Abstract：
:Proteins are continuously exposed to diverse chemical stresses, and the resulting chemical modifications can provide significant information on biological events. Keratins are the main constituent of human skin and are the major target proteins of various chemical modifications. We have previously developed a mass spectrometry-based noninvasive proteomic methodology to screen oxidative modifications in human skin keratins. We have improved this methodology in terms of sample preparation time and amino acid sequence coverage using an on-tape digestion method. After sampling by tape stripping, skin proteins on the tape were subjected to reduction/alkylation, followed by trypsin digestion without a presolubilization step using detergents. To screen chemical modifications in keratins, target modifications and tryptic target peptides carrying the modification sites were determined from in vitro experiments with major reactive chemical species (4-hydroxy-2(E)-nonenal (HNE), 4-oxo-2(E)-nonenal, glucose, methylglyoxal, peroxynitrite, and hydrogen peroxide). The developed method was used to screen target modifications in controls and patients with a swollen red rash. Basal levels of lipid-derived modification, oxidation, nitration, and glycation in keratins were detected in controls. Principal component analysis based on the relative chemical modification resulted in a clear classification of both groups within a 95% confidence interval. Lipid-derived HNE modification increased most significantly in the patient group. This methodology can be easily applied to patients with other diseases, and the target modifications can be used as biomarkers of certain physiological conditions.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Lee SH,Kawase J,Hiroshima Y,Oe Tdoi
10.1021/acs.jproteome.0c00406subject
Has Abstractpub_date
2020-09-04 00:00:00pages
3837-3845issue
9eissn
1535-3893issn
1535-3907journal_volume
19pub_type
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journal_title：Journal of proteome research
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