scholarly journals Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species

1984 ◽  
Vol 222 (3) ◽  
pp. 649-655 ◽  
Author(s):  
S L Marklund
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Tissue Distribution ◽  
Mammalian Species ◽  
Superoxide Dismutase Activity ◽  
Rat Tissues ◽  
Extracellular Superoxide Dismutase ◽  
Liver And Kidney ◽  
Cuzn Superoxide Dismutase

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.

Abstract B52: The role of extracellular superoxide dismutase activity in pancreatic cancer biology and therapy

2015 ◽  
Author(s):  
James J. Mezhir ◽  
Brianne R. O'Leary ◽  
Andrew M. Bellizzi ◽  
Sean Altekruse ◽  
Charles F. Lynch ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Superoxide Dismutase ◽  
Cancer Biology ◽  
Superoxide Dismutase Activity ◽  
Extracellular Superoxide Dismutase

Tissue distribution of immunoreactive mouse extracellular superoxide dismutase

1998 ◽  
Vol 275 (3) ◽  
pp. C840-C847 ◽  
Author(s):  
Tomomi Ookawara ◽  
Nobuo Imazeki ◽  
Osamu Matsubara ◽  
Takako Kizaki ◽  
Shuji Oh-Ishi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Adrenal Gland ◽  
Sandwich Elisa ◽  
Brown Fat ◽  
Extracellular Superoxide Dismutase ◽  
Physiological Importance ◽  
Vascular Walls ◽  
Mouse Tissues ◽  
White Fat

Protein content and mRNA expression of extracellular superoxide dismutase (EC-SOD) were investigated in 16 mouse tissues. We developed a double-antibody sandwich ELISA using the affinity-purified IgG against native mouse EC-SOD. EC-SOD could be detected in all of the tissues examined (lung, kidney, testis, brown fat, liver, adrenal gland, pancreas, colon, white fat, thymus, stomach, spleen, heart, skeletal muscle, ileum, and brain, in decreasing order of content measured as μg/g wet tissue). Lung showed a markedly higher value of EC-SOD than other tissues. Interestingly, white fat had a high content of EC-SOD in terms of micrograms per milligram protein, which corresponded to that of lung. Kidney showed the strongest expression of EC-SOD mRNA. Relatively strong expression of the mRNA was observed in lung, white fat, adrenal gland, brown fat, and testis. Heart and brain showed only weak signals, and no such expression could be detected in either digestive organs or skeletal muscle. Immunohistochemically, EC-SOD was localized mainly to connective tissues and vascular walls in the tissues examined. Deep staining in the cytosol was observed in the cortical tubular cells of kidney. These results suggest that EC-SOD is distributed systemically in mice and that the physiological importance of this enzyme may be a compensatory adaptation to oxidative stress, particularly in lung and kidney.

Reduction in extracellular superoxide dismutase activity in African-American patients with hypertension

2006 ◽  
Vol 41 (9) ◽  
pp. 1384-1391 ◽  
Author(s):  
LiChun Zhou ◽  
Wei Xiang ◽  
James Potts ◽  
Michael Floyd ◽  
Chakradhari Sharan ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
African American ◽  
Superoxide Dismutase Activity ◽  
Extracellular Superoxide Dismutase

A new perspective on the role of CuZn superoxide dismutase (SOD1)

2007 ◽  
Vol 2 (3) ◽  
pp. 337-350 ◽  
Author(s):  
Paolo Mondola ◽  
Rosalba Seru ◽  
Simona Damiano ◽  
Mariarosaria Santillo
Keyword(s):  
Superoxide Dismutase ◽  
Biological Action ◽  
Gh3 Cells ◽  
Oxygen Species ◽  
Cuzn Superoxide Dismutase ◽  
New Perspective ◽  
Rat Synaptosomes ◽  
Lateral Sclerosis ◽  
Dependent Mechanism

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.

Absence of Modulating Effects of Cytokines on Antioxidant Enzymes in Peritoneal Mesothelial Cells

1997 ◽  
Vol 17 (5) ◽  
pp. 455-466 ◽  
Author(s):  
Jinn-Yang Chen ◽  
An-Hang Yang ◽  
Yao-Ping Lin ◽  
Jen-Kou Lin ◽  
Wu-Chang Yang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Human Liver ◽  
Mesothelial Cells ◽  
Superoxide Dismutase Activity ◽  
Antioxidant Enzyme Activities ◽  
Peritoneal Mesothelial Cells ◽  
Liver And Kidney ◽  
Human Peritoneal Mesothelial Cells

Objective To investigate the modulation of superoxide dismutase, glutathione peroxidase, and catalase by cytokines and endotoxin in human peritoneal mesothelial cells. Design Cultured human peritoneal mesothelial cells were treated with various concentrations of interleu kin-1 α, tumor necrosis factor-α(TNFα), interleukin-6, interleukin-8, transforming growth factor-β (TGFβ), and lipopolysaccharide. Cell morphology was observed and the activities of superoxide dismutase, catalase, and glutathione peroxidase were assayed. The antioxidant enzyme activities of human peritoneal mesothelial cells were also compared with those of human liver and kidney tissues. Results Interleukin-1α, TNFα, TGFβ, and lipopolysaccharide caused dose-dependent cytotoxicities in mesothelial cells. The activities of these three antioxidant enzymes did not change after treatment with cytokines and endotoxin. The total superoxide dismutase activity of confluent human peritoneal mesothelial cells was found to be greater than that of human liver and kidney tissues and was composed mostly of manganese superoxide dismutase activity. Furthermore, glutathione peroxidase and catalase activities of human peritoneal mesothelial cells were lower than those of human liver and kidney tissues. Conclusion In human peritoneal mesothelial cells, lack of induction of antioxidant enzymes by inflammatory cytokines, as well as high superoxide dismutase activity accompanied by insufficient glutathione peroxidase and catalase activities may both contribute to the susceptibility of these cells to oxidative damage. Therefore, appropriate management to decrease oxidative injury to the peritoneum should be taken into consideration when treating long-term continuous ambulatory peritoneal dialysis patients.

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