Abstract：
:Wilson's disease is a rare inherited disorder of copper metabolism, manifesting hepatic, neurological and psychiatric symptoms. Early diagnosis is often unfeasible and a unique diagnostic test is currently inapplicable. We performed the qualitative/quantitative characterization of the salivary proteome/peptidome of 32 Wilson's disease patients by an integrated top-down/bottom-up approach. Patients exhibited significant higher levels of S100A9 and S100A8 proteoforms, and their oxidized forms with respect to controls. Oxidation occurred on methionine and tryptophan residues, and on the unique cysteine residue, in position 42 in S100A8, and 3 in S100A9, that generated glutathionylated, cysteinylated, sulfinic, sulfonic, and disulfide dimeric forms. Wilson's disease patient saliva showed high levels of two new fragments of the polymeric immunoglobulin receptor, and of α-defensins 2 and 4. Overall, the salivary proteome of Wilson's disease patients reflected oxidative stress and inflammatory conditions characteristic of the pathology, highlighting differences that could be useful clues of disease exacerbation.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Cabras T,Sanna M,Manconi B,Fanni D,Demelia L,Sorbello O,Iavarone F,Castagnola M,Faa G,Messana Idoi
10.1016/j.jprot.2015.07.033subject
Has Abstractpub_date
2015-10-14 00:00:00pages
154-63eissn
1874-3919issn
1876-7737pii
S1874-3919(15)30087-7journal_volume
128pub_type
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