scholarly journals The Role of Manganese Superoxide Dismutase in Inflammation Defense

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Chang Li ◽  
Hai-Meng Zhou

Antioxidant enzymes maintain cellular redox homeostasis. Manganese superoxide dismutase (MnSOD), an enzyme located in mitochondria, is the key enzyme that protects the energy-generating mitochondria from oxidative damage. Levels of MnSOD are reduced in many diseases, including cancer, neurodegenerative diseases, and psoriasis. Overexpression of MnSOD in tumor cells can significantly attenuate the malignant phenotype. Past studies have reported that this enzyme has the potential to be used as an anti-inflammatory agent because of its superoxide anion scavenging ability. Superoxide anions have a proinflammatory role in many diseases. Treatment of a rat model of lung pleurisy with the MnSOD mimetic MnTBAP suppressed the inflammatory response in a dose-dependent manner. In this paper, the mechanisms underlying the suppressive effects of MnSOD in inflammatory diseases are studied, and the potential applications of this enzyme and its mimetics as anti-inflammatory agents are discussed.

1994 ◽  
Vol 14 (2) ◽  
pp. 77-81 ◽  
Author(s):  
M. Shingu ◽  
S. Takahashi ◽  
M. Ito ◽  
N. Hamamatu ◽  
Y. Suenaga ◽  
...  

2008 ◽  
Vol 147 (1) ◽  
pp. 101-114 ◽  
Author(s):  
Megan J. Morgan ◽  
Martin Lehmann ◽  
Markus Schwarzländer ◽  
Charles J. Baxter ◽  
Agata Sienkiewicz-Porzucek ◽  
...  

1997 ◽  
Vol 272 (4) ◽  
pp. L714-L719
Author(s):  
D. J. Chung ◽  
L. B. Clerch

A redox-sensitive protein in rat lung binds to the 3'-untranslated region (3'-UTR) of manganese superoxide dismutase (Mn-SOD) mRNA; the activity of this Mn-SOD RNA-binding protein (Mn-SOD-BP) is greater in 12,000-g supernatant fractions (S12) from neonates than in S12 from adults (H. Fazzone, A. Wangner, and L. B. Clerch. J. Clin. Invest. 92: 1278-1281, 1993). To determine the mechanism underlying this developmental difference, lung subcellular fractions were tested for their effect on Mn-SOD-BP activity. Protein in the 130,000-g supernatant (S130) of lung extracts bound the 3'-UTR. However, the developmental difference in binding was not present in S130. The 130,000-g pellet (P130) did not bind the 3'-UTR; rather, it contained an inhibitor of Mn-SOD-BP activity. Addition of P130 to S130 decreased RNA binding in a dose-dependent manner. Furthermore, adult P130 was a more potent inhibitor of RNA-binding activity than neonatal P130. These data indicate that the developmental difference in Mn-SOD-BP activity is due, in part, to an inhibitor in P130. Biochemical characterization revealed that the inhibitor is an RNA that may participate in the posttranscriptional control of Mn-SOD gene expression.


Sign in / Sign up

Export Citation Format

Share Document