Blood online
Home About Blood Authors Subscriptions Permission Advertising Public Access contact us
 

 
Advanced
Current Issue
First Edition
Archives
Submit to Blood
Search
American Society of Hematology
Meeting Abstracts
Email Alerts
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Right arrow Rights and Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Johnson, R. M.
Right arrow Articles by Ho, Y.-S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Johnson, R. M.
Right arrow Articles by Ho, Y.-S.
Related Collections
Right arrow Red Cells
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

arrow to previous article Previous Article  |  Table of Contents  |  Next Article next article arrow

Blood, 1 September 2000, Vol. 96, No. 5, pp. 1985-1988

RED CELLS

Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides

Robert M. Johnson, Gerard Goyette Jr, Yaddanapudi Ravindranath, and Ye-Shih Ho

From the Department of Biochemistry and Molecular Biology, the Department of Pediatrics, and the Institute of Chemical Toxicology, Wayne State Medical School, Detroit, MI.

The role of glutathione peroxidase in red cell anti-oxidant defense was examined using erythrocytes from mice with a genetically engineered disruption of the glutathione peroxidase-1 (GSHPx-1) gene. Because GSHPx-1 is the sole glutathione peroxidase in the erythrocyte, all red cell GSH peroxidase activity was eliminated. Oxidation of hemoglobin and membrane lipids, using the cis-parinaric acid assay, was determined during oxidant challenge from cumene hydroperoxide and H2O2. No difference was detected between wild-type red cells and GSHPx-1-deficient cells, even at high H2O2 exposures. Thus, GSHPx-1 appears to play little or no role in the defense of the erythrocyte against exposure to peroxide. Simultaneous exposure to an H2O2 flux and the catalase inhibitor 3-amino-1,2,4-triazole supported this conclusion. Hemoglobin oxidation occurred only when catalase was depleted. Circulating erythrocytes from the GSHPx-1-deficient mice exhibited a slight reduction in membrane thiols, indicating that high exposure to peroxides might occur naturally in the circulation.

© 2000 by The American Society of Hematology.
 

Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 BloodHome page
E. Beutler
Glucose-6-phosphate dehydrogenase deficiency: a historical perspective
Blood, January 1, 2008; 111(1): 16 - 24.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
F. M. Low, M. B. Hampton, A. V. Peskin, and C. C. Winterbourn
Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
Blood, March 15, 2007; 109(6): 2611 - 2617.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
R. M. Johnson, G. Goyette Jr, Y. Ravindranath, and Y.-S. Ho
Oxidation of glutathione peroxidase-deficient red cells by organic peroxides
Blood, July 30, 2002; 100(4): 1515 - 1516.
[Full Text] [PDF]


click for free articles
home about blood authors subscriptions permissions advertising public access contact us
  Copyright © 2000 by American Society of Hematology         Online ISSN: 1528-0020