Document Detail


The mutual sparing effects of selenium and vitamin E in animal nutrition may be further explained by the discovery that mammalian thioredoxin reductase is a selenoenzyme.
MedLine Citation:
PMID:  8722124     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The recent discovery that mammalian thioredoxin reductase is a selenoprotein furnishes an additional explanation of the mutual sparing roles of selenium and vitamin E in cellular antioxidant systems. Thioredoxin reductases isolated from human lung adenocarcinoma cells, human Jurkat T-cells and HeLa cells contain selenocysteine which is located in a C-terminal tripeptide, -Cys-SeCys-Gly.
Authors:
T Tamura; V Gladyshev; S Y Liu; T C Stadtman
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  BioFactors (Oxford, England)     Volume:  5     ISSN:  0951-6433     ISO Abbreviation:  Biofactors     Publication Date:    1995-1996
Date Detail:
Created Date:  1997-01-17     Completed Date:  1997-01-17     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8807441     Medline TA:  Biofactors     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  99-102     Citation Subset:  IM    
Affiliation:
Okayama University, Faculty of Agriculture, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animal Nutritional Physiological Phenomena*
Animals
Antioxidants / pharmacology
Humans
Mammals / metabolism*
Molecular Sequence Data
Selenium / chemistry,  pharmacology*
Selenocysteine / chemistry*
Thioredoxin-Disulfide Reductase / chemistry*
Tumor Cells, Cultured
Vitamin E / pharmacology*
Chemical
Reg. No./Substance:
0/Antioxidants; 10236-58-5/Selenocysteine; 1406-18-4/Vitamin E; 7782-49-2/Selenium; EC 1.8.1.9/Thioredoxin-Disulfide Reductase

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


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