Document Detail


Assays of proteasome activity in relation to aging.
MedLine Citation:
PMID:  12470834     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteasomes play a major role in intracellular protein turnover. They exist in cells in several different molecular forms including 20S proteasomes, 26S proteasomes and PA28-20S proteasome complexes. In this study we have compared the properties of these purified proteasome complexes to try to design assays that will distinguish between the different complexes (26S proteasome, 20S proteasome, PA28-20S proteasome) in cell extracts. Although the different purified complexes were found to have differences in stability, and in their sensitivity to low concentrations of SDS and salt, the results suggest that it is not straightforward to assay selectively for each type of complex in cell extracts. The relative contribution of different proteasome complexes varies in different cell types and there may be other proteases present which hydrolyse the chosen substrate. Proteasome assays carried out under defined conditions allow comparisons of activity in cell extracts as a function of age, but separation by gel filtration on a Superose 6 column was found to be a useful method for determining the level of different proteasome related complexes.
Authors:
A Jennifer Rivett; Suchira Bose; Alexander J Pemberton; Paul Brooks; David Onion; David Shirley; Fiona L L Stratford; Katia Forti
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Experimental gerontology     Volume:  37     ISSN:  0531-5565     ISO Abbreviation:  Exp. Gerontol.     Publication Date:    2002 Oct-Nov
Date Detail:
Created Date:  2002-12-09     Completed Date:  2003-04-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0047061     Medline TA:  Exp Gerontol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1217-22     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK. j.rivett@bristol.ac.uk
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MeSH Terms
Descriptor/Qualifier:
Aging / physiology*
Animals
Cells, Cultured
Chromatography, Gel / methods
Cysteine Endopeptidases / metabolism*
Humans
Multienzyme Complexes / metabolism*
Proteasome Endopeptidase Complex
Proteins / metabolism
Rats
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; 0/Proteins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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