Effect of cadmium exposure on antioxidant enzyme catalase in different tissues of Acrossocheilus fasciatus

Wu, J. P. & Chen, H. C. Effects of cadmium and zinc on oxygen consumption, ammonium excretion, and osmoregulation of white shrimp (litopenaeus vannamei). Chemosphere 57:1591–1598 (2004).

Fassett, D. W. Cadmium: Biological Effects and Occurrence in the Environment. Annu Rev Pharmaco 15:425–435 (1975).

Hare, L. & Tessier, A. Predicting animal cadmium concentrations in lakes. Nature 380:430–432 (1996).

Klaassen, C. D., Liu, J. & Diwan, B. A. Metallothionein protection of cadmium toxicity. Toxicol Appl Pharm 238:215–220 (2009).

Siu, E. R., Mruk, D. D., Porto, C. S. & Cheng, C. Y. Cadmium-induced testicular injury. Toxicol Appl Pharm 238:240–249 (2009).

Han, Y. L. et al. Cloning, characterization and cadmium inducibility of metallothionein in the testes of the mudskipper Boleophthalmus pectinirostris. Ecotox Environ Safe 119:1–8 (2015).

Hollis, L. et al. Cadmium accumulation, gill Cd binding, acclimation, and physiological effects during long term sublethal Cd exposure in rainbow trout. Aquat Toxicol 46:101–119 (1999).

Ercal, N., Gurer-Orhan, H. & Aykin-Burns, N. Toxic metals and oxidative stress part I: mechanisms involved in metal-induced oxidative damage. Curr Top Med Chem 1:529–539 (2001).

Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F. & Vercesi, A. E. Mitochondria and reactive oxygen species. Free Radic Biol Med 47:33–43 (2009).

Buonocore, G., Perrone, S. & Tataranno, M. L. Oxygen toxicity: chemistry and biology of reactive oxygen species. Semin Fetal Neonatal Med 15:86–90 (2010).

Circu, M. L. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 48:49–62 (2010).

Nordberg, J. & Arner, E. S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31:287–312 (2001).

Wei, X. J., Hu, T. J., Chen, J. R. & Wei, Y. Y. Inhibitory effect of carboxymethylpachymaran on cyclophosphamide-induced oxidative stress in mice. Int J Biol Macromol 49:801–805 (2011).

Kashiwagi, A. et al. Comparison of catalase in diploid and haploid Rana rugosa using heat and chemical inactivation techniques. Comp Biochem Physiol B 118:499–503 (1997).

Klotz, M. G., Klassen, G. R. & Loewen, P. C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 14:1–8 (1997).

Yamamoto, K. et al. Catalase from the silkworm, Bombyx mori: gene sequence, distribution, and overexpression. Insect Biochem Mol Biol 35:77–83 (2005).

Scibior, D. & Czeczot, H. Catalase: structure, properties, functions. Postepy Higieny i Medycyny Doswiadczalne 60:70–80 (2006).

Chelikani, P., Fita, I. & Loewen, P. C. Diversity of structures and properties among catalases. Cell Mol Life Sci 61:192–208 (2004).

Kamata, H. et al. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120:49–61 (2005).

Ekanayake, P. M. et al. Cloning, characterization and tissue expression of disk abalone (Haliotis discus discus) catalase. Fish Shellfish Immunol 24:267–278 (2008).

Wu, C. L. et al. Molecular cloning, characterization and mRNA expression of selenium-dependent glutathione peroxidase from abalone Haliotis discus hannai Ino in response to dietary selenium, zinc and iron. Comp Biochem Physiol C Toxicol Pharmacol 152:21–32 (2010).

Lambert, C., Soudant, P., Choquet, G. & Paillard, C. Measurement of Crassostrea gigas hemocyte oxidative metabolism by flow cytometry and the inhibiting capacity of pathogenic vibrios. Fish Shellfish Immunol 15:25–40 (2003).

Liu, C., Tseng, M. & Cheng, W. Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection. Fish Shellfish Immunol 23:34–45 (2007).

Jang, H. H. et al. Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 117:25–35 (2004).

Mao, H. et al. Expression and function analysis of metallothionein in the testis of stone crab Charybdis japonica exposed to cadmium. Aquat Toxicol 124/125:11–21 (2012).

Rhee, S. G. et al. Controlled elimination of intracellular H2O2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid Redox Sign 7:19–26 (2005).

Cao, C. et al. Catalase is regulated by ubiquitination and proteosornal degradation. Biochemistry 42:48–53 (2003).

Yu, L. et al. Autophagic programmed cell death by selective catalase degradation. Proc Natl Acad Sci USA 103:2–7 (2006).

Levine, A., Tenhaken, R., Dixon, R. & Lamb, C. H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79:83–93 (1994).

Eide, M., Karlsen, O. A., Kryvi, H., Olsvik, P. A. & Goksoyr, A. Precision-cut liver slices of Atlantic cod (Gadus morhua): an in vitro system for studying the effects of environmental contaminants. Aquat Toxicol 153:110–115 (2014).

Oliveira, H., Spanò, M., Santos, C. & Pereira, M. L. Adverse effects of cadmium exposure on mouse sperm. Reprod Toxicol 28:550–555 (2009).

Leignel, V., Marchand, J., Moreau, B. & Chénais, B. Metallothionein genes from hydrothermal crabs (Bythograeidae, Decapoad): characterization, sequence analysis, gene expression and comparison with coastal crabs. Comp Biochem Physiol C Toxicol Pharmacol 148:6–13 (2008).