Identifying changes in the synaptic proteome of cirrhotic alcoholic superior frontal gyrus

Etheridge, N., Mayfield, R. D., Harris, R. A. and Dodd, P. R. (2011) Identifying changes in the synaptic proteome of cirrhotic alcoholic superior frontal gyrus. Current Neuropharmacology, 9 1: 122-128. doi:10.2174/157015911795017164

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Author Etheridge, N.
Mayfield, R. D.
Harris, R. A.
Dodd, P. R.
Title Identifying changes in the synaptic proteome of cirrhotic alcoholic superior frontal gyrus
Journal name Current Neuropharmacology   Check publisher's open access policy
ISSN 1570-159X
1875-6190
Publication date 2011-03
Sub-type Article (original research)
DOI 10.2174/157015911795017164
Volume 9
Issue 1
Start page 122
End page 128
Total pages 7
Place of publication Bussum, Netherlands
Publisher Bentham Science Publishers
Collection year 2012
Language eng
Formatted abstract
Hepatic complications are a common side-effect of alcoholism. Without the detoxification capabilities of the liver, alcohol misuse induces changes in gene and protein expression throughout the body. A global proteomics approach was used to identify these protein changes in the brain. We utilised human autopsy tissue from the superior frontal gyrus (SFG) of six cirrhotic alcoholics, six alcoholics without comorbid disease, and six non-alcoholic non-cirrhotic controls. Synaptic proteins were isolated and used in two-dimensional differential in-gel electrophoresis coupled with mass spectrometry. Many expression differences were confined to one or other alcoholic sub-group. Cirrhotic alcoholics showed 99 differences in protein expression levels from controls, of which half also differed from non-comorbid alcoholics. This may reflect differences in disease severity between the sub-groups of alcoholics, or differences in patterns of harmful drinking. Alternatively, the protein profiles may result from differences between cirrhotic and non-comorbid alcoholics in subjects' responses to alcohol misuse. Ten proteins were identified in at least two spots on the 2D gel; they were involved in basal energy metabolism, synaptic vesicle recycling, and chaperoning. These post-translationally modified isoforms were differentially regulated in cirrhotic alcoholics, indicating a level of epigenetic control not previously observed in this disorder.
Keyword Alcoholism
Cirrhosis
Proteomics
Post-translational modification
Ethylmaleimide-sensitive factor
S-nitrosylation
In-vivo
Stress-proteins
Brain proteins
Liver-disease
Rat
Phosphorylation
Dynamin
Dehydrogenase
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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Citation counts: TR Web of Science Citation Count  Cited 7 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 17 May 2011, 14:43:04 EST by Dr Naomi Etheridge on behalf of School of Chemistry & Molecular Biosciences