Human copper-zinc superoxide dismutase

Ceballos-Picot, I., Nicole, A., Briand, P., Grimber, G., Delacourte, A., Defossez, A., Javoy-Agid, F., Lafon, M., Blouin, J.L. and Sinet, P.M. (1991). Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice animal model of gene dosage effects in Down s syndrome. Brain Res, 552, 198-214. 

C2. Ceballos-Picot, I., Trivier, J.-M., Nicole, A., Sinet, P.-M., and Thevenin, M., Age-correlated modifications of copper-zinc superoxide dismutase and glutathione-related enzyme activities in human erythrocytes. Clin. Chem. 38 66-70 (1992). 

Yang G, Chan PH, Chen J, Cadson E, Chen SF, Weinstein P, Epstein CJ, Kamii H (1994) Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia. Stroke 25 165-170... 

Bergeron C, Petrunka C, Weyer L (1996) Copper/zinc superoxide dismutase expression in the human central nervous system. Correlation with selective neuronal vulnerability. Am J Pathol... 

From One Type 2 Copper Protein to Another Type 2 Copper Protein. It has been shown that a type 2 copper protein called copper-zinc superoxide dismutase (CuZnSOD) (Figure 15b) shares the same overall scaffold as its copper chaperone protein called copper chaperone for SOD (CCS). All of e zinc site ligands and three of four copper site histidine ligands in CuZnSOD are conserved in human CCS (hCCS). The zinc site in hCCS displayed the same structure as in CuZnSOD. The fourth ligand in the copper site of CuZnSOD is replaced by an aspartate residue in hCCS. Although aspartate could... 

Goto JJ, Gralla EB, Valentine JS, Cabelli DE. (1998) Reactions of hydrogen peroxide with FALS mutant human copper-zinc superoxide dismutases studied by pulse radiolysis. J Biol Chem 273 30104-30109. 

Nagai M, Aoki M, Miyoshi I, Kato M, Pasinelh P, Kasai N, Brown RH, Jr., Itoyama Y (2001) Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis Associated mutations develop motor nemon disease. J Neurosci 21 9246-9254. 

M27. Miyata-Asano, M., Ito, K., Ikeda, H., and Sekiguchi, S., Purification of copper-zinc-superoxide dismutase and catalase from human erythrocytes by copper-chelate affinity chromatography. J. Chromatogr. 370, 501-507 (1986). 

Oka, S., Ogino, K., Matsuura, S., Yoshimura, S., Yamamoto, K., Okazaki, Y., Takemoto, T., Kato, N., and Uda, T Human serum immuno-reactive copper, zinc-superoxide dismutase assayed with an enzyme monoclonal immunosorbent in patients with digestive cancer. Clin. Chim. Acta 182, 209-220 (1989). 

W8. Weselake, R. J., Chesney, S. L., Petkau, A., and Friese, A. D., Purification of human copper,zinc superoxide dismutase by copper chelate affinity chromatography. Anal. Biochem. 155, 193-197 (1986). 

Tribble DL, Gong EL, Leeuwenburgh C, et al. Fatty streak formation in fat-fed mice expressing human copper-zinc superoxide dismutase. Arterioscler Thromb Vase Biol 1997 17 1734-1740. 

Antonyuk, S.V., Strange, R.W., Marklund, S.L., Hasnain, S.S., 2009. The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution insights into heparin and collagen binding. J. Mol. Biol. 388, 310-326. 

Kamnakaran, C., Zhang, H., Crow, J.P., Anthohne, W.E., Kalyanaraman, B., 2004. Direct probing of copper active site and free radical formed during bicarbonate-dependent peroxidase activity of bovine and human copper, zinc-superoxide dismutases. Low-temperature electron paramagnetic resonance and electron nuclear double resonance studies. J. Biol. Chem. 279, 32534—32540. 

Beyer, W. F., Jr., Fridovich, 1., Mullenbach, G. T., and Hallewell, R. (1987). Examination of the role of arginine-143 in the human copper and zinc superoxide dismutase by site-specific mutagenesis. J. Biol. Chem, 262, 11182-11187. 

Copper occurs in almost all life forms and it plays a role at the active site of a large number of enzymes. Copper is the third most abundant transition metal in the human body after iron and zinc. Enzymes of copper include superoxide dismutase, tyrosinase, nitrite reductase and cytochrome c oxidase. Most copper proteins and enzymes have roles as electron transfer agents and in redox reactions, as Cu(II) and Cu(I) are accessible. 

Marklund, S.L., Westman, N.G., Lundgren, E. and Roos, G. (1982). Copper and zincsuperoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues. Cancer Res. 42, 1955-1961. 

Copper is an essential element to most life forms. In humans it is the third most abundant trace element only iron and zinc are present in higher quantity. Utilization of copper usually involves a protein active site which catalyzes a critical oxidation reaction, e.g., cytochrome oxidase, amine oxidases, superoxide dismutase, ferroxidases, dopamine-/ -hydrox-ylase, and tyrosinase. Accordingly, animals exhibit unique homeostatic mechanisms for the absorption, distribution, utilization, and excretion of copper (J). Moreover, at least two potentially lethal inherited diseases of copper metabolism are known Wilson s Disease and Menkes s Kinky Hair Syndrome (I). 

Copper is a cofactor in several enzymes, including lysyl oxidase and superoxide dismutase. Ceruloplasmin, a deep-blue glycoprotein, is the principal copper-containing protein in blood. It is used to transport Cu2+ and maintain appropriate levels of Cu2+ in the body s tissues. Ceruloplasmin also catalyzes the oxidation of Fe2+ to Fe3+, an important reaction in iron metabolism. Because the metal is widely found in foods, copper deficiency is rare in humans. Deficiency symptoms include anemia, leukopenia (reduction in blood levels of white blood cells), bone defects, and weakened arterial walls. The body is partially protected from exposure to excessive copper (and several other metals) by metal-lothionein, a small, metal-binding protein that possesses a large proportion of cysteine residues. Certain metals (most notably zinc and cadmium) induce the synthesis of metallothionein in the intestine and liver. 

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