Measuring mitochondrial protein thiol redox state.
Protein thiols are an important component of mammalian intramitochondrial antioxidant defenses owing to their selective interaction with reactive oxygen and nitrogen species (ROS and RNS). Reversible modifications of protein thiols resulting from these interactions are also an important aspect of redox signal transduction. Therefore, to assess how mitochondria respond to oxidative stress and act as nodes in redox signaling pathways, it is important to measure general changes to protein thiol redox states and also to identify the specific mitochondrial thiol proteins involved. Here we outline some of the approaches that can be used to accomplish these goals and thereby infer the multiple roles of mammalian mitochondrial protein thiols in antioxidant defense and redox signaling.
Requejo
Raquel
R
Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Cambridge, UK.
Chouchani
Edward T
ET
Hurd
Thomas R
TR
Menger
Katja E
KE
Hampton
Mark B
MB
Murphy
Michael P
MP
D015153:Blotting, Western; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D024101:Mitochondrial Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D032383:Myocytes, Cardiac / Q000201:enzymology; D010084:Oxidation-Reduction; D011485:Protein Binding; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism
D024101:Mitochondrial Proteins; D013438:Sulfhydryl Compounds; D005978:Glutathione