Redox signalling and detection of protein oxidation by mass spectrometry

Research output: Contribution to conferenceAbstract

Abstract

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.
LanguageEnglish
Pages33
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

Conference

Conference11th International Congress on Amino Acids, Peptides and Proteins
CountryUnited Kingdom
CityVienna (AT)
Period3/08/097/08/09

Fingerprint

Mass spectrometry
Oxidation
Cysteine
Tyrosine
Sulfenic Acids
Nitration
Proteins
Protein Tyrosine Phosphatases
Chlorination
Biomarkers
Pathology
Proline
Oxidants
Tryptophan
Disulfides
Methionine
Transcription Factors
Modulation
Health
Ions

Bibliographical note

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

Keywords

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

Cite this

Spickett, C. M., & Pitt, A. R. (2009). Redox signalling and detection of protein oxidation by mass spectrometry. 33. Abstract from 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom.
Spickett, Corinne M. ; Pitt, Andrew R. / Redox signalling and detection of protein oxidation by mass spectrometry. Abstract from 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom.1 p.
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Spickett, CM & Pitt, AR 2009, 'Redox signalling and detection of protein oxidation by mass spectrometry' 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom, 3/08/09 - 7/08/09, pp. 33.

Redox signalling and detection of protein oxidation by mass spectrometry. / Spickett, Corinne M.; Pitt, Andrew R.

2009. 33 Abstract from 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom.

Research output: Contribution to conferenceAbstract

TY - CONF

T1 - Redox signalling and detection of protein oxidation by mass spectrometry

AU - Spickett, Corinne M.

AU - Pitt, Andrew R.

N1 - Abstract published in Abstracts - 11th International Congress on Amino Acids, Peptides and Proteins, Amino Acids, 37 (Suppl.1) S33

PY - 2009/7

Y1 - 2009/7

N2 - 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 diagnosisand understanding pathology.

AB - 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 diagnosisand understanding pathology.

KW - redox control

KW - protein oxidation

KW - signalling pathways

KW - mass spectrometry

KW - Science (General)

M3 - Abstract

SP - 33

ER -

Spickett CM, Pitt AR. Redox signalling and detection of protein oxidation by mass spectrometry. 2009. Abstract from 11th International Congress on Amino Acids, Peptides and Proteins, Vienna (AT), United Kingdom.