Superoxide dismutase, extracellular

Karlsson, K., Sandstrom, J., Edlund, A., Edlund, T. and Mark-lund, S.L. (1993). Pharmacokinetics of extracellular superoxide dismutase in the vascular system. Free Rad. Biol. Med. 14, 185-190. 

Sheng, H., Bart, R. D., Oury, T. D., Pearlstein, R. D., Crapo, J. D. and Warner, D. S. Mice overexpressing extracellular superoxide dismutase have increased resistance to focal cerebral ischemia. Neuroscience 88 185-191,1999. 

Park JW, Qi WN, Liu JQ, Urbaniak JR, Folz RJ, Chen LE (2005) Inhibition of iNOS attenuates skeletal muscle reperfusion injury in extracellular superoxide dismutase knockout mice. Microsurgery 25(8) 606-613... 

Li Q, Bolli R, Qiu Y Tang X-L, Guo Y French BA. Gene therapy with extracellular superoxide dismutase protects conscious rabbits against myocardial infarction. Circulation 2001 103 1893-1898. 

Chen ER Bittner HB, Davis RD, Van Trigt R Folz R. Physiological effects of extracellular superoxide dismutase transgene overexpression on myocardial function after ischemia and reperfusion injury. J Thorac Cardiovasc Surg 1998 I 15 450-458. 

Figure 5.5 Tryptic digest of extracellular superoxide dismutase separated by (a) reversed-phase HPLC, using 0.1% (v/v) trifluoracetic acid in an acetonitrile/water gradient, and (b) CZE, using a 100 mM phosphate buffer, pH 2.5. (Reprinted from Ref. 15 with permission.)...

The three-dimensional structure of human extracellular superoxide dismutase (EC-SOD) is unknown. Studies of structure-function relationships have been severely limited by its poor production in mammalian cell lines and failure to be expressed in prokaryotic and yeast systems. In contrast, extra- and intracellular Cu- and Zn-containing superoxide dismutases (CuZn-SOD) are expressed very well in E. coli and yeast. CuZn-SOD is homologous to a large interior fragment of EC-SOD, but lacks its extra N-terminal and C-terminal domains. Fusions of either the N-terminal domain of EC-SOD or both the N- and C-terminal domains of EC-SOD to CuZn-SOD resulted in a domain-swapped enzyme that expressed well and whose characteristics resemble EC-SOD (Stenlund and Tibell, 1999). 

Oury, T. D., Piantadosi, C. A., andCrapo, J. D., Cold-induced brain edema in mice. Involvement of extracellular superoxide dismutase and nitric oxide. J. Biol. Chem. 268,15394—15398 (1993). 

A number of copper requiring enzymes are located at the cell surface or are exported into the extracellular milieu. Examples of such secretory Cu-enzymes include copper requiring ferroxidases that fimction in iron transport (e g. ceruloplasmin, CP), enzymes for neurotransmission (peptidyl amidating enzyme and dopamine hydroxylase), an extracellular superoxide dismutase (SOD) that fimctions in antioxidant defense and enzymes for formation of connective tissue (lysyl oxidase), and pigments (tyrosinase) (reviewed in ). En route to their designated location, each of these enzymes passes through a specialized compartment of the late Golgi where copper insertion takes place. 

Fattman, C.L., Schaefer, L.M., and Oury, T.D. (2003). Extracellular superoxide dismutase in biology and medicine. Free Radic Biol Med 35, 236-56. 

H13. Hjalmarsson, K., Marklund, S. L., Engstrom, A., and Edlund, T., Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc. Natl. Acad. Sci. U.SA. 84, 6340-6344 (1987). 

M7. Marklund, S. L., Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem. J. 222, 649-655 (1984). 

Sheng H, Kudo M, Mackensen GB, Pearlstein RD, Crapo JD, Warner DS. Mice overexpressing extracellular superoxide dismutase have increased resistance to global cerebral ischemia. Exp Neurol 2000 163 392-398. 

Stromqvist M, Houdebine L, Andersson J, et al. Recombinant human extracellular superoxide dismutase produced in milk of transgenic rabbits. Transgenic Res., 1997 6(4) 271-278. 

Extracellular superoxide dismutase (ecSOD) 317 Extrachromosomal palindrome 664... 

Ceruloplasmin Cu-amino acid complexes Cu-albumin complex (and extracellular superoxide dismutases)... 

Geriach D, Reighardt W and Vettermann S (1998) Extracellular superoxide dismutase from Streptococcus pyogenes type 12 strain is manganese-dependent. FFMS Microbiol Lett 160 217-224. 

Fig 24.24. Protection against ozone in the lung lining fluid GSH. glutathione AA, ascorbic acid (vitamin C) UA, uric acid CHO, carbohydrate a-TOC, vitamin E GSH-Px, glutathione peroxidase- ED-SOD, extracellular superoxide dismutase Neut, neutrophil. 

Chu Y, Piper R, Richardson S, Watanabe Y, Patel P, Heistad DD. Endocytosis of extracellular superoxide dismutase into endothelial cells role of the heparin-binding domain. Arterioscler Thromb Vase Biol 2006 26 1985-1990. 

C. Davis, D.B. Milne and F.H. Nielsen, Changes in Dietary Zinc and Copper Affect Zinc Status Indicators of Postmenopausal Women, Notably Extracellular Superoxide Dismutase and Amyloid Precursor Proteins, American Journal Clinical Nutrition. 2000, in press. 

Turunen, P., Puhakka, H.L., Heikura, T, Romppanen, E., Inkala, M Leppanen, 0., and Yla-Herttuala, S. (2006) Extracellular superoxide dismutase with vaccinia virus anti-inflammatory protein 35K or tissue inhibitor of metaDoproteinase-l Combination gene therapy in the treatment of vein graft stenosis in rabbits. Human Gene Therapy, 17, 405—414. 

In a rat type II pneumocyte analogue, the L2 cell line, exposed for 6 h to a combination of interferon-y (2,000 U/ml) and tumour necrosis factor-a (500 U/ml), extracellular superoxide dismutase and inducible nitric oxide synthase transcription was upregulated (Brady et al. 1997). Transcription of both genes was linked by activation of the transcription factor nuclear factor-xB. 

Extracellular superoxide dismutase mRNA expression was demonstrated in the alveolar macrophages of four patients undergoing surgical resections for carcinoma and carcinoid tumour, respectively (Su et al. 1997). 

The activity of extracellular superoxide dismut-ase (EC 1.15.1.1) in mouse lungs is 3- to 10-fold higher than that found in most mammals, and is 30-fold higher than that found in rat lungs (Mar-KLUND 1984). Extracellular superoxide dismutase labelling is strongest in the matrix of vessels, airways, and alveolar septa, especially in the septal tips (Fattman et al. 2000). 

Rabbani ZN, Anscher MS, Folz RJ et al. (2005) Overexpression of extracellular superoxide dismutase reduces acute radiation induced lung toxicity. BMC Cancer 5 59 Rabbani ZN, Batinic-Haberle I, Anscher MS etal. (2007a) Long-term administration of a small molecular weight catalytic metalloporphyrin antioxidant, AEOL 10150, protects lungs from radiation-induced injury. Int J Radiat Oncol Biol Phys 67 573-580... 

Fukai T, Folz RJ, Landmesser U, Harrison E)G. Extracellular superoxide dismutase and cardiovascular disease. Cardiovasc Res 2002 55 239-249. 

Adachi, T. Inoue, M. Hara, H. Maehata, E. Suzuki, S. (2004). Relationship of plasma extracellular-superoxide dismutase level with insulin resistance in type 2 diabetic patients. / Endocrinol, Vol. 181, No. 3, pp. 413 17, ISSN 0022-0795. 

Marklund, SL. (1984). Extracellular superoxide dismutase in human tissues and human cell lines. JClin Invest, Vol. 74, No. 4, pp. 1398-1403, ISSN 0021-9738. 

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