Document Detail


Metabolism of hydroperoxy-phospholipids in human hepatoma HepG2 cells.
MedLine Citation:
PMID:  8978487     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two enzymatic mechanisms have been proposed for the metabolism of hydroperoxy-phospholipids: i) the combined action of phospholipase A2 and glutathione peroxidase, and/or ii) direct enzymatic reduction. The latter reaction may be catalyzed by selenium-dependent phospholipid hydroperoxide glutathione peroxidase and/or by glutathione S-transferase alpha. To study the pathway of this reaction, we used human hepatoma HepG2 cells into which was incorporated labeled, hydroperoxy-phospholipids. The major product of incorporated l-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl)-L-3-phosphatidylcholine was the corresponding hydroxy-phospholipid with no hydroxy- or hydroperoxy-fatty acids. The contributions to reduction of hydroperoxy-phospholipids in HepG2 cells from glutathione S-transferase Al and phospholipid hydroperoxide glutathione peroxidase were calculated to be 0.5% and 99.5%, respectively. Increasing selenium in the cell culture medium led to increases in selenium-dependent phospholipid hydroperoxide glutathione peroxidase activity but not in glutathione S-transferase alpha. This increase in the selenium-dependent enzyme was paralleled by a concomitant increase in the extent of reduction of the incorporated hydroperoxy-phospholipid. We conclude that the main metabolic fate of hydroperoxy-phospholipids in HepG2 cells is by direct reduction to hydroxy-phospholipids by phospholipid hydroperoxide glutathione peroxidase but also by glutathione S-transferase alpha, and that phospholipase A2/selenium-dependent glutathione peroxidase does not play a significant role in the reduction.
Authors:
Y Bao; G Williamson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of lipid research     Volume:  37     ISSN:  0022-2275     ISO Abbreviation:  J. Lipid Res.     Publication Date:  1996 Nov 
Date Detail:
Created Date:  1997-03-25     Completed Date:  1997-03-25     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0376606     Medline TA:  J Lipid Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2351-60     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Institute of Food Research, Norwich Laboratory, Norwich Research Park, Colney, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Carcinoma, Hepatocellular / metabolism*
Chromatography, High Pressure Liquid
Glutathione Peroxidase / metabolism
Glutathione Transferase / metabolism
Humans
Lipid Peroxides / metabolism*
Liver Neoplasms / metabolism*
Phospholipases A / metabolism
Phospholipases A2
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Lipid Peroxides; EC 1.11.1.9/Glutathione Peroxidase; EC 2.5.1.18/Glutathione Transferase; 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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