References
- Antonyuk, S.V., Strange, R.W., Marklund, S.L., and 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. https://doi.org/10.1016/j.jmb.2009.03.026
- Arnelle, D.R., Day, B.J., and Stamler, J.S. (1997). Diethyl dithiocarbamate- induced decomposition of S-nitrosothiols. Nitric Oxide. 1, 56-64. https://doi.org/10.1006/niox.1996.0107
- Bae, J.Y., Koo, B.K., Ryu, H.B., Song, J.A., Nguyen, M.T., Vu, T.T., Son, Y.J., Lee, H.K., and Choe, H. (2013). Cu/Zn incorporation during purification of soluble human EC-SOD from E. coli stabilizes proper disulfide bond formation. Appl. Biochem. Biotechnol. 169, 1633-1647. https://doi.org/10.1007/s12010-012-0025-x
- Beyer, W., Imlay, J., and Fridovich, I. (1991). Superoxide dismutases. Prog. Nucl. Acid Res. Mol. Biol. 40, 221-253. https://doi.org/10.1016/S0079-6603(08)60843-0
- Bowler, R.P., Nicks, M., Warnick, K., and Crapo, J.D. (2002). Role of extracellular superoxide dismutase in bleomycin-induced pulmonary fibrosis. Am. J. Physiol. Lung Cell Mol. Physiol. 282, L719-726. https://doi.org/10.1152/ajplung.00058.2001
- Bowler, R.P., Nicks, M., Tran, K., Tanner, G., Chang, L.Y., Young, S.K., and Worthen, G.S. (2004). Extracellular superoxide dismutase attenuates lipopolysaccharide-induced neutrophilic inflammation. Am. J. Respir. Cell. Mol. Biol. 31, 432-439. https://doi.org/10.1165/rcmb.2004-0057OC
- Byun, S.J., Ji, M.R., Jang, Y.J., Hwang, A.I., Chung, H.K., Kim, J.S., Kim, K.W., Yoo, J.G., and Kim, T.Y. (2013). Human extracellular superoxide dismutase (EC-SOD) expression in transgenic chicken. BMB Rep. 46, 404-409. https://doi.org/10.5483/BMBRep.2013.46.8.251
- Carlsson, L.M., Jonsson, J., Edlund, T., and Marklund, S.L. (1995). Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia. Proc. Natl. Acad. Sci. USA 92, 6264-6268. https://doi.org/10.1073/pnas.92.14.6264
- Chen, H.L., Yen, C.C., Tsai, T.C., Yu, C.H., Liou, Y.J., and Lai, Y.W. (2006). Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris. J. Agric. Food Chem. 54, 8041-8047. https://doi.org/10.1021/jf061379x
- Chen, C.M., Lai, Z.L., Yen, C.C., Wang, M.L., and Chen, H.L. (2013). Cloning and expression of the human extracellular superoxide dismutase (EC-SOD) gene in probiotic lactobacillus casei. Int. J. Biosci. Biochem. Bioinforma 3, 557-561.
- Demchenko, I.T., Oury, T.D., Crapo, J.D., and Piantadosi, C.A. (2002). Regulation of the brain's vascular responses to oxygen. Circ. Res. 91, 1031-1037. https://doi.org/10.1161/01.RES.0000043500.03647.81
- Didion, S.P., Hathaway, C.A., and Faraci, F.M. (2001). Superoxide levels and function of cerebral blood vessels after inhibition of CuZn-SOD. Am. J. Physiol. Heart Circ. Physiol. 281, H1697-H1703. https://doi.org/10.1152/ajpheart.2001.281.4.H1697
- Due, A.V., Petersen, S.V., Valnickova, Z., Ostergaard, L., Oury, T.D., and Crapo, J.D. (2006). Extracellular superoxide dismutase exists as an octamer. FEBS Lett. 580, 1485-1489. https://doi.org/10.1016/j.febslet.2006.01.081
- Edlund, A., Edlund, T., Hjalmarsson, K., Marklund, S.L., Sandstrom, J., Stromqvist, M., and Tibell, L. (1992). A non-glycosylated extracellular superoxide dismutase variant. Biochem. J. 288, 451-456. https://doi.org/10.1042/bj2880451
- Folz, R.J., Abushamaa, A.M., and Suliman, H.B. (1999). Extracellular superoxide dismutase in the airways of transgenic mice reduces inflammation and attenuates lung toxicity following hyperoxia. J. Clin. Invest. 103, 1055-1066. https://doi.org/10.1172/JCI3816
- He, H.J., Yuan, Q.S., Yang, G. Z., and Wu, X.F. (2002). High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells. Protein Expr. Purif. 24, 13-17. https://doi.org/10.1006/prep.2001.1529
- Iqbal, J., and Whitney, P. (1991). Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutases. Free Radic. Biol. Med. 10, 69-77. https://doi.org/10.1016/0891-5849(91)90023-V
- Li, J., Li, P.F., Dietz, R., and von Harsdorf, R. (2002). Intracellular superoxide induces apoptosis in VSMCs: role of mitochondrial membrane potential, cytochrome C and caspases. Apoptosis 7, 511-517. https://doi.org/10.1023/A:1020639025669
- Liu, T., Qian, W.J., Gritsenko, M.A., Camp 2nd, D.G., Monroe, M.E., Moore R.J., and Smith, R.D. (2005). Human plasma Nglycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 4, 2070-2080. https://doi.org/10.1021/pr0502065
- Mamo, L.B., Suliman, H.B., Giles, B.L., Auten, R.L., Piantadosi, C.A., and Nozik-Grayck, E. (2004). Discordant extracellular superoxide dismutase expression and activity in neonatal hyperoxic lung. Am. J. Respir. Crit. Care Med. 170, 313-318. https://doi.org/10.1164/rccm.200309-1282OC
- Nozik-Grayck, E., Suliman, H.B., and Piantadosi, C.A. (2005). Extracellular superoxide dismutase. Int. J. Biochem. Cell Biol. 37, 2466-2471. https://doi.org/10.1016/j.biocel.2005.06.012
- Ohta, H., Adachi, T., and Hirano, K. (1994). Internalization of human extracellular- superoxide dismutase by bovine aortic endothelial cells. Free Rad. Biol. Med. 16, 501-507. https://doi.org/10.1016/0891-5849(94)90128-7
- Oury, T.D., Day, B.J., and Crapo, J.D. (1996a). Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability. Lab. Invest. 75, 617- 636.
- Oury, T.D., Day, B.J., and Crapo, J.D. (1996b). Extracellular superoxide dismutase in vessels and airways of humans and baboons. Free Radic. Biol. Med. 20, 957-965. https://doi.org/10.1016/0891-5849(95)02222-8
- Oury, T.D., Schaefer, L.M., Fattman, C.L., Choi, A., Weck, K.E., and Watkins, S.C. (2002). Depletion of pulmonary EC-SOD after exposure to hyperoxia. Am J. Physiol. Lung Cell Mol. Physiol. 283, L777-784. https://doi.org/10.1152/ajplung.00011.2002
-
Petersen, S.V., Olsen, D.A., Kenney, J.M., Oury, T.D., Valnickova, Z., Thogersen, I.B., Crapo, and J.D., Enghild, J.J. (2005). The high concentration of
$Arg^{213}{\rightarrow}Gly$ extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities. Biochem. J. 385, 427-432. https://doi.org/10.1042/BJ20041218 - Ryu, K., Kim, Y.H., Lee, J.S., Jeon, B., Kim, and T.Y. (2008). Increased yield of high-purity and active tetrameric recombinant human EC-SOD by solid phase refolding. J. Microbiol. Biotechnol. 18, 1648-1654.
- Suliman, H.B., Ali, M., and Piantadosi, C.A. (2004). Superoxide dismutase-3 promotes full expression of the EPO response to hypoxia. Blood 104, 43-50. https://doi.org/10.1182/blood-2003-07-2240
- Tan, A.S., and Berridge, M.V. (2000). Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening antiinflammatory agents. J. Immunol. Methods 238, 59-68. https://doi.org/10.1016/S0022-1759(00)00156-3
- Tan, R.J., Fattman, C.L., Watkins, S.C., and Oury, T.D (2004). Redistribution of pulmonary EC-SOD after exposure to asbestos. J. Appl. Physiol. 97, 2006-2013. https://doi.org/10.1152/japplphysiol.00480.2004
- Tibell, L., Hjalmarsson, K., Edlund, T., Skogman, G., Engstrom, V., and Marklund, S.L. (1987). Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product. Proc. Natl. Acad. Sci. USA 84, 6634-6638. https://doi.org/10.1073/pnas.84.19.6634
- Yun, J.H., Kim, K., Jung, Y., Park, J.H., Cho H.S., and Lee, W. (2015). Co-expression of human agouti-related protein enhances expression and stability of human melanocortin-4 receptor. Biochem. Biophys. Res. Commun. 456, 116-121. https://doi.org/10.1016/j.bbrc.2014.11.044
- Zelko, I.N., Mariani, T.J., and Folz, R.J. (2002). Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radical. Biol. Med. 33, 337-349. https://doi.org/10.1016/S0891-5849(02)00905-X
Cited by
- Production of functional human CuZn-SOD and EC-SOD in bitransgenic cloned goat milk vol.27, pp.4, 2018, https://doi.org/10.1007/s11248-018-0080-3
- Zinc(II) ion promotes anti-inflammatory effects of rhSOD3 by increasing cellular association vol.50, pp.2, 2016, https://doi.org/10.5483/bmbrep.2017.50.2.150
- Interchangeable utilization of metals: New perspectives on the impacts of metal ions employed in ancient and extant biomolecules vol.297, pp.6, 2021, https://doi.org/10.1016/j.jbc.2021.101374