Document Detail


Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism.
MedLine Citation:
PMID:  15890616     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Peroxiredoxin 6 (Prdx6), a bifunctional 25-kDa protein with both GSH peroxidase and phospholipase A2 activities, is the only mammalian 1-Cys member of the peroxiredoxin superfamily and is expressed in all major organs, with a particularly high level in lung. Prdx6 uses GSH as an electron donor to reduce H2O2 and other hydroperoxides including phospholipid hydroperoxides at approximately 5 micromol/mg protein/min with K1 approximately 3 x 10(6) M(-1) s(-1). Oxidation of the Cys47 to a sulfenic acid during catalysis requires piGST-catalyzed glutathionylation and reduction with GSH to complete the enzymatic cycle. Prdx6 stably overexpressed in cells protected against oxidative stress, whereas antisense treatment resulted in oxidant stress and apoptosis. Adenoviral-mediated overexpression of Prdx6 in mouse lungs protected against the toxicity of hyperoxia, whereas Prdx6-null mice were more sensitive to the effects of hyperoxia or paraquat. We postulate that Prdx6 functions in antioxidant defense mainly by facilitating repair of damaged cell membranes via reduction of peroxidized phospholipids. The PLA2 activity of Prdx6 is Ca2+ independent and maximal at acidic pH. Inhibition of PLA2 activity results in alterations of lung surfactant phospholipid synthesis and turnover. Thus, Prdx6, a unique mammalian peroxiredoxin, is an important antioxidant enzyme and has a major role in lung phospholipid metabolism.
Authors:
Yefim Manevich; Aron B Fisher
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Free radical biology & medicine     Volume:  38     ISSN:  0891-5849     ISO Abbreviation:  Free Radic. Biol. Med.     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-05-13     Completed Date:  2005-10-06     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8709159     Medline TA:  Free Radic Biol Med     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1422-32     Citation Subset:  IM    
Affiliation:
Institute for Environmental Medicine, University of Pennsylvania Medical Center, Philadelphia, PA 19104, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anoxia / metabolism
Antioxidants / chemistry,  metabolism
Apoptosis
Binding Sites
Calcium / metabolism
Cell Line, Tumor
Electrons
Glutathione / chemistry,  metabolism
Humans
Hydrogen Peroxide / pharmacology
Hydrogen-Ion Concentration
Kinetics
Lung / metabolism
Mice
Mice, Inbred C57BL
Models, Chemical
Models, Molecular
Oxidative Stress
Oxygen / metabolism
Peroxidases / biosynthesis*,  chemistry,  metabolism,  physiology
Peroxiredoxin VI
Peroxiredoxins
Phospholipases A / chemistry
Phospholipases A2
RNA, Messenger / metabolism
Structure-Activity Relationship
Time Factors
Tissue Distribution
Grant Support
ID/Acronym/Agency:
HL19737/HL/NHLBI NIH HHS; HL65543/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Antioxidants; 0/RNA, Messenger; 70-18-8/Glutathione; 7440-70-2/Calcium; 7722-84-1/Hydrogen Peroxide; 7782-44-7/Oxygen; EC 1.11.1.-/Peroxidases; EC 1.11.1.15/PRDX6 protein, human; EC 1.11.1.15/Peroxiredoxin VI; EC 1.11.1.15/Peroxiredoxins; EC 1.11.1.15/Prdx6 protein, mouse; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2

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


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