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Strategy for identification and detection of multiple oxidative modifications within proteins applied on persulfate-oxidized hemoglobin and human serum albumin.

Mörtstedt, Harriet LU ; Jeppsson, Marina; Ferrari, Giovanni LU ; Jönsson, Bo A LU ; Kåredal, Monica LU and Lindh, Christian LU (2011) In Rapid Communications in Mass Spectrometry 25(2). p.327-340
Abstract
Oxidative stress has been suggested as an underlying mechanism of many human diseases. However, definitive evidence for this association has not been presented due to different shortcomings of the methods used to measure biomarkers of oxidative stress. Persulfates are oxidizing agents known to elicit hypersensitive reactions from the airways and skin. Despite a frequent use of persulfates at many work places, no biomarkers for persulfate exposure are available. The aim of this study was to develop a strategy for the identification and detection of multiple oxidative modifications within proteins. This strategy was applied on persulfate-oxidized proteins to identify oxidized peptides suitable for further investigation as biomarkers of... (More)
Oxidative stress has been suggested as an underlying mechanism of many human diseases. However, definitive evidence for this association has not been presented due to different shortcomings of the methods used to measure biomarkers of oxidative stress. Persulfates are oxidizing agents known to elicit hypersensitive reactions from the airways and skin. Despite a frequent use of persulfates at many work places, no biomarkers for persulfate exposure are available. The aim of this study was to develop a strategy for the identification and detection of multiple oxidative modifications within proteins. This strategy was applied on persulfate-oxidized proteins to identify oxidized peptides suitable for further investigation as biomarkers of persulfate exposure or oxidative stress. A strategy for the identification and the relative quantification of multiple oxidative modifications within proteins was developed. The usage of two software packages facilitated the search for modified peptides to a great extent. Oxidized peptides were relatively quantified using liquid chromatography/tandem mass spectrometry in selected reaction monitoring mode. The result showed that persulfates oxidize tryptophans and methionines resulting in mass shifts of 16 and/or 32 Da. Also, oxidized albumin peptides in nasal lavage fluid samples from subjects challenged with persulfate were detected. The oxidation degree before and after challenge remained constant for peptides containing methionine sulfoxide. For peptides containing oxidized tryptophan the oxidation degree increased after exposure. Some of these oxidized peptides may be suitable as biomarkers; however, further evaluation is required. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
Rapid Communications in Mass Spectrometry
volume
25
issue
2
pages
327 - 340
publisher
John Wiley & Sons
external identifiers
  • wos:000285848800009
  • pmid:21192028
  • scopus:78650718216
ISSN
1097-0231
DOI
10.1002/rcm.4867
language
English
LU publication?
yes
id
543e1371-0bd3-411f-9ffe-54253c9df23f (old id 1777998)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21192028?dopt=Abstract
date added to LUP
2011-02-01 10:01:19
date last changed
2017-01-01 07:29:43
@article{543e1371-0bd3-411f-9ffe-54253c9df23f,
  abstract     = {Oxidative stress has been suggested as an underlying mechanism of many human diseases. However, definitive evidence for this association has not been presented due to different shortcomings of the methods used to measure biomarkers of oxidative stress. Persulfates are oxidizing agents known to elicit hypersensitive reactions from the airways and skin. Despite a frequent use of persulfates at many work places, no biomarkers for persulfate exposure are available. The aim of this study was to develop a strategy for the identification and detection of multiple oxidative modifications within proteins. This strategy was applied on persulfate-oxidized proteins to identify oxidized peptides suitable for further investigation as biomarkers of persulfate exposure or oxidative stress. A strategy for the identification and the relative quantification of multiple oxidative modifications within proteins was developed. The usage of two software packages facilitated the search for modified peptides to a great extent. Oxidized peptides were relatively quantified using liquid chromatography/tandem mass spectrometry in selected reaction monitoring mode. The result showed that persulfates oxidize tryptophans and methionines resulting in mass shifts of 16 and/or 32 Da. Also, oxidized albumin peptides in nasal lavage fluid samples from subjects challenged with persulfate were detected. The oxidation degree before and after challenge remained constant for peptides containing methionine sulfoxide. For peptides containing oxidized tryptophan the oxidation degree increased after exposure. Some of these oxidized peptides may be suitable as biomarkers; however, further evaluation is required.},
  author       = {Mörtstedt, Harriet and Jeppsson, Marina and Ferrari, Giovanni and Jönsson, Bo A and Kåredal, Monica and Lindh, Christian},
  issn         = {1097-0231},
  language     = {eng},
  number       = {2},
  pages        = {327--340},
  publisher    = {John Wiley & Sons},
  series       = {Rapid Communications in Mass Spectrometry},
  title        = {Strategy for identification and detection of multiple oxidative modifications within proteins applied on persulfate-oxidized hemoglobin and human serum albumin.},
  url          = {http://dx.doi.org/10.1002/rcm.4867},
  volume       = {25},
  year         = {2011},
}