ArticleBMB reports2015
Enhancement of potency and stability of human extracellular superoxide dismutase.
Article in BMB reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Inhibitory effects of superoxide dismutase 3 on IgE production in B cells.Biochemistry and biophysics reports · 2022Article
- Superoxide dismutase 3 prevents early stage diabetic retinopathy in streptozotocin-induced diabetic rat model.PloS one · 2022Article
- Superoxide Dismutase 3 Controls the Activation and Differentiation of CD4Frontiers in immunology · 2021Article
- Inhibitory effects of superoxide dismutase 3 on Propionibacterium acnes-induced skin inflammation.Scientific reports · 2018Article
- N-Adamantyl-4-Methylthiazol-2-Amine Attenuates Glutamate-Induced Oxidative Stress and Inflammation in the Brain.Neurotoxicity research · 2017Article
- Zinc(II) ion promotes anti-inflammatory effects of rhSOD3 by increasing cellular association.BMB reports · 2017Article
- Recent developments in the role of reactive oxygen species in allergic asthma.Journal of thoracic disease · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells express several antioxidant enzymes to scavenge reactive oxygen species (ROS) responsible for oxidative damages and various human diseases. Therefore, antioxidant enzymes are considered biomedicine candidates. Among them, extracellular superoxide dismutase (SOD3) had showed prominent efficacy against asthma and inflammation. Despite its advantages as a biomedicine, the difficulty in obtaining large quantity of active recombinant human SOD3 (rhSOD3) has limited its clinical applications. We found that a significant fraction of overexpressed rhSOD3 was composed of the inactive apo-enzyme and its potency against inflammation depended on the rate of metal incorporation. Also, purified rhSOD3 was unstable and lost its activity very quickly. Here, we suggest an ideal preparative method to express, purify, and store highly active rhSOD3. The enzymatic activity of rhSOD3 was maximized by incorporating metal ions into rhSOD3 after purification. Also, albumin or polyethylene glycol prevented rapid inactivation or degradation of rhSOD3 during preparative procedures and long-term storage.
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Registered trials
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