Difference between revisions of "Bleier 2014 Free Radic Biol Med"

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{{Publication
{{Publication
|title=Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4 (2014) Generator-specific targets of mitochondrial reactive oxygen species. Free Radic Biol Med ahead of print.  
|title=Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4 (2014) Generator-specific targets of mitochondrial reactive oxygen species. Free Radic Biol Med ahead of print.
|info==[http://www.ncbi.nlm.nih.gov/pubmed/25451644 PMID: 25451644]
|info==[http://www.ncbi.nlm.nih.gov/pubmed/25451644 PMID: 25451644]
|authors=Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4
|authors=Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4
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|abstract=To understand the role of reactive oxygen species (ROS) in oxidative stress and redox signaling it is necessary to link their site of generation to the oxidative modification of specific targets. Here we have studied the selective modification of protein thiols by mitochondrial ROS that have been implicated as deleterious agents in a number of degenerative diseases and in the process of biological aging, but also as important players in cellular signal transduction. We hypothesized that this bipartite role might be based on different generator sites for "signaling" and "damaging" ROS and a directed release into different mitochondrial compartments. Because two main mitochondrial ROS generators, complex I (NADH:ubiquinone oxidoreductase) and complex III (ubiquinol:cytochrome c oxidoreductase; cytochrome bc1 complex), are known to predominantly release superoxide and the derived hydrogen peroxide (H2O2) into the mitochondrial matrix and the intermembrane space, respectively, we investigated whether these ROS generators selectively oxidize specific protein thiols. We used redox fluorescence difference gel electrophoresis analysis to identify redox-sensitive targets in the mitochondrial proteome of intact rat heart mitochondria. We observed that the modified target proteins were distinctly different when complex I or complex III was employed as the source of ROS. These proteins are potential targets involved in mitochondrial redox signaling and may serve as biomarkers to study the generator-dependent dual role of mitochondrial ROS in redox signaling and oxidative stress.
|abstract=To understand the role of reactive oxygen species (ROS) in oxidative stress and redox signaling it is necessary to link their site of generation to the oxidative modification of specific targets. Here we have studied the selective modification of protein thiols by mitochondrial ROS that have been implicated as deleterious agents in a number of degenerative diseases and in the process of biological aging, but also as important players in cellular signal transduction. We hypothesized that this bipartite role might be based on different generator sites for "signaling" and "damaging" ROS and a directed release into different mitochondrial compartments. Because two main mitochondrial ROS generators, complex I (NADH:ubiquinone oxidoreductase) and complex III (ubiquinol:cytochrome c oxidoreductase; cytochrome bc1 complex), are known to predominantly release superoxide and the derived hydrogen peroxide (H2O2) into the mitochondrial matrix and the intermembrane space, respectively, we investigated whether these ROS generators selectively oxidize specific protein thiols. We used redox fluorescence difference gel electrophoresis analysis to identify redox-sensitive targets in the mitochondrial proteome of intact rat heart mitochondria. We observed that the modified target proteins were distinctly different when complex I or complex III was employed as the source of ROS. These proteins are potential targets involved in mitochondrial redox signaling and may serve as biomarkers to study the generator-dependent dual role of mitochondrial ROS in redox signaling and oxidative stress.
|keywords=Biomarker; Complex I; Complex III, Free radicals, Mitochondria, Reactive oxygen species, Redox proteomics, Redox signaling, Thiol oxidation
|keywords=Biomarker; Complex I; Complex III, Free radicals, Mitochondria, Reactive oxygen species, Redox proteomics, Redox signaling, Thiol oxidation
|mipnetlab=DE Frankfurt Droese S, NL Nijmegen Brandt U
}}
}}
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Revision as of 12:59, 10 December 2014

Publications in the MiPMap
Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4 (2014) Generator-specific targets of mitochondrial reactive oxygen species. Free Radic Biol Med ahead of print.

» =PMID: 25451644

Bleier L, Wittig I, Heide H, Steger M, Brandt U, Droese S4 (2014) Free Radic Biol Med

Abstract: To understand the role of reactive oxygen species (ROS) in oxidative stress and redox signaling it is necessary to link their site of generation to the oxidative modification of specific targets. Here we have studied the selective modification of protein thiols by mitochondrial ROS that have been implicated as deleterious agents in a number of degenerative diseases and in the process of biological aging, but also as important players in cellular signal transduction. We hypothesized that this bipartite role might be based on different generator sites for "signaling" and "damaging" ROS and a directed release into different mitochondrial compartments. Because two main mitochondrial ROS generators, complex I (NADH:ubiquinone oxidoreductase) and complex III (ubiquinol:cytochrome c oxidoreductase; cytochrome bc1 complex), are known to predominantly release superoxide and the derived hydrogen peroxide (H2O2) into the mitochondrial matrix and the intermembrane space, respectively, we investigated whether these ROS generators selectively oxidize specific protein thiols. We used redox fluorescence difference gel electrophoresis analysis to identify redox-sensitive targets in the mitochondrial proteome of intact rat heart mitochondria. We observed that the modified target proteins were distinctly different when complex I or complex III was employed as the source of ROS. These proteins are potential targets involved in mitochondrial redox signaling and may serve as biomarkers to study the generator-dependent dual role of mitochondrial ROS in redox signaling and oxidative stress.

Keywords: Biomarker; Complex I; Complex III, Free radicals, Mitochondria, Reactive oxygen species, Redox proteomics, Redox signaling, Thiol oxidation

O2k-Network Lab: DE Frankfurt Droese S, NL Nijmegen Brandt U


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