Identification of the oxidative stress proteome in the brain

Rukhsana Sultana, D. Allan Butterfield

Research output: Contribution to journalShort surveypeer-review

28 Scopus citations

Abstract

The redox proteomics technique normally combines two-dimensional gel electrophoresis, mass spectrometry, and protein databases to analyze the cell proteome from various samples, thereby leading to the identification of specific targets of oxidative modification. Oxidative stress that occurs because of increased levels of reactive oxygen species and reactive nitrogen species can target most biomolecules, consequently leading to altered physiological function of the cells. Redox proteomics has identified oxidatively modified protein targets in various pathological conditions, consequently providing insight into the pathways involved in the pathogenesis of these conditions. This approach also can be used to identify possible protective mechanisms to prevent or delay these disorders.

Original languageEnglish
Pages (from-to)487-494
Number of pages8
JournalFree Radical Biology and Medicine
Volume50
Issue number4
DOIs
StatePublished - Feb 15 2011

Bibliographical note

Funding Information:
This research was supported by a NIH grant to D.A.B. (AG-05119).

Keywords

  • 3-Nitrotyrosine
  • Mass spectrometry
  • Oxidative modification
  • Protein carbonyls
  • Protein-bound HNE
  • Redox proteomics
  • Two-dimensional gel electrophoresis

ASJC Scopus subject areas

  • Biochemistry
  • Physiology (medical)

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