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Am J Physiol Regul Integr Comp Physiol 293: R1882-R1892, 2007. First published September 12, 2007; doi:10.1152/ajpregu.00383.2007
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GENETICALLY MODIFIED ANIMALS AND MODEL ORGANISMS

Oxidative stress response and gene expression with acute copper exposure in zebrafish (Danio rerio)

Paul M. Craig, Chris M. Wood, and Grant B. McClelland

Department of Biology, McMaster University, Hamilton, Ontario, Canada

Submitted 31 May 2007 ; accepted in final form 11 September 2007

In fish, environmental pollution is one factor that induces oxidative stress, and this can disturb the natural antioxidant defense system. Oxidative stress has been well characterized in vitro, yet the in vivo effects of metal-induced oxidative stress have not been extensively studied. In two experiments we examined the impacts of copper (Cu) on gene expression, oxidative damage, and cell oxidative capacity in liver and gill of zebrafish. In the first experiment, soft water-acclimated zebrafish were exposed to 8 and 15 µg/l Cu for 48 h. This exposure resulted in significant increases in gene expression of cytochrome c oxidase subunit 17 (COX-17) and catalase, associated with both increased Cu load and protein carbonyl concentrations in the gill and liver after 48 h. In addition, we examined the potential protective effects of increased waterborne Ca2+ (3.3 mM) and Na+ (10 mM) on acute Cu toxicity. While both treatments were effective at reducing liver and/or gill Cu loads and attenuating oxidative damage at 48 h, 10 mM Na+ was more protective than 3.3 mM Ca2+. There were variable changes in the maximal activities of COX and citrate synthase (CS), indicating possible alterations in cell oxidative capacity. Moreover, Cu affected COX-to-CS ratios in both gill and liver, suggesting that Cu alters normal mitochondrial biogenic processes, possibly though metallochaperones like COX-17. Overall, this study provides important steps in determining the transcriptional and physiological endpoints of acute Cu toxicity in a model tropical species.

gene expression; oxidative capacity; catalase; COX-17; protein-carbonyls



Address for reprint requests and other correspondence: P. M. Craig, Dept. of Biology, McMaster Univ., 1280 Main St. West, Hamilton, ON L8S 4K1 Canada (e-mail: craigpm{at}mcmaster.ca)




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