Measuring mitochondrial protein thiol redox state

Methods Enzymol. 2010;474:123-47. doi: 10.1016/S0076-6879(10)74008-8. Epub 2010 Jun 20.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Glutathione / chemistry
  • Glutathione / metabolism
  • Liver / enzymology
  • Mitochondrial Proteins / analysis
  • Mitochondrial Proteins / chemistry*
  • Mitochondrial Proteins / metabolism
  • Myocytes, Cardiac / enzymology
  • Oxidation-Reduction
  • Protein Binding
  • Signal Transduction
  • Sulfhydryl Compounds / analysis
  • Sulfhydryl Compounds / chemistry*
  • Sulfhydryl Compounds / metabolism

Substances

  • Mitochondrial Proteins
  • Sulfhydryl Compounds
  • Glutathione