Source:http://linkedlifedata.com/resource/pubmed/id/16962996
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2006-9-22
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| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Butyrylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfoxides
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0006-291X
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
27
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| pubmed:volume |
349
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
931-8
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16962996-Acetylcholinesterase,
pubmed-meshheading:16962996-Binding Sites,
pubmed-meshheading:16962996-Butyrylcholinesterase,
pubmed-meshheading:16962996-Cells, Cultured,
pubmed-meshheading:16962996-Computer Simulation,
pubmed-meshheading:16962996-Epidermis,
pubmed-meshheading:16962996-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:16962996-Humans,
pubmed-meshheading:16962996-Hydrogen Peroxide,
pubmed-meshheading:16962996-Keratinocytes,
pubmed-meshheading:16962996-Melanocytes,
pubmed-meshheading:16962996-Methionine,
pubmed-meshheading:16962996-Models, Molecular,
pubmed-meshheading:16962996-Oxidation-Reduction,
pubmed-meshheading:16962996-Oxidative Stress,
pubmed-meshheading:16962996-Protein Binding,
pubmed-meshheading:16962996-Protein Structure, Tertiary,
pubmed-meshheading:16962996-RNA, Messenger,
pubmed-meshheading:16962996-Sulfoxides,
pubmed-meshheading:16962996-Vitiligo
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| pubmed:year |
2006
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| pubmed:articleTitle |
Butyrylcholinesterase is present in the human epidermis and is regulated by H2O2: more evidence for oxidative stress in vitiligo.
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| pubmed:affiliation |
Clinical and Experimental Dermatology/Department of Biomedical Sciences, University of Bradford, Bradford BD7 1DP, UK. K.Schallreuter@bradford.ac.uk <K.Schallreuter@bradford.ac.uk>
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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