Redox proteomics: From protein modifications to cellular dysfunction and disease

D. Allan Butterfield, Isabella Dalle-Donne

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

Reactive oxygen and nitrogen species are part of any aerobic lifestyle/metabolism. Low concentrations of selected ROS and RNS are continuously produced inside and outside the cell by a number of pathways, either accidentally or purposefully. Because of the potential toxicity of these reactive species, a number of cellular and extracellular antioxidant defenses, both enzymatic and non-enzymatic, are designed to remove/neutralize ROS, RNS, and RCS directly, to minimize the extent of either their production or damage they can provoke, or to repair oxidative/nitrosative damage caused by them. Due to their high chemical reactivity, ROS and RNS can modify and oxidize various biological molecules, often altering their biological function, such as unsaturated lipids, carbohydrates, nucleic acids, but mostly, because of their high abundance, proteins. These oxidized cellular molecules can cause toxicity as such and/or may degrade to form further toxic products, such as reactive carbonyl species (RCS) generated by peroxidation of polyunsaturated fatty acids (PUFA).

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalMass Spectrometry Reviews
Volume33
Issue number1
DOIs
StatePublished - Jan 2014

ASJC Scopus subject areas

  • Analytical Chemistry
  • Condensed Matter Physics
  • General Biochemistry, Genetics and Molecular Biology
  • Spectroscopy

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