Document Detail


Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats.
MedLine Citation:
PMID:  15042443     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In order to investigate the relationship between lens opacities and the various modifications of lens proteins, we analyzed and compared the properties of lens proteins of 85-day old normal Wistar rats and the hereditary cataract model, ICR/f rats. The present study identified many differences between normal and mutant lens proteins. In the ICR/f mutant rats, the relative amounts of gamma-crystallin decreased and high molecular weight (HMW) protein increased. Racemization and isomerization of Asp-151 of alpha A-crystallin was observed in the mutant ICR/f rats, and Met-1 of alpha A-crystallin was oxidized to methionine sulfoxide. These modifications were not found in the age-matched normal rats. These tendencies are consistent with aged and cataractous human lenses.
Authors:
N Fujii; N Takeuchi; N Fujii; T Tezuka; K Kuge; T Takata; A Kamei; T Saito
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2003-12-18
Journal Detail:
Title:  Amino acids     Volume:  26     ISSN:  0939-4451     ISO Abbreviation:  Amino Acids     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-25     Completed Date:  2004-12-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  147-52     Citation Subset:  IM    
Affiliation:
Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan. nfujii@HL.rri.kyoto-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Aging / physiology
Animals
Aspartic Acid / analogs & derivatives,  chemistry,  metabolism
Cataract / genetics,  metabolism*
Disease Models, Animal
Humans
Isomerism
Lens, Crystalline / chemistry,  metabolism
Methionine / metabolism
Molecular Structure
Oxidation-Reduction
Peptides / chemistry
Protein Processing, Post-Translational*
Rats
Rats, Mutant Strains
Rats, Wistar
Time Factors
alpha-Crystallin A Chain / chemistry*,  metabolism*,  physiology
Chemical
Reg. No./Substance:
0/Peptides; 0/alpha-Crystallin A Chain; 56-84-8/Aspartic Acid; 63-68-3/Methionine

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


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