scholarly journals Pertussis toxin treatment alters manganese superoxide dismutase activity in lung. Evidence for lung oxygen toxicity in air-breathing rats.

1994 ◽  
Vol 93 (6) ◽  
pp. 2482-2489 ◽  
Author(s):  
L B Clerch ◽  
G Neithardt ◽  
U Spencer ◽  
J A Melendez ◽  
G D Massaro ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Pertussis Toxin ◽  
Manganese Superoxide Dismutase ◽  
Oxygen Toxicity ◽  
Superoxide Dismutase Activity ◽  
Air Breathing ◽  
Manganese Superoxide

Pertussis toxin alters the concentration and turnover of manganese superoxide dismutase in rat lung

1996 ◽  
Vol 271 (6) ◽  
pp. L875-L879
Author(s):  
A. Berkovich ◽  
D. Massaro ◽  
L. B. Clerch
Keyword(s):  
Superoxide Dismutase ◽  
Pertussis Toxin ◽  
Manganese Superoxide Dismutase ◽  
Specific Activity ◽  
Oxygen Toxicity ◽  
Translational Efficiency ◽  
Sod Activity ◽  
Manganese Superoxide ◽  
Guanine Nucleotide Binding ◽  
Nucleotide Binding Proteins

Treatment of rats with pertussis toxin (PTX) decreases the activity of manganese superoxide dismutase (Mn-SOD) in the lung and results in oxygen toxicity in air (L. B. Clerch, G. Neithardt, U. Spencer, J. A. Melendez, G. D. Massaro, and D. Massaro. J. Clin. Invest. 93: 2482-2489, 1994). To examine aspects of the mechanism of the PTX-induced fall in Mn-SOD activity, we injected rats with PTX (50 micrograms/kg), killed the rats 72 h later, and measured the activity, concentration, specific activity, and turnover of Mn-SOD in the lung. Treatment with PTX caused an approximately 50% fall in Mn-SOD activity and Mn-SOD concentration but no change in Mn-SOD specific activity. PTX also caused an increase in Mn-SOD mRNA concentration, a fall in Mn-SOD synthesis, and an increase in the half-life of Mn-SOD and general proteins. We conclude the PTX-induced low concentration of Mn-SOD is due to a decrease of translational efficiency. We suggest that, under normoxic conditions, signal transduction via heterotrimeric guanine nucleotide binding proteins regulates the expression of Mn-SOD at the level of translation and Mn-SOD degradation.

Reduced mitochondrial manganese-superoxide dismutase activity exacerbates glutamate toxicity in cultured mouse cortical neurons

1998 ◽  
Vol 814 (1-2) ◽  
pp. 164-170 ◽  
Author(s):  
Yibing Li ◽  
Jean-Christophe Copin ◽  
Liza F Reola ◽  
Bernard Calagui ◽  
Glenn T Gobbel ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Cortical Neurons ◽  
Manganese Superoxide Dismutase ◽  
Superoxide Dismutase Activity ◽  
Glutamate Toxicity ◽  
Manganese Superoxide

The effect of tumor necrosis factor-α on human malignant glial cells

1992 ◽  
Vol 76 (4) ◽  
pp. 652-659 ◽  
Author(s):  
Rolando F. Del Maestro ◽  
Monica Lopez-Torres ◽  
Warren B. McDonald ◽  
Eric C. Stroude ◽  
Indrasen S. Vaithilingam
Keyword(s):  
Superoxide Dismutase ◽  
Tumor Necrosis Factor ◽  
Cell Line ◽  
Tumor Necrosis ◽  
Manganese Superoxide Dismutase ◽  
Tumor Necrosis Factor Α ◽  
Superoxide Dismutase Activity ◽  
Manganese Superoxide ◽  
Factor Α ◽  
Necrosis Factor

✓ The influence of human recombinant tumor necrosis factor-α has been assessed on a cell line (U-251) derived from a human malignant glial tumor. The results of this study demonstrate that tumor necrosis factor-α at doses of 50 and 100 ng/ml: 1) did not have cytotoxic or cytostatic effects on the U-251 cell line; 2) significantly increased the intracellular activity of manganese superoxide dismutase but had no effect on copper and zinc superoxide dismutase, catalase, or glutathione peroxidase activity; and 3) did not significantly alter the intracellular or extracellular general protease and collagenase type IV activity of these cells. The resistance of the U-251 cell line to tumor necrosis factor-α cytotoxicity may be related in part to the high intrinsic manganese superoxide dismutase activity present in this cell line combined with the ability of this cell line to induce substantial amounts of protective manganese superoxide dismutase activity in response to tumor necrosis factor-α.

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