Superoxide dismutase 2 mice

Nonaka, A., Manabe, T., Tamura, K., Asano, N., Imanishi, K. and Tobe, T. (1989b). Changes of xanthine oxidase, lipid peroxide and superoxide dismutase in mouse acute pancreatitis. Digestion 43, 41-46. 

Figure 11.1 Force production by isoiated mouse extensor digitorum iongus (a) or soleus (b) muscies with ( ) or without ( ) treatment with superoxide dismutase (1000 U/ml). iMuscies were stimuiated at 40 Hz for 250 ms every second for 5 min. Vaiues significantiy different to controi muscies, P < 0.01. Data derived from McArdie...

Hirata, H., Ladenheim, B., Carlson, E., Epstein, C., Cadet, J.L. Autoradiographic evidence for methamphetamine-induced striatal dopaminergic loss in mouse brain attenuation in CuZn-superoxide dismutase transgenic mice. Brain Res. 714 95, 1996. 

Turner, B. J., Lopes, E. C. and Cheema, S. S. Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis. Neurosci. Lett. 350 132-136, 2003. 

Johnston, J. A., et al.. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA, 2000, 97(23), 12571-6. 

Transgenic mouse models, which have enhanced superoxide dismutase (SOD) activity... 

MPTP decreases glutathione levels and increases the levels of reactive oxygen species and the degree of lipid peroxidation in mouse brain slices in vitro and increases the levels of reactive oxygen species in mouse brain in vivo. MPTP neurotoxicity in vitro is reduced by glutathione. In vitro studies have shown that MPP neurotoxicity can be reduced by vitamin E, vitamin C, coenzyme Q, and mannitol (but not by superoxide dismutase, catalase, allopurinol, or dimethyl sulfoxide). P-Carotene, vitamin C, and /V-acctylcystcine partially protect against the neurotoxic effects of MPTP in mice, as do nicotinamide, coenzyme Q, and the free-radical spin trap A-tert-butyl-a-(sulfophenyl) nitrone. 

Zhu, J.-H., and Lei, X. G. Double null of selenium-glutathione peroxidase-1 and copper,zinc-superoxide dismutase enhances resistance of mouse primary hepatocytes to acetaminophen toxicity. Exp. Biol. Med. 231 545-552, 2006. 

Cyanide-induced cell death involves the selective activation of apoptosis or necrosis in different nemonal populations. Mills et al (1999) reported that cyanide-induced cell death occurred via apoptosis in the cortical region of a mouse brain and via necrosis in the substantia nigra. Similarly, Prabhakaran et al (2002) reported that cyanide-induced cell death occurred via apoptosis in primary cortical cells and via necrosis in primary mesencephalic cells. While exposure to potassium cyanide (400 pM) increased the formation of ROS in both cell types, the rates of formation and the nature of ROS varied. For example, catalase and superoxide dismutase decreased the formation of ROS in cortical cells but not in mesencephalic cells. These findings suggest that the selective vulnerabihty of these neuronal populations to cyanide may be related to differences in their susceptibility to oxidative stress. 

This is a widely studied cell line derived from a human cervix adenocarcinoma (Gey et al, 1952). The cells are epithelial-like in morphology and are susceptible to polio virus type 1 and adenovirus type 3. HeLa cells are used for the expression of recombinant proteins, including mouse metallothionein 1 gene, human Cu/Zn superoxide dismutase and hepatitis B surface antigen. They have been widely used as an in vitro model system because of the ease with which they can be cultivated but one drawback of this is that the cell line has been responsible for widespread contamination of other cell lines (Nelson-Rees et al, 1981). 

Chinese hamster ovary (CHO) and lung V79 cells, human lymphoblast TK6 cells, mouse lymphoma L5178Y cells GSTs, no CYPs Low Catalase, superoxide dismutase, peroxidase present... 

N3. Nakamura, Y., Gindhart, T. D., Winterstein, D., Tomita, I., Seed, J. L., and Colburn, N. H., Early superoxide dismutase-sensitive event promotes neoplastic transformation in mouse epidermal JB6 cells. Carcinogenesis (London) 9, 203-207 (1988). 

Sheng H, Brady TC, Pearlstein RD, Crapo JD, Warner DS. Extracellular superoxide dismutase deficiency worsens outcome from focal ecrebral ischemia in the mouse. Neurosci Lett 1999 267 13-16. 

Grankvist, K., Marklund, L. and Tiiljedal, l.-B. (1981) CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse. Biochem. J. 199 393-398. 

A similar study has identified 185 different gene products Irom around 600 protein spots in the mitochondrial proteome of the neuroblastoma cell line IMR-32 (Fountoulakis and Schlaeger, 2003). This approach has not been systematically applied to the study of the mitochondrial proteome of the heart, although the 2-DE/PMF approach has been applied in differential expression studies of hearts from knockout mouse strains deficient in creatine kinase (Kemec et ah, 2001) and mitochondrial superoxide dismutase (Lopez and Melov, 2002). 

Studies on some cell lines have shown that in tumor models such as mouse epidermal 1B6 cells and MCF-7, ROS were observed to stimulate cell growth in monolayers. In other cell lines, ROS can also be involved in the pathogenesis of cancer. By promoting cell proliferation in the transformed cancer cell lines MCF-7, HeLa, and Jurkat cells, reduced antioxidant levels were implicated in malignant transformation. Overexpression of manganese superoxide dismutase (MnSOD), a normal cellular antioxidant, enzyme was reported to revert transformation or tumor-promotion response in these and other transformed cell tines, such as human melanoma (UACC-903) cells, human breast cancer (MCF-7) cells, and mouse epidermal JB6 cells. ... 

Amstad, P.A. et at. Manganese superoxide dismutase expression inhibits soft agar growth in JB6 clone41 mouse epidermal cells. Carcinogenesis, 18 (3), 479, 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). 

Neuronal loss was initiated by inhibition of the antioxidant enzyme, superoxide dismntase (EC 1.15.1.1.) type 1, using the copper chelator diethyl-dithiocarbamate (Moskowitz et al. 2001). Continuous diethyldithiocarbamate treatment of Sprague-Dawley rat or C57/B16 mouse hippocampal slice cultures induced delayed neuronal loss beginning at 9 days of treatment that lasted for over 4 weeks. Neuronal loss was significantly attenuated in slice cultures that overexpress superoxide dismutase type 1, suggesting that superoxide dismutase inhibition was responsible. Inhibitors of nitric oxide synthase also attenuated diethyldithiocarbamate-induced neuronal loss. 

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