Redox signalling and detection of protein oxidation by mass spectrometry

Research output: Unpublished contribution to conferenceAbstractpeer-review


It is now recognised that redox control of proteins plays an important role in many signalling pathways both in health and disease. Proteins can undergo a wide variety of oxidative post-translational modifications (oxPTM); while the reversible modifications are thought to be most important in physiological processes, non-reversible oxPTM may contribute to pathological situations and disease. The oxidant is also important in determining the type of oxPTM (chlorination, nitration, etc.), and the susceptibilities of residues vary depending on their structural location. The best characterized oxPTMs involved in signalling modulation are partial oxidations of cysteine to the disulfide, glutathionylated or sulfenic acid forms, but there is increasing evidence that specific oxidations of methionine and tyrosine may have some biological roles. Well understood examples of oxidative regulation include protein tyrosine phosphatases, e.g. PTP1B/C, and members of the MAPK pathways such as MEKK1 and ASK1. Transcription factors such as NFkB and Nrf-2 are also regulated by redox-active cysteines. Improved methods for analysing specific oxPTMs in biological samples are critical for understanding the physiological and pathological roles of these changes, and tandem or MS3 mass spectrometry techniques interfaced with nano-LC separation are being now used. MS3 fragmentation markers for a variety of oxidized residues including tyrosine, tryptophan and proline have been identified, and a precursor ion scanning method that allows the selective identification of these oxPTMs in complex samples has been developed. Such advances in technology offer potential for biomarker development, disease diagnosis
and understanding pathology.
Original languageEnglish
Number of pages1
Publication statusPublished - Jul 2009
Event11th International Congress on Amino Acids, Peptides and Proteins - Vienna (AT), United Kingdom
Duration: 3 Aug 20097 Aug 2009


Conference11th International Congress on Amino Acids, Peptides and Proteins
Country/TerritoryUnited Kingdom
CityVienna (AT)

Bibliographical note

Abstract published in Abstracts - 11th International Congress on Amino Acids, Peptides and Proteins, Amino Acids, 37 (Suppl.1) S33


  • redox control
  • protein oxidation
  • signalling pathways
  • mass spectrometry
  • Science (General)


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