scholarly journals Superoxide radicals have a protective role during H2O2 stress

2013 ◽  
Vol 24 (18) ◽  
pp. 2876-2884 ◽  
Author(s):  
Geoffrey W. Thorpe ◽  
Mayfebelle Reodica ◽  
Michael J. Davies ◽  
Gino Heeren ◽  
Stefanie Jarolim ◽  
...  
Keyword(s):  
Superoxide Radical ◽  
Defense Mechanism ◽  
Chain Complex ◽  
Protective Role ◽  
Superoxide Radicals ◽  
Complex Iii ◽  
Yeast Cells ◽  
Oxygen Species ◽  
Radical Production ◽  
Hormetic Effect

Reactive oxygen species (ROS) consist of potentially toxic, partly reduced oxygen species and free radicals. After H2O2 treatment, yeast cells significantly increase superoxide radical production. Respiratory chain complex III and possibly cytochrome b function are essential for this increase. Disruption of complex III renders cells sensitive to H2O2 but not to the superoxide radical generator menadione. Of interest, the same H2O2-sensitive mutant strains have the lowest superoxide radical levels, and strains with the highest resistance to H2O2 have the highest levels of superoxide radicals. Consistent with this correlation, overexpression of superoxide dismutase increases sensitivity to H2O2, and this phenotype is partially rescued by addition of small concentrations of menadione. Small increases in levels of mitochondrially produced superoxide radicals have a protective effect during H2O2-induced stress, and in response to H2O2, the wild-type strain increases superoxide radical production to activate this defense mechanism. This provides a direct link between complex III as the main source of ROS and its role in defense against ROS. High levels of the superoxide radical are still toxic. These opposing, concentration-dependent roles of the superoxide radical comprise a form of hormesis and show one ROS having a hormetic effect on the toxicity of another.

scholarly journals Studies on Production and Chemical Property of Singlet Oxygen and Superoxide Radical by Dyestuffs

2009 ◽  
Vol 6 (s1) ◽  
pp. S79-S86 ◽  
Author(s):  
Vikesh Kumar ◽  
M. R. Tripathi ◽  
Manish Kumar ◽  
Gopal Shukla ◽  
Sarvesh Dwivedi ◽  
...  
Keyword(s):  
Singlet Oxygen ◽  
Chemical Property ◽  
Superoxide Radical ◽  
Skin Diseases ◽  
Food Additives ◽  
Reactive Oxygen ◽  
Superoxide Radicals ◽  
Photochemical Oxidation ◽  
Oxygen Species ◽  
Metanil Yellow

There are several low lying singlet oxygen (1O2) and superoxide radical (O-2) which are important in photochemical oxidation. In our present analysis we are studying chemical property of singlet oxygen (1O2) and super oxide radical (O-2) and some dyestuffs species to produce reactive oxygen such as singlet oxygen1O2and superoxide radicals. Irradiation with sun lightin vitrothe dyestuff like benzanthrone, metanil yellow andp-aminodiphenylamine were found to produce reactive oxygen species such as singlet oxygen (1O2) and/or superoxide radicals (O-2) .The dose response relationship between singlet1O2production when sunlight expose of those dyestuffs (0-25 min), and (0-12 min) for super oxide (O-2) production were studied. However benzanthrone produces detectable amount of1O2, Although metanil yellow andp-aminodiphenylamine (p-ADPA) did not produce detectable amounts of1O2under similar conditions. The above dye stuffs are routinely used in textiles, cosmetics, detergents, leather industries as well as food additives and role of these activated oxygen species in the development of skin diseases.

Chemical and biochemical aspects of superoxide radicals and related species of activated oxygen

1982 ◽  
Vol 60 (11) ◽  
pp. 1330-1345 ◽  
Author(s):  
Ajit Singh
Keyword(s):  
Hydrogen Peroxide ◽  
Hydroxyl Radicals ◽  
Superoxide Radical ◽  
Superoxide Radicals ◽  
Living Systems ◽  
Biological Processes ◽  
Oxygen Species ◽  
Peroxy Radicals ◽  
Activated Oxygen ◽  
Oxygen Yield

The spectrum of biological processes in which oxygen is used by living systems is quite large, and the products include some damaging species of activated oxygen, particularly the superoxide radical [Formula: see text] and hydrogen peroxide (H2O2). Superoxide radicals and hydrogen peroxide, in turn, can lead to the formation of other damaging species: hydroxyl radicals (∙OH) and singlet oxygen (1O2). Hydroxyl radicals react with organic compounds to give secondary free radicals that, in the presence of oxygen, yield peroxy radicals, peroxides, and hydroperoxides. Formation, interconversion, and reactivity of [Formula: see text] and related activated oxygen species, methods available for their detection, and the basis of their biological toxicity are briefly reviewed.

scholarly journals Effect of Riboflavin on the Precocious Maturation of Spine Grape Berries (Vitis davidii Foex)

HortScience ◽  
2019 ◽  
Vol 54 (9) ◽  
pp. 1521-1525
Author(s):  
Mingtao Zhu ◽  
Jun Yu ◽  
Sheng Wu ◽  
Meijun Wang ◽  
Guoshun Yang
Keyword(s):  
Superoxide Radical ◽  
Soluble Solids ◽  
Wild Plant ◽  
Maturation Stage ◽  
Oxygen Species ◽  
Grape Berries ◽  
Radical Production ◽  
Wild Plant Species ◽  
Environmentally Safe ◽  
Vitis Davidii

Spine grape (Vitis davidii Foex) is an important wild plant species in South China. To provide economical and environmentally safe ways to promote the precocious maturation of spine grape berries, the effects of riboflavin were investigated. Riboflavin affected the reactive oxygen species metabolism in spine grape berries by increasing superoxide radical production and the hydrogen peroxide content, and it impaired the activities of the antioxidant enzymes superoxide dismutase and catalase. Riboflavin also induced the upregulated expression of maturation-related genes in advance, and the earlier accumulation of anthocyanin and total soluble solids. Phenological observations revealed that the treated grape berries underwent a color-turning stage 9 days earlier than the control, and the maturation stage occurred 7 days earlier than the control. Thus, riboflavin may significantly promote the precocious maturation of spine grape berries.

The yeast CBP1 gene produces two differentially regulated transcripts by alternative 3'-end formation

1989 ◽  
Vol 9 (10) ◽  
pp. 4161-4169
Author(s):  
S A Mayer ◽  
C L Dieckmann
Keyword(s):  
Carbon Source ◽  
Cytochrome B ◽  
Mitochondrial Protein ◽  
Nuclear Gene ◽  
Chain Complex ◽  
Complex Iii ◽  
Yeast Cells ◽  
Transcriptional Level ◽  
Amino Acid Residues ◽  
Gene Encoding

CBP1 is a yeast nuclear gene encoding a mitochondrial protein that stabilizes the 5' end of cytochrome b (cob) pre-mRNA. Cytochrome b is the only mitochondrially synthesized component of the respiratory chain complex III. Since the nuclearly encoded subunits of this complex are regulated at the transcriptional level by catabolite repression, we hypothesized that CBP1 might be similarly regulated. To test the idea that transcriptional regulation of CBP1 could coordinate an increase in cytochrome b mRNA stability with an increase in nuclearly encoded complex III subunit production, we characterized the change in abundance of CBP1 mRNA during derepression on a nonfermentable carbon source. Poly(A)+ RNA from derepressed yeast cells was examined by Northern (RNA) analyses with cRNA probes from CBP1. Both 2.2- and 1.3-kilobase (kb) transcripts were detected. The 1.3-kb mRNA lacked approximately 900 nucleotides of the 3' end of the 2.2-kb mRNA, which encodes the carboxyl-terminal 250 amino acid residues of the CBP1 coding sequence. Northern analyses of RNA isolated from deletion-insertion mutants of CBP1 and from strains that overexpress CBP1 mRNA demonstrated that both mRNAs were transcribed from the CBP1 gene. Furthermore, we demonstrated that the levels of the two CBP1 mRNAs were reciprocally regulated by the carbon source in the growth medium. This is the first description of a yeast gene from which two transcripts that can encode proteins with distinctly different coding properties are generated by alternative 3'-end formation.

scholarly journals The yeast CBP1 gene produces two differentially regulated transcripts by alternative 3'-end formation.

1989 ◽  
Vol 9 (10) ◽  
pp. 4161-4169 ◽  
Author(s):  
S A Mayer ◽  
C L Dieckmann
Keyword(s):  
Carbon Source ◽  
Cytochrome B ◽  
Mitochondrial Protein ◽  
Nuclear Gene ◽  
Chain Complex ◽  
Complex Iii ◽  
Yeast Cells ◽  
Transcriptional Level ◽  
Amino Acid Residues ◽  
Gene Encoding

CBP1 is a yeast nuclear gene encoding a mitochondrial protein that stabilizes the 5' end of cytochrome b (cob) pre-mRNA. Cytochrome b is the only mitochondrially synthesized component of the respiratory chain complex III. Since the nuclearly encoded subunits of this complex are regulated at the transcriptional level by catabolite repression, we hypothesized that CBP1 might be similarly regulated. To test the idea that transcriptional regulation of CBP1 could coordinate an increase in cytochrome b mRNA stability with an increase in nuclearly encoded complex III subunit production, we characterized the change in abundance of CBP1 mRNA during derepression on a nonfermentable carbon source. Poly(A)+ RNA from derepressed yeast cells was examined by Northern (RNA) analyses with cRNA probes from CBP1. Both 2.2- and 1.3-kilobase (kb) transcripts were detected. The 1.3-kb mRNA lacked approximately 900 nucleotides of the 3' end of the 2.2-kb mRNA, which encodes the carboxyl-terminal 250 amino acid residues of the CBP1 coding sequence. Northern analyses of RNA isolated from deletion-insertion mutants of CBP1 and from strains that overexpress CBP1 mRNA demonstrated that both mRNAs were transcribed from the CBP1 gene. Furthermore, we demonstrated that the levels of the two CBP1 mRNAs were reciprocally regulated by the carbon source in the growth medium. This is the first description of a yeast gene from which two transcripts that can encode proteins with distinctly different coding properties are generated by alternative 3'-end formation.

scholarly journals Enhanced photocatalytic performance of rhodamine B and enrofloxacin by Pt loaded Bi4V2O11: boosted separation of charge carriers, additional superoxide radical production, and the photocatalytic mechanism

RSC Advances ◽  
2021 ◽  
Vol 11 (16) ◽  
pp. 9746-9755
Author(s):  
Yanjun Zhao ◽  
Xintong Liu ◽  
Shaonan Gu ◽  
Jiemin Liu
Keyword(s):  
Rhodamine B ◽  
Photocatalytic Performance ◽  
Superoxide Radical ◽  
Superoxide Radicals ◽  
Charge Carriers ◽  
Photocatalytic Mechanism ◽  
Radical Production

The Effect of Pt for producing additional superoxide radicals, and the photocatalytic mechanism.

scholarly journals Myeloperoxidase-Related Chlorination Activity Is Positively Associated with Circulating Ceruloplasmin in Chronic Heart Failure Patients: Relationship with Neurohormonal, Inflammatory, and Nutritional Parameters

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Aderville Cabassi ◽  
Simone Maurizio Binno ◽  
Stefano Tedeschi ◽  
Gallia Graiani ◽  
Cinzia Galizia ◽  
...  
Keyword(s):  
Heart Failure ◽  
Nitrosative Stress ◽  
Defense Mechanism ◽  
Nyha Class ◽  
Protein Nitration ◽  
Class Iii ◽  
Oxidative And Nitrosative Stress ◽  
Radical Production ◽  
Antioxidant Function ◽  
The Relationship

Rationale. Heart failure (HF) is accompanied by the development of an imbalance between oxygen- and nitric oxide-derived free radical production leading to protein nitration. Both chlorinating and peroxidase cycle of Myeloperoxidase (MPO) contribute to oxidative and nitrosative stress and are involved in tyrosine nitration of protein. Ceruloplasmin (Cp) has antioxidant function through its ferroxidase I (FeOxI) activity and has recently been proposed as a physiological defense mechanism against MPO inappropriate actions.Objective. We investigated the relationship between plasma MPO-related chlorinating activity, Cp and FeOxI, and nitrosative stress, inflammatory, neurohormonal, and nutritional biomarkers in HF patients.Methods and Results. In chronic HF patients (n=81, 76±9 years, NYHA Class II (26); Class III (29); Class IV (26)) and age-matched controls (n=17, 75±11 years, CTR), plasma MPO chlorinating activity, Cp, FeOxI, nitrated protein, free Malondialdehyde, BNP, norepinephrine, hsCRP, albumin, and prealbumin were measured. Plasma MPO chlorinating activity, Cp, BNP, norepinephrine, and hsCRP were increased in HF versus CTR. FeOxI, albumin, and prealbumin were decreased in HF. MPO-related chlorinating activity was positively related to Cp (r= 0.363,P<0.001), nitrated protein, hsCRP, and BNP and inversely to albumin.Conclusions. Plasma MPO chlorinated activity is increased in elderly chronic HF patients and positively associated with Cp, inflammatory, neurohormonal, and nitrosative parameters suggesting a role in HF progression.

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