Butyrylcholinesterase is present in the human epidermis and is regulated by H2O2: more evidence for oxidative stress in vitiligo

The human epidermis holds the capacity for autocrine cholinergic signal transduction, but the presence of butyrylcholinesterase (BchE) has not been shown so far. Our results demonstrate that this compartment transcribes a functional BchE. Its activity is even higher compared to acetylcholinesterase...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-10, Vol.349 (3), p.931-938
Main Authors: Schallreuter, Karin U, Gibbons, Nicholas C J, Zothner, Carsten, Elwary, Souna M, Rokos, Hartmut, Wood, John M
Format: Article
Language:English
Subjects:
Acetylcholinesterase - metabolism
Binding Sites
Butyrylcholinesterase - chemistry
Butyrylcholinesterase - genetics
Butyrylcholinesterase - metabolism
Cells, Cultured
Computer Simulation
Epidermis - metabolism
Gene Expression Regulation, Enzymologic
Humans
Hydrogen Peroxide - metabolism
Hydrogen Peroxide - pharmacology
Keratinocytes - enzymology
Melanocytes - enzymology
Methionine - analogs & derivatives
Methionine - metabolism
Models, Molecular
Oxidation-Reduction - drug effects
Oxidative Stress
Protein Binding
Protein Structure, Tertiary
RNA, Messenger - genetics
Sulfoxides - metabolism
Vitiligo - metabolism
Vitiligo - pathology
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Summary:The human epidermis holds the capacity for autocrine cholinergic signal transduction, but the presence of butyrylcholinesterase (BchE) has not been shown so far. Our results demonstrate that this compartment transcribes a functional BchE. Its activity is even higher compared to acetylcholinesterase (AchE). Moreover, we show that BchE is subject to regulation by H(2)O(2) in a concentration-dependent manner as it was recently described for AchE. Epidermal BchE protein expression and enzyme activities are severely affected by H(2)O(2) in vitiligo as previously demonstrated for AchE. Removal/reduction of H(2)O(2) by a pseudocatalase PC-KUS yields normal/increased protein expression and activities. H(2)O(2)-mediated oxidation of methionine residues in BchE was confirmed by FT-Raman spectroscopy. Computer simulation supported major alteration of the enzyme active site and its tetramerisation domain suggesting deactivation of the enzyme due to H(2)O(2)-mediated oxidation. Based on our results we conclude that H(2)O(2) is a major player in the regulation of the cholinergic signal via both AchE and BchE and this signal is severely affected in the epidermis of patients with active vitiligo.
ISSN:0006-291X
DOI:10.1016/j.bbrc.2006.08.138