inactivated by NADPH oxidase Nox4. Biochem J 452:231-9. |
Koziel R, Pircher H, Kratochwil M, Lener B, Hermann M, Dencher NA, Jansen-Duerr P (2013) Biochem J
Abstract: ROS (reactive oxygen species) generated by NADPH oxidases play an important role in cellular signal transduction regulating cell proliferation, survival and differentiation. Nox4 (NADPH oxidase 4) induces cellular senescence in human endothelial cells; however, intracellular targets for Nox4 remained elusive. In the present study, we show that Nox4 induces mitochondrial dysfunction in human endothelial cells. Nox4 depletion induced alterations in mitochondrial morphology, stabilized mitochondrial membrane potential and decreased production of H2O2 in mitochondria. High-resolution respirometry in permeabilized cells combined with native PAGE demonstrated that Nox4 specifically inhibits the activity of mitochondrial electron transport chain complex I, and this was associated with a decreased concentration of complex I subunits. These data suggest a new pathway by which sustained Nox4 activity decreases mitochondrial function. • Keywords: Complex I, Eelectron transport chain, Mitochondrion, Nox4, Oxidative stress, Senescence
• O2k-Network Lab: AT Innsbruck Jansen-Duerr P
Labels: MiParea: Respiration
Pathology: Aging;senescence
Organism: Human Tissue;cell: Endothelial;epithelial;mesothelial cell Preparation: Permeabilized cells
Coupling state: OXPHOS
HRR: Oxygraph-2k
