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                            Library & Multimedia
 Reversible and irreversible protein glutathionylation: biological and clinical aspects
NCJ Number
              308541
Journal

*Expert Opinion on Drug Metabolism & Toxicology* Volume: 7 Issue: 7 Dated: 2011 Pages: 891-810
Author(s)
          Arthur JL Cooper;
                        John T Pinto;
                        Patrick S Callery
Date Published

2011
Length
              20 pages
Annotation
              This study examines biological and clinical aspects of reversible and irreversible protein glutathionylation.
Abstract
              This article reviews factors contributing to reversible and irreversible protein glutathionylation and their biomedical implications. It also examines the possibility that certain drugs such as busulfan may be toxic by promoting irreversible glutathionylation. The reader will gain an appreciation of the protective nature and control of function resulting from reversible protein glutathionylation. The reader is also introduced to the recently identified phenomenon of irreversible protein glutathionylation and its possible deleterious effects. Depending in part on the glutathione:glutathione disulfide ratio, reversible protein glutathionylation to a mixed disulfide may occur. Reversible glutathionylation is important in protecting proteins against oxidative stress, guiding correct protein folding, regulating protein activity and modulating proteins critical to redox signaling. The potential also exists for irreversible protein glutathionylation via Michael addition of an -SH group to a dehydroalanyl residue, resulting in formation of a stable, non-reducible thioether linkage. The process of reversible protein glutathionylation is now well established but these findings need to be substantiated at the tissue and organ levels, and also with disease state. That being said, irreversible protein glutathionylation can also occur and this has implications in disease and aging. Toxicologists should consider this when evaluating the possible side effects of certain drugs such as busulfan that may generate a glutathionylating species in vivo. (Published Abstract Provided)
      
  
          Additional Details
Grant Number(s)
        2005-IJ-CX-K014


  
  
        
  Agencies
        NIJ-Sponsored


  
  
        
  Publication Type
        Research (Applied/Empirical)


  
  
        
  Award
        Enhanced Forensic Mass Spectrometry Methods
    
  
  
Date Published: January 1, 2011
    
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