Recent Developments in Enzymatic Antioxidant Defence Mechanism in Plants with Special Reference to Abiotic Stress
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Formaldehyde Induces Bone Marrow Toxicity in Mice by Inhibiting Peroxiredoxin 2 Expression
MOLECULAR MEDICINE REPORTS 10: 1915-1920, 2014 Formaldehyde induces bone marrow toxicity in mice by inhibiting peroxiredoxin 2 expression GUANGYAN YU1, QIANG CHEN1, XIAOMEI LIU1, CAIXIA GUO2, HAIYING DU1 and ZHIWEI SUN1,2 1Department of Preventative Medicine, School of Public Health, Jilin University, Changchun, Jilin 130021; 2 Department of Hygenic Toxicology, School of Public Health, Capital Medical University, Beijing 100069, P.R. China Received November 4, 2013; Accepted June 5, 2014 DOI: 10.3892/mmr.2014.2473 Abstract. Peroxiredoxin 2 (Prx2), a member of the perox- Introduction iredoxin family, regulates numerous cellular processes through intracellular oxidative signal transduction pathways. Formaldehyde (FA) is an environmental agent commonly Formaldehyde (FA)-induced toxic damage involves reactive found in numerous products, including paint, cloth and oxygen species (ROS) that trigger subsequent toxic effects and exhaust gas, as well as other medicinal and industrial products. inflammatory responses. The present study aimed to inves- FA exposure has raised significant concerns due to mounting tigate the role of Prx2 in the development of bone marrow evidence suggesting its carcinogenic potential and severe toxicity caused by FA and the mechanism underlying FA effects on human health (1). Epidemiological and experi- toxicity. According to the results of the preliminary inves- mental data have demonstrated that FA may cause leukemia, tigations, the mice were divided into four groups (n=6 per particularly myeloid leukemia; however, the mechanism group). One group was exposed to ambient air and the other underlying this effect remains unclear (2-4). In the process three groups were exposed to different concentrations of FA of tumor formation, DNA damage may be the initiating (20, 40, 80 mg/m3) for 15 days in the respective inhalation factor (5), while myeloperoxidase (MPO) activity is associ- chambers, for 2 h a day. -
Current IUBMB Recommendations on Enzyme Nomenclature and Kinetics$
Perspectives in Science (2014) 1,74–87 Available online at www.sciencedirect.com www.elsevier.com/locate/pisc REVIEW Current IUBMB recommendations on enzyme nomenclature and kinetics$ Athel Cornish-Bowden CNRS-BIP, 31 chemin Joseph-Aiguier, B.P. 71, 13402 Marseille Cedex 20, France Received 9 July 2013; accepted 6 November 2013; Available online 27 March 2014 KEYWORDS Abstract Enzyme kinetics; The International Union of Biochemistry (IUB, now IUBMB) prepared recommendations for Rate of reaction; describing the kinetic behaviour of enzymes in 1981. Despite the more than 30 years that have Enzyme passed since these have not subsequently been revised, though in various respects they do not nomenclature; adequately cover current needs. The IUBMB is also responsible for recommendations on the Enzyme classification naming and classification of enzymes. In contrast to the case of kinetics, these recommenda- tions are kept continuously up to date. & 2014 The Author. Published by Elsevier GmbH. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Contents Introduction...................................................................75 Kinetics introduction...........................................................75 Introduction to enzyme nomenclature ................................................76 Basic definitions ................................................................76 Rates of consumption and formation .................................................76 Rate of reaction .............................................................76 -
Collection of Information on Enzymes a Great Deal of Additional Information on the European Union Is Available on the Internet
European Commission Collection of information on enzymes A great deal of additional information on the European Union is available on the Internet. It can be accessed through the Europa server (http://europa.eu.int). Luxembourg: Office for Official Publications of the European Communities, 2002 ISBN 92-894-4218-2 © European Communities, 2002 Reproduction is authorised provided the source is acknowledged. Final Report „Collection of Information on Enzymes“ Contract No B4-3040/2000/278245/MAR/E2 in co-operation between the Federal Environment Agency Austria Spittelauer Lände 5, A-1090 Vienna, http://www.ubavie.gv.at and the Inter-University Research Center for Technology, Work and Culture (IFF/IFZ) Schlögelgasse 2, A-8010 Graz, http://www.ifz.tu-graz.ac.at PROJECT TEAM (VIENNA / GRAZ) Werner Aberer c Maria Hahn a Manfred Klade b Uli Seebacher b Armin Spök (Co-ordinator Graz) b Karoline Wallner a Helmut Witzani (Co-ordinator Vienna) a a Austrian Federal Environmental Agency (UBA), Vienna b Inter-University Research Center for Technology, Work, and Culture - IFF/IFZ, Graz c University of Graz, Department of Dermatology, Division of Environmental Dermatology, Graz Executive Summary 5 EXECUTIVE SUMMARY Technical Aspects of Enzymes (Chapter 3) Application of enzymes (Section 3.2) Enzymes are applied in various areas of application, the most important ones are technical use, manufacturing of food and feedstuff, cosmetics, medicinal products and as tools for re- search and development. Enzymatic processes - usually carried out under mild conditions - are often replacing steps in traditional chemical processes which were carried out under harsh industrial environments (temperature, pressures, pH, chemicals). Technical enzymes are applied in detergents, for pulp and paper applications, in textile manufacturing, leather industry, for fuel production and for the production of pharmaceuticals and chiral substances in the chemical industry. -
K746-200 Myeloperoxidase (MPO) Inhibitor Screening
FOR RESEARCH USE ONLY! Myeloperoxidase (MPO) Inhibitor Screening Kit (Fluorometric) rev. 08/15 (Catalog # K746-200; 200 assays; Store at -20°C) I. Introduction: Myeloperoxidase (MPO: EC 1.11.2.2) is a peroxidase abundantly expressed in neutrophil granulocytes. It catalyzes the hydrogen peroxide dependent oxidation of halide ions to generate hypochlorite (HClO), the reaction by which MPO exhibits cytotoxic activity against tumor cells and microorganisms. MPO also oxidizes various substances such as phenol and anilines. MPO undergoes chlorination or peroxidation reaction depending upon the relative concentrations of chloride and the reducing substrates. Recent studies suggest that increased levels of MPO are associated with an increased risk for cardiovascular disease and myocardial infarction, thus development of novel and specific inhibitors of MPO is critical for therapeutic purposes. BioVision’s MPO Inhibitor Screening Kit provides screening assays for both MPO chlorination and peroxidation activities. In the chlorination assay (specific for MPO), MPO converts hydrogen peroxide and sodium chloride to sodium hypochlorite, which reacts with Chlorination substrate to give an intensely fluorescent product (Ex/Em = 480/520 nm). In the Peroxidation Assay, MPO oxidizes peroxidation substrate to generate fluorescence (Ex/Em = 535/587 nm). The fluorescence generated is directly proportional to any peroxidase activity present. In the presence of MPO inhibitor, reactions are impeded, thus decreasing the rate and/or extent of generation of MPO-dependent fluorescence. This kit provides a sensitive, quick, and easy method for screening potential inhibitors of MPO, and identifying whether one or both activities are inhibited. MPO Inhibitor Control is included to compare the efficacy of test inhibitors. -
The Alteration of Superoxide Dismutase, Catalase, Glutathione
The alteration of superoxide dismutase, catalase, glutathione peroxidase, and NAD(P)H cytochrome c reductase in guinea pig polymorphonuclear leukocytes and alveolar macrophages during hyperoxia. M Rister, R L Baehner J Clin Invest. 1976;58(5):1174-1184. https://doi.org/10.1172/JCI108570. Research Article Superoxide dismutase, catalase, glutathione peroxidase and NAD(P)H cytochrome c reductase were quantitated in polymorphonuclear leukocytes (PMN) and alveolar macrophages (AM) obtained from guinea pigs exposed up to 90 h to 85% oxygen. PMN and AM were sonicated and separated into a 16,000-g pellet, a 100,000-g pellet, and a 100,00-g supernate. Superoxide dismutase activity increased in both cells within 18 h, persisted for 66 h and decreased by 90 h. The highest rate of increase was in the 100,000-g pellet containing 3.4% of total enzyme activity in PMN but 28% in AM. The enzyme induction in PMN and AM was partially inhibited by daily intracardiac injections of 50 mg/kg actinomycin D. During oxygen exposure, catalase activity in PMN and AM decreased to 60% of its original activity, and gluthathione peroxidase was reduced in PMN to 60% and in AM to 20% of control values. Although NAD(P)H cytochrome c reductase decreased to 50% in PMN, no change was noted in AM. Upon exposure to superoxide anion, purified catalase, the glutathione peroxidase of the 100,000-g supernate, NADH, and NADPH cytochrome c reductases of the 16,000-g pellet decreased to 66+/-5%, 72+/-4%, 52+/-8%, and 40+/-9%, respectively, of their original activity. -
Hydrogen Peroxide Metabolism and Functions in Plants
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Open Research Exeter PROF. NICHOLAS SMIRNOFF (Orcid ID : 0000-0001-5630-5602) Article type : Commissioned Material - Tansley Review Hydrogen peroxide metabolism and functions in plants Nicholas Smirnoff and Dominique Arnaud Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, UK. Corresponding author: Nicholas Smirnoff [email protected]. +44 (0)1392 725168, ORCID: Article 0000-0001-5630-5602 Received: 10 April 2018 Accepted: 28 August 2018 Contents Summary I. Introduction II. Measuring and imaging hydrogen peroxide III. Hydrogen peroxide and superoxide toxicity IV. Production of hydrogen peroxide: enzymes and subcellular locations V. Hydrogen peroxide transport VI. Control of hydrogen peroxide concentration: how and where? VII. Metabolic functions of hydrogen peroxide VIII. Hydrogen peroxide signalling This article has been accepted for publication and undergone full peer review but has not Accepted been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1111/nph.15488 This article is protected by copyright. All rights reserved. IX. Where next? Acknowledgements References Summary H2O2 is produced, via superoxide and superoxide dismutase, by electron transport in chloroplasts and mitochondria, plasma membrane NADPH oxidases, peroxisomal oxidases, type III peroxidases and other apoplastic oxidases. Intracellular transport is facilitated by aquaporins and H2O2 is removed by catalase, peroxiredoxin, glutathione peroxidase-like enzymes and ascorbate peroxidase, all of which have cell compartment-specific isoforms. Apoplastic H2O2 influences cell expansion, development and defence by its involvement in type III peroxidase-mediated polymer cross-linking, lignification and, possibly, cell expansion via H2O2-derived hydroxyl radicals. -
Metalloenzymes: Native Co-Factor Or Experimental Artifact? Marcy Hernick* Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA
nalytic A al & B y i tr o s c i h e Hernick, Biochem Anal Biochem 2012, 1:6 m m e Biochemistry & i h s c t r o DOI: 10.4172/2161-1009.1000e120 i y B ISSN: 2161-1009 Analytical Biochemistry Editorial Open Access Metalloenzymes: Native Co-factor or Experimental Artifact? Marcy Hernick* Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA There has been much interest in the biochemical characterization metallohydrolases. Superoxide dismutase (SOD) is an example of a of metalloenzymes, owing in part to past successes in targeting metalloenzyme that utilizes Mn2+, Fe2+, or Mn/Fe as native co-factors metalloenzymes for the development of therapeutic agents. It is across different species [16-20]. (Note: The cited references offer just a estimated that ~10% of approved drugs target metalloenzymes, [1] such small sampling of the research examining SOD co-factor preferences). as carbonic anhydrase, matrix metalloprotesases, and angiotensin- These detailed studies on SOD reinforce the important contributions converting enzyme [2-5]. Inhibitors of metalloenzymes typically that metal ion availability and experimental conditions have on contain a metal-binding group that targets the catalytic metal ion, identifying the native co-factor(s) preferences of metalloenzymes. and therefore, inhibitor affinity is affected by changes to the catalytic In addition to metalloenzymes that prefer a single co-factor as metal ion. Consequently, the development of therapeutically effective described above, there are also increasing numbers of cambialistic inhibitors requires that the biologically relevant form(s) of the enzyme enzymes that can utilize multiple co-factors in vivo has been identified. -
The Role of Peroxiredoxin 6 in Cell Signaling
antioxidants Review The Role of Peroxiredoxin 6 in Cell Signaling José A. Arevalo and José Pablo Vázquez-Medina * Department of Integrative Biology, University of California, Berkeley, CA, 94705, USA; [email protected] * Correspondence: [email protected]; Tel.: +1-510-664-5063 Received: 7 November 2018; Accepted: 20 November 2018; Published: 24 November 2018 Abstract: Peroxiredoxin 6 (Prdx6, 1-cys peroxiredoxin) is a unique member of the peroxiredoxin family that, in contrast to other mammalian peroxiredoxins, lacks a resolving cysteine and uses glutathione and π glutathione S-transferase to complete its catalytic cycle. Prdx6 is also the only peroxiredoxin capable of reducing phospholipid hydroperoxides through its glutathione peroxidase (Gpx) activity. In addition to its peroxidase activity, Prdx6 expresses acidic calcium-independent phospholipase A2 (aiPLA2) and lysophosphatidylcholine acyl transferase (LPCAT) activities in separate catalytic sites. Prdx6 plays crucial roles in lung phospholipid metabolism, lipid peroxidation repair, and inflammatory signaling. Here, we review how the distinct activities of Prdx6 are regulated during physiological and pathological conditions, in addition to the role of Prdx6 in cellular signaling and disease. Keywords: glutathione peroxidase; phospholipase A2; inflammation; lipid peroxidation; NADPH (nicotinamide adenine dinucleotide phosphate) oxidase; phospholipid hydroperoxide 1. Introduction Peroxiredoxins are a ubiquitous family of highly conserved enzymes that share a catalytic mechanism in which a redox-active (peroxidatic) cysteine residue in the active site is oxidized by a peroxide [1]. In peroxiredoxins 1–5 (2-cys peroxiredoxins), the resulting sulfenic acid then reacts with another (resolving) cysteine residue, forming a disulfide that is subsequently reduced by an appropriate electron donor to complete a catalytic cycle [2,3]. -
Investigation of Glutathione Peroxidase Activity in Chicken Meat
Ciência e Tecnologia de Alimentos ISSN 0101-2061 Investigation of glutathione peroxidase activity in chicken meat under different experimental conditions Original Investigação da atividade de glutationa peroxidase em carne de frango submetida a diferentes condições experimentais Alexandre José CICHOSKI1*, Renata Bezerra ROTTA2, Gerson SCHEUERMANN3, Anildo CUNHA JUNIOR3, Juliano Smanioto BARIN1 Abstract Due to the fact that previous studies on the enzymatic activity of Glutathione peroxidase (GSH-Px) diverge widely in their methodology and results, this study aimed to investigate the influence of different analytical conditions on GSH-Px activity in chicken thighs from broilers that were fed different diets with different sources and concentrations of selenium. GSH-Px activity was evaluated six hours after slaughter and 120 days after frozen storage at –18 °C. The different analytical conditions included time of pre-incubation (0, 10 and 30 minutes), reaction medium, types of substrate (H2O2 (0.72 mM, 7.2 mM, and 72 mM) and Terc-butil hydroperoxide 15 mM), and different buffer concentrations (buffer 1, potassium phosphate 50 mM pH 7.0 + EDTA 1 mM + mercaptoethanol 1 mM, and buffer 2, tris-HCl 50 mM pH 7.6 + EDTA 1 mM + mercapthanol 5 mM). The results show that the highest GSH-Px activity was observed when enzyme and substrate were in contact at 22 °C without any pre-incubation, and that, when used at concentrations above 0.72 mM, hydrogen peroxide saturated the GSH-Px enzyme and inhibited its activity. The enzyme presented higher affinity to hydrogen peroxide when compared to terc-butil peroxide, and the addition of a buffer containing mercaptoethanol did not increase GSH-Px enzymatic activity. -
Translational Regulation of Glutathione Peroxidase 4 Expression Through Guanine- Rich Sequence-Binding Factor 1 Is Essential for Embryonic Brain Development
Downloaded from genesdev.cshlp.org on September 24, 2021 - Published by Cold Spring Harbor Laboratory Press Translational regulation of glutathione peroxidase 4 expression through guanine- rich sequence-binding factor 1 is essential for embryonic brain development Christoph Ufer,1,2,6 Chi Chiu Wang,3,4,6 Michael Fähling,5 Heike Schiebel,1 Bernd J. Thiele,5 E. Ellen Billett,2 Hartmut Kuhn,1,7 and Astrid Borchert1 1Institute of Biochemistry, University Medicine Berlin–Charité, D-10117 Berlin, F.R. Germany; 2School of Science and Technology, Nottingham Trent University, Nottingham NG11 8NS, United Kingdom; 3Li Ka Shing Institute of Health Sciences, The Chinese University of Hong Kong, Shatin, Hong Kong; 4Department of Obstetrics and Gynaecology, The Chinese University of Hong Kong, Shatin, Hong Kong; 5Institute of Physiology, University Medicine Berlin–Charité, D-10117 Berlin, F.R. Germany Phospholipid hydroperoxide glutathione peroxidase (GPx4) is a moonlighting selenoprotein, which has been implicated in basic cell functions such as anti-oxidative defense, apoptosis, and gene expression regulation. GPx4-null mice die in utero at midgestation, and developmental retardation of the brain appears to play a major role. We investigated post-transcriptional mechanisms of GPx4 expression regulation and found that the guanine-rich sequence-binding factor 1 (Grsf1) up-regulates GPx4 expression. Grsf1 binds (to a defined target sequence in the 5-untranslated region (UTR) of the mitochondrial GPx4 (m-GPx4 mRNA, up-regulates UTR-dependent reporter gene expression, recruits m-GPx4 mRNA to translationally active polysome fractions, and coimmunoprecipitates with GPx4 mRNA. During embryonic brain development, Grsf1 and m-GPx4 are coexpressed, and functional knockdown (siRNA) of Grsf1 prevents embryonic GPx4 expression. -
Expression of Manganese Superoxide Dismutase in Ovine Kidney Cortex During Development
003 I-3998/94/350 1-004 1 $03.00/0 PEDIATRIC RESEARCH Vol. 35, No. 1, 1994 Copyright O 1993 International Pediatric Research Foundation, Inc. Printed in U.S.A. Expression of Manganese Superoxide Dismutase in Ovine Kidney Cortex during Development G. M. R. CARBONE, D. K. ST. CLAIR, Y. ANNE XU, AND J. C. ROSE Department of Physiology and Pharmacology, Perinatal Research Laboratories, Bowman Gray School of Medicine of Wake Forest University, Winston-Salem.North Carolina 27157[G.M.R.C.,J.C.R.], and Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40506-0054 [D.K.St.C.,Y.A.X.] ABSTRACT. Manganese superoxide dismutase (MnSOD) Recent data indicate that the activity of antioxidant enzymes is one of the main antioxidant enzymes in mammalian is developmentally regulated in the kidney as it is in the lung. tissue. Previous studies have shown that the activity of MnSOD activity has been shown to increase in guinea pig and MnSOD increases in the rat kidney during development. rat kidney from fetal to the adult period (2, 7). In addition, To define further the developmental change in MnSOD MnSOD has been also detected by immunohistochemistry in activity and better understand some of the steps involved kidney cortex and medulla in the Syrian hamster and the staining in the control of MnSOD expression during kidney devel- increases progressively during development (8). opment, we measured MnSOD messenger RNA and en- Therefore, to understand better the mechanisms of MnSOD zyme activity in the ovine kidney cortex during fetal life, expression in the developing kidney, we measured MnSOD in the newborn period, and in adults. -
Contribution of Glutathione Peroxidase to the Virulence of Streptococcus Pyogenes Audrey Brenot Washington University School of Medicine in St
Washington University School of Medicine Digital Commons@Becker Open Access Publications 2004 Contribution of glutathione peroxidase to the virulence of streptococcus pyogenes Audrey Brenot Washington University School of Medicine in St. Louis Katherine Y. King Washington University School of Medicine in St. Louis Blythe Janowiak Medical College of Wisconsin Owen Griffith Medical College of Wisconsin Michael G. Caparon Washington University School of Medicine in St. Louis Follow this and additional works at: https://digitalcommons.wustl.edu/open_access_pubs Recommended Citation Brenot, Audrey; King, Katherine Y.; Janowiak, Blythe; Griffith, Owen; and Caparon, Michael G., ,"Contribution of glutathione peroxidase to the virulence of streptococcus pyogenes." Infection and Immunity.72,1. 408-413. (2004). https://digitalcommons.wustl.edu/open_access_pubs/2058 This Open Access Publication is brought to you for free and open access by Digital Commons@Becker. It has been accepted for inclusion in Open Access Publications by an authorized administrator of Digital Commons@Becker. For more information, please contact [email protected]. Contribution of Glutathione Peroxidase to the Virulence of Streptococcus pyogenes Audrey Brenot, Katherine Y. King, Blythe Janowiak, Owen Griffith and Michael G. Caparon Infect. Immun. 2004, 72(1):408. DOI: 10.1128/IAI.72.1.408-413.2004. Downloaded from Updated information and services can be found at: http://iai.asm.org/content/72/1/408 http://iai.asm.org/ These include: REFERENCES This article cites 31 articles, 23 of which can be accessed free at: http://iai.asm.org/content/72/1/408#ref-list-1 CONTENT ALERTS Receive: RSS Feeds, eTOCs, free email alerts (when new on January 16, 2014 by Washington University in St.