Document Detail


Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival.
MedLine Citation:
PMID:  15853675     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
One of the most oxidation-sensitive amino acids is methionine. Oxidation of methionine to methionine sulfoxide (MetO) could, on the one hand, be an important component of signal transduction pathways and on the other hand, may lower the cellular antioxidant capacity, alter protein function, interfere with signal transduction, and damage proteins. The latter changes could lead to the accumulation and malfunction of various proteins. As a result, enhanced development of certain diseases and signs of aging may occur. So far, two major enzymes that could reduce MetO in proteins have been described, denoted as MsrA and MsrB (Methionine sulfoxide reductases). In general, Msrs have been shown to be important in protecting cells from oxidative stress throughout many species from bacteria to mammals. In addition, the activities of certain enzymes could be restored or controlled following reduction of their MetO residues, through the Msr system. Of all Msrs, MsrA seems to be important in controlling MetO reduction in general and MsrB, thioredoxin reductase (Trr), and the adhesion capabilities of certain bacterial cells in particular. The recently discovered MsrB can reduce specifically the R-MetO enantiomer while MsrA can reduce specifically the S-MetO enantiomer. Another significant difference between MsrA and MsrB is that the latter's major form in mammalian cells is a selenoprotein. The current review will discuss the major characteristics of methionine sulfoxide reductases as physiological antioxidants, repair systems, and cellular regulating enzymes.
Authors:
Jackob Moskovitz
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Current pharmaceutical design     Volume:  11     ISSN:  1381-6128     ISO Abbreviation:  Curr. Pharm. Des.     Publication Date:  2005  
Date Detail:
Created Date:  2005-04-27     Completed Date:  2005-05-24     Revised Date:  2012-05-28    
Medline Journal Info:
Nlm Unique ID:  9602487     Medline TA:  Curr Pharm Des     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1451-7     Citation Subset:  IM    
Affiliation:
The University of Kansas, Department of Pharmacology and Toxicology, School of Pharmacy, Lawrence, KS 66045-7582, USA. moskovij@ku.edu
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MeSH Terms
Descriptor/Qualifier:
Aging / metabolism*,  pathology
Animals
Antioxidants / metabolism*
Humans
Methionine / analogs & derivatives*,  metabolism*
Methionine Sulfoxide Reductases
Oxidation-Reduction
Oxidative Stress*
Oxidoreductases / metabolism*
Proteins / metabolism*
Selenoproteins
Chemical
Reg. No./Substance:
0/Antioxidants; 0/Proteins; 0/Selenoproteins; 454-41-1/methionine sulfoxide; 63-68-3/Methionine; EC 1.-/Oxidoreductases; EC 1.8.4.-/Methionine Sulfoxide Reductases; EC 1.8.4.11/methionine sulfoxide reductase

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


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