SOD Enzymes and Microbial Pathogens: Surviving the Oxidative Storm of Infection

Broxton, Chynna N.; Culotta, Valeria C.

doi:10.1371/journal.ppat.1005295

Cited by 120 publications

(86 citation statements)

References 30 publications

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“…It is an active substance generated by living organisms, which can eliminate harmful materials such as free radicals produced during normal oxygen metabolism (28). It can react with oxygen free radicals to generate hydrogen peroxide (29); the latter is converted into water by the organism and excreted.…”

Section: Discussionmentioning

confidence: 99%

Influence of different concentrations of uric acid on oxidative stress in steatosis hepatocytes

Cheng

Yang²,

Zhou

et al. 2018

Exp Ther Med

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Abstract. The development of nonalcoholic fatty liver disease (NAFLD) is caused by the steatosis of hepatocytes, which induces oxidative stress (OS). Thus, OS has an important role in the development of NAFLD. In the present study, the L-02 hepatocyte cell line was used to develop a steatosis cell model. The best model was determined using an MTT assay and the triglyceride levels. Model cells were treated with high concentrations of uric acid (UA; 0, 5, 10, 20 and 30 mg/dl) for 24, 48, 72 and 96 h. Indicators of oxidation were then measured, which included total superoxide dismutase (SOD), malonaldehyde (MDA) and reduced glutathione (GSH), and the transcriptional and translational levels of SOD1 and γ-glutamate-cysteine ligase (γ-GCLC) were also determined. In addition, the intracellular levels of aspartate aminotransferase and alanine aminotransferase (ALT) were detected. The activity of SOD1 decreased over time and the result was supported by the results of western blotting. The transcriptional levels of SOD1 in model cells was significantly higher than untreated cells at 48 h. With the decreased levels of SOD1 and GSH, MDA increased in a time-dependent manner. The content of GSH decreased with time as well, which was also reflected in the results of western blotting. The transcriptional levels of γ-GCLC in all UA-treated groups were lower when compared with those observed in the model group. The activity of ALT tended to increase, depending on the duration of treatment. Treatment with 5 and 10 mg/dl UA had an antioxidative effect on the model cells, and 30 mg/dl UA treatment for 48 h increased OS in the cells.

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Section: Discussionmentioning

confidence: 99%

Influence of different concentrations of uric acid on oxidative stress in steatosis hepatocytes

Cheng

Yang²,

Zhou

et al. 2018

Exp Ther Med

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“…SODs protect cells from oxidative stress, particularly in the removal of superoxide produced during metabolism (4,5), and also have key roles in cell signaling through the local production of H 2 O 2 (6)(7)(8). In addition, many SODs are virulence factors for pathogens, allowing them to survive the oxidative burst of macrophages and neutrophils at the host-pathogen interface (9,10).…”

Section: Cu (Ii) + Omentioning

confidence: 99%

“…Even so, within the eubacterial kingdom, Cu-only SOD enzymes appear unique to the Mycobacterium genus, as all other periplasmic SODs characterized to date have both Cu and Zn (9,34,45,57).…”

Section: A Bacterial Cu-sod Functions Without Znmentioning

confidence: 99%

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Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains

Robinett

Peterson

Culotta

2018

Journal of Biological Chemistry

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The Cu-containing superoxide dismutases (SODs) represent a large family of enzymes that participate in the metabolism of reactive oxygen species by disproportionating superoxide anion radical to oxygen and hydrogen peroxide. Catalysis is driven by the redox-active Cu ion, and in most cases, SODs also harbor a Zn at the active site that enhances Cu catalysis and stabilizes the protein. Such bimetallic Cu/Zn SODs are widespread, from the periplasm of bacteria to virtually every organelle in the human cell. However, a new class of Cu-containing SODs has recently emerged that function without Zn. These Cu-only enzymes serve as extracellular SODs in specific bacteria (i.e., Mycobacteria), throughout the fungal kingdom, and in the fungus-like oomycetes. The eukaryotic Cu-only SODs are particularly unique in that they lack an electrostatic loop for substrate guidance and have an unusual open-access Cu site, yet can still react with superoxide at rates limited only by diffusion. Cu-only SOD sequences similar to those seen in fungi and oomycetes are also found in the animal kingdom, but rather than single-domain enzymes, they appear as tandem repeats in large polypeptides we refer to as CSRPs (Cu-only SODrepeat proteins). Here, we compare and contrast the Cu/Zn versus Cu-only SODs and discuss the evolution of Cu-only SOD protein domains in animals and fungi.

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“…Identification of more potent bacteria and fungi can broaden the spectrum of PGPB and mycorrhiza that can survive and perform well in soil conditions. Pearl millet [Pennisetum glaucum (L.)] is the main coarse grain crop in semi-arid regions and is grown in India as rain-fed or irrigated crop on 10 million hectares producing 7.01 million tons (Bhatnagar et al, 2002). Pearl millet is a crop of marginal land, provides staple food for poor in semiarid regions of Asia and Africa.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Plant Growth Promoting Rhizobacteria and Mycorrhizal Fungi for Growth and Nutrient Uptake in Pearl Millet (Pennisetum glaucum)

Singh¹,

Joshi²,

Kumar³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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SOD Enzymes and Microbial Pathogens: Surviving the Oxidative Storm of Infection

Cited by 120 publications

References 30 publications

Influence of different concentrations of uric acid on oxidative stress in steatosis hepatocytes

Influence of different concentrations of uric acid on oxidative stress in steatosis hepatocytes

Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains

Evaluation of Plant Growth Promoting Rhizobacteria and Mycorrhizal Fungi for Growth and Nutrient Uptake in Pearl Millet (Pennisetum glaucum)

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