scholarly journals Subunit interaction in extracellular superoxide dismutase: Effects of mutations in the N-terminal domain

2008 ◽  
Vol 6 (11) ◽  
pp. 2350-2358 ◽  
Author(s):  
Peter Stenlund ◽  
Lena A. E. Tibell ◽  
Dick Andersson
Keyword(s):  
Superoxide Dismutase ◽  
Extracellular Superoxide Dismutase ◽  
Subunit Interaction ◽  
Terminal Domain

scholarly journals Extracellular Superoxide Dismutase Is a Major Antioxidant in Human Fibroblasts and Slows Telomere Shortening

2002 ◽  
Vol 278 (9) ◽  
pp. 6824-6830 ◽  
Author(s):  
Violeta Serra ◽  
Thomas von Zglinicki ◽  
Mario Lorenz ◽  
Gabriele Saretzki
Keyword(s):  
Superoxide Dismutase ◽  
Human Fibroblasts ◽  
Extracellular Superoxide Dismutase ◽  
Telomere Shortening

Nitric Oxide and Blood Pressure in Mice Lacking Extracellular-Superoxide Dismutase

2002 ◽  
Vol 36 (7) ◽  
pp. 755-758 ◽  
Author(s):  
Lena M. Jonsson ◽  
Daryl D. Rees ◽  
Thomas Edlund ◽  
Stefan L. Marklund
Keyword(s):  
Nitric Oxide ◽  
Blood Pressure ◽  
Superoxide Dismutase ◽  
Extracellular Superoxide Dismutase

scholarly journals RasOncogene-Mediated Progressive Silencing of Extracellular Superoxide Dismutase in Tumorigenesis

2015 ◽  
Vol 2015 ◽  
pp. 1-13 ◽  
Author(s):  
Francesca Cammarota ◽  
Gabriella de Vita ◽  
Marco Salvatore ◽  
Mikko O. Laukkanen
Keyword(s):  
Superoxide Dismutase ◽  
Cancer Cells ◽  
Self Regulation ◽  
Thyroid Cell ◽  
Extracellular Superoxide Dismutase ◽  
Mrna Synthesis ◽  
Ras Activation ◽  
Degree Of Differentiation ◽  
In Cells

Extracellular superoxide dismutase (SOD3) is a secreted enzyme that uses superoxide anion as a substrate in a dismutase reaction that results in the formation of hydrogen peroxide. Both of these reactive oxygen species affect growth signaling in cells. Although SOD3 has growth-supporting characteristics, the expression ofSOD3is downregulated in epithelial cancer cells. In the current work, we studied the mechanisms regulatingSOD3expressionin vitrousing thyroid cell models representing different stages of thyroid cancer. We demonstrate that a low level of RAS activation increasesSOD3mRNA synthesis that then gradually decreases with increasing levels of RAS activation and the decreasing degree of differentiation of the cancer cells. Our data indicate thatSOD3regulation can be divided into two classes. The first class involves RAS–driven reversible regulation ofSOD3expression that can be mediated by the following mechanisms: RAS GTPase regulatory genes that are responsible forSOD3self-regulation; RAS-stimulated p38 MAPK activation; and RAS-activated increased expression of themir21microRNA, which inversely correlates withsod3mRNA expression. The second class involves permanent silencing ofSOD3mediated by epigenetic DNA methylation in cells that represent more advanced cancers. Therefore, the work suggests thatSOD3belongs to the group ofrasoncogene-silenced genes.

An Inter-subunit Disulfide Bond Affects Affinity of Human Lung Extracellular Superoxide Dismutase to Heparin

2003 ◽  
Vol 37 (8) ◽  
pp. 823-827 ◽  
Author(s):  
Tomomi Ookawara ◽  
Hironobu Eguchi ◽  
Takako Kizaki ◽  
Chitose Nakao ◽  
Yuzo Sato ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Disulfide Bond ◽  
Human Lung ◽  
Extracellular Superoxide Dismutase
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