Role of CuZn superoxide dismutase in regulating lymphocyte apoptosis during sepsis

2000 ◽  
Vol 28 (6) ◽  
pp. 1701-1708 ◽  
Author(s):  
Bradley D. Freeman ◽  
Andrew G. Reaume ◽  
Paul E. Swanson ◽  
Charles J. Epstein ◽  
Elaine J. Carlson ◽  
...  
2007 ◽  
Vol 2 (3) ◽  
pp. 337-350 ◽  
Author(s):  
Paolo Mondola ◽  
Rosalba Seru ◽  
Simona Damiano ◽  
Mariarosaria Santillo

AbstractThe CuZn superoxide dismutase (SOD1), a member of a group of isoenzymes involved in the scavenger of superoxide anions, is a dimeric carbohydrate free protein, mainly localized in the cytosol. The reactive oxygen species (ROS) are involved in many pathophysiological events correlated with mutagenesis, cancer, degenerative processes and aging. In the first part of this mini-review the well known role of SOD1 and ROS are briefly summarized. Following, a potential novel biological action that SOD1 could exert is described, based on the recent researches demonstrating the secretion of this enzyme in many cellular lines. Moreover, the role of impaired mutant SOD1 secretion, associated with cytoplasmic toxic inclusion, which occurs in familial amyotrophic lateral sclerosis (ALS), is summarized. In addition, a depolarization-dependent release of SOD1 in pituitary GH3 cells and in rat synaptosomes through a calcium and SNARE-dependent mechanism is reported.


1984 ◽  
Vol 222 (3) ◽  
pp. 649-655 ◽  
Author(s):  
S L Marklund

The contents of extracellular superoxide dismutase, CuZn superoxide dismutase and Mn superoxide dismutase were determined in tissues from nine mammalian species. The pattern of CuZn superoxide dismutase distribution was similar in all species, with high activity in metabolically active organs such as liver and kidney and low activity in, for example, skeletal muscle. Mn superoxide dismutase activity was high in organs with high respiration, such as liver, kidney, and myocardium. Overall the Mn superoxide dismutase activity in organs was almost as high as the CuZn superoxide dismutase activity. The content of extracellular superoxide dismutase was, almost without exception, lower than the content of the other isoenzymes. The pattern of tissue distribution was distinctly different from those of CuZn superoxide dismutase and Mn superoxide dismutase. The tissue distribution of extracellular superoxide dismutase differed among species, but in general there was much in lungs and kidneys and little in skeletal muscle. In man, pig, sheep, cow, rabbit and mouse the overall tissue extracellular superoxide dismutase activities were similar to each other, whereas dog, cat and rat tissues contained distinctly less. There was no general correlation between the tissue extracellular superoxide dismutase activity of any of the various species and the variable plasma activity. The ratio between the plasma and the overall tissue activities was high, for some species over unity, providing further evidence for the notion that one role of extracellular superoxide dismutase is as a plasma protein.


2008 ◽  
Vol 81 (4) ◽  
pp. 678-685 ◽  
Author(s):  
Y. Ding ◽  
Y.-L. Li ◽  
M. C. Zimmerman ◽  
R. L. Davisson ◽  
H. D. Schultz

1989 ◽  
Vol 264 (9) ◽  
pp. 5260-5268 ◽  
Author(s):  
R A Hallewell ◽  
I Laria ◽  
A Tabrizi ◽  
G Carlin ◽  
E D Getzoff ◽  
...  

1991 ◽  
Vol 24 (1) ◽  
pp. 85-91 ◽  
Author(s):  
KATSUHIKO NARIMOTO ◽  
YOICHI NODA ◽  
MASAHIDE SHIOTANI ◽  
SATOSHI NATSUYAMA ◽  
TAKAHIDE MORI ◽  
...  

Synapse ◽  
1995 ◽  
Vol 21 (2) ◽  
pp. 169-176 ◽  
Author(s):  
Jean Lud Cadet ◽  
Bruce Ladenheim ◽  
Hiroshi Hirata ◽  
Richard B. Rothman ◽  
Syed Ali ◽  
...  

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