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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1777998
- author
- Mörtstedt, Harriet
LU
; Jeppsson, Marina
; Ferrari, Giovanni
LU
; Jönsson, Bo A
LU
; Kåredal, Monica
LU
and Lindh, Christian
LU
- organization
- publishing date
- 2011
- 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 Inc.
- external identifiers
-
- wos:000285848800009
- pmid:21192028
- scopus:78650718216
- pmid:21192028
- 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
- 2016-04-04 07:07:32
- date last changed
- 2022-02-13 04:33:51
@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 Inc.}},
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}},
doi = {{10.1002/rcm.4867}},
volume = {{25}},
year = {{2011}},
}