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Toxicologic Pathology
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*COPPER(II) CHLORIDE
*COPPER, ELEMENTAL
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Journal Article

Inhibition of Copper-Associated Erythrocyte Ghost Membrane Lipid Peroxidation by Hepatic Cytosolic Low Molecular Weight Proteins

Bruce L. Homer

Department of Comparative and Experimental Pathology, College of Veterinary Medicine, University of Florida, Gainesville, Florida 32610

Kenneth R. Pierce

Department of Veterinary Pathology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77343-4463

Charles H. Bridges

Department of Veterinary Pathology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77343-4463

James E. Womack

Department of Veterinary Pathology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77343-4463

Blair A. Sowa

Department of Veterinary Pathology, College of Veterinary Medicine, Texas A&M University, College Station, Texas 77343-4463

Ramon C. Littell

Department of Statistics, University of Florida, Gainesville, Florida 32610

Male weanling Fischer rats were injected ip once daily with either 12.5 mg/kg body weight cupric chloride or 2 ml/kg body weight saline for up to 70 days. As the hepatic cytosolic copper increased in copper-treated rats, copper bound to proteins of different molecular weights; this was determined by gel filtration chromatography. Hepatic cytosolic copper from rats treated with cupric chloride for 14 days eluted in 3 peaks. These included a 150,000 + dalton peak, a 29,000 dalton peak and an 11,000-12,800 dalton peak. In addition to these peaks, hepatic cytosolic copper from rats treated with cupric chloride for ≥28 days also eluted in a 4th, but shorter, 6,000-7,000 dalton peak. Hepatic cytosolic copper from saline-treated rats eluted only in a single 29,000 dalton peak. Experiments using an erythrocyte ghost membrane model of copper-associated lipid peroxidation demonstrated that incubation of membranes with protein-bound copper eluted in the 11,000-12,000 dalton peak was associated with less lipid peroxidation than incubation of membranes with cupric chloride or protein-bound copper eluted in the 150,000+ dalton peak. Experimental results suggest that the ability of copper to catalyze lipid peroxidation is significantly reduced by binding with hepatic cytosolic low molecular weight proteins but not by binding with hepatic cytosolic high molecular weight proteins.

Key Words: Copper • toxicity • lipid peroxidation • copper-binding proteins • liver • rat • erythrocyte

Toxicologic Pathology, Vol. 19, No. 3, 206-213 (1991)
DOI: 10.1177/019262339101900302
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This Article
Right arrow Abstract Freely available
Right arrow Free Full Text (Free PDF) Free
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 Add to Saved Citations
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Request Reprints
Right arrow Add to My Marked Citations
Citing Articles
Right arrow Citing Articles via Google Scholar
Right arrow Citing Articles via Scopus
Google Scholar
Right arrow Articles by Homer, B. L.
Right arrow Articles by Littell, R. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Homer, B. L.
Right arrow Articles by Littell, R. C.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*COPPER(II) CHLORIDE
*COPPER, ELEMENTAL
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?