DOCSLIB.ORG

Thioredoxin and Glutaredoxin Systems

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Thioredoxin and Glutaredoxin Systems antioxidants Thioredoxin and Glutaredoxin Systems Edited by Jean-Pierre Jacquot and Mirko Zaffagnini Printed Edition of the Special Issue Published in Antioxidants www.mdpi.com/journal/antioxidants Thioredoxin and Glutaredoxin Systems Thioredoxin and Glutaredoxin Systems Special Issue Editors Jean-Pierre Jacquot Mirko Zaffagnini MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editors Jean-Pierre Jacquot Mirko Zaffagnini Universite´ de Lorraine University of Bologna France Italy Editorial Office MDPI St. Alban-Anlage 66 4052 Basel, Switzerland This is a reprint of articles from the Special Issue published online in the open access journal Antioxidants (ISSN 2076-3921) from 2018 to 2019 (available at: https://www.mdpi.com/journal/ antioxidants/special issues/Thioredoxin and Glutaredoxin Systems) For citation purposes, cite each article independently as indicated on the article page online and as indicated below: LastName, A.A.; LastName, B.B.; LastName, C.C. Article Title. Journal Name Year, Article Number, Page Range. ISBN 978-3-03897-836-7 (Pbk) ISBN 978-3-03897-837-4 (PDF) Cover image courtesy of Jean-Pierre Jacquot. Fog rolling over the french Ormont mountain in the Vosges near Nayemont les Fosses in the fall of 2018. This was taken on a clear and very cold and sunny day, conditions favorable for generating reactive oxygen species in plants. The article of Dreyer and Dietz in this issue deals with cold and light stress in plants and the research done in the Rouhier group in Nancy addresses the physiology of trees in relation with their interacting with microorganisms and also in response to stress. c 2019 by the authors. Articles in this book are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book as a whole is distributed by MDPI under the terms and conditions of the Creative Commons license CC BY-NC-ND. Contents About the Special Issue Editors ..................................... vii Jean-Pierre Jacquot and Mirko Zaffagnini Thioredoxin and Glutaredoxin Systems Antioxidants Special Issue Reprinted from: Antioxidants 2019, 8, 68, doi:10.3390/antiox8030068 ................. 1 Christine Rampon, Michel Volovitch, Alain Joliot and Sophie Vriz Hydrogen Peroxide and Redox Regulation of Developments Reprinted from: Antioxidants 2018, 7, 159, doi:10.3390/antiox7110159 ................ 5 Pascal Rey and Lionel Tarrago Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling Reprinted from: Antioxidants 2018, 7, 114, doi:10.3390/antiox7090114 ................ 28 Sofia Louren¸co dos Santos, Isabelle Petropoulos and Bertrand Friguet The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function Reprinted from: Antioxidants 2018, 7, 191, doi:10.3390/antiox7120191 ................ 54 Anna Dreyer and Karl-Josef Dietz Reactive Oxygen Species and the Redox-Regulatory Network in Cold Stress Acclimation Reprinted from: Antioxidants 2018, 7, 169, doi:10.3390/antiox7110169 ................ 76 Rub´en M. Buey, Ruth A. Schmitz, Bob B. Buchanan and Monica Balsera Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon Reprinted from: Antioxidants 2018, 7, 166, doi:10.3390/antiox7110166 ................ 91 Genevi`eve Alloing, Karine Mandon, Eric Boncompagni, Fran¸coise Montrichard and Pierre Frendo Involvement of Glutaredoxin and Thioredoxin Systems in the Nitrogen-Fixing Symbiosis between Legumes and Rhizobia Reprinted from: Antioxidants 2018, 7, 182, doi:10.3390/antiox7120182 ................102 Juan Fern´andez-Trijueque, Antonio-Jesus ´ Serrato and Mariam Sahrawy Proteomic Analyses of Thioredoxins f and m Arabidopsis thaliana Mutants Indicate Specific Functions for These Proteins in Plants Reprinted from: Antioxidants 2019, 8, 54, doi:10.3390/antiox8030054 .................119 St´ephane D. Lemaire, Daniele Tedesco, Pierre Crozet, Laure Michelet, Simona Fermani, Mirko Zaffagnini and Julien Henri Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties Reprinted from: Antioxidants 2018, 7, 171, doi:10.3390/antiox7120171 ................133 Luis L´opez-Maury, Luis G. Heredia-Mart´ınez and Francisco J. Florencio Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria Reprinted from: Antioxidants 2018, 7, 164, doi:10.3390/antiox7110164 ................150 v Christophe H. Marchand, Simona Fermani, Jacopo Rossi, Libero Gurrieri, Daniele Tedesco, Julien Henri, Francesca Sparla, Paolo Trost, St´ephane D. Lemaire and Mirko Zaffagnini Structural and Biochemical Insights into the Reactivity of Thioredoxin h1 from Chlamydomonas reinhardtii Reprinted from: Antioxidants 2019, 8, 10, doi:10.3390/antiox8010010 .................165 Flavien Zannini, Thomas Roret, Jonathan Przybyla-Toscano, Tiphaine Dhalleine, Nicolas Rouhier and J´er´emy Couturier Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron–Sulfur Cluster and Reduce NFU Proteins In Vitro Reprinted from: Antioxidants 2018, 7, 142, doi:10.3390/antiox7100142 ................185 Keisuke Yoshida and Toru Hisabori Determining the Rate-Limiting Step for Light-Responsive Redox Regulation in Chloroplasts Reprinted from: Antioxidants 2018, 7, 153, doi:10.3390/antiox7110153 ................206 Adnan Khan Niazi, Laetitia Bariat, Christophe Riondet, Christine Carapito, Amna Mhamdi, Graham Noctor and Jean-Philippe Reichheld Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation Reprinted from: Antioxidants 2019, 8, 16, doi:10.3390/antiox8010016 .................214 H´el`ene Vanacker, Marjorie Guichard, Anne-Sophie Bohrer and Emmanuelle Issakidis-Bourguet Redox Regulation of Monodehydroascorbate Reductase by Thioredoxin y in Plastids Revealed in the Context of Water Stress Reprinted from: Antioxidants 2018, 7, 183, doi:10.3390/antiox7120183 ................231 Daniel Wittmann, Sigri Kløve, Peng Wang and Bernhard Grimm Towards Initial Indications for a Thiol-Based Redox Control of Arabidopsis 5-Aminolevulinic Acid Dehydratase Reprinted from: Antioxidants 2018, 7, 152, doi:10.3390/antiox7110152 ................247 Nicolas Navrot, Rikke Buhl Holstborg, Per H¨agglund, Inge Lise Povlsen and Birte Svensson New Insights into the Potential of Endogenous Redox Systems in Wheat Bread Dough Reprinted from: Antioxidants 2018, 7, 190, doi:10.3390/antiox7120190 ................261 vi About the Special Issue Editors Jean-Pierre Jacquot, Prof., works on redox regulation in plants via the thioredoxin and glutaredoxin systems. His early work elucidated the regulatory cascade of the ferredoxin–thioredoxin system and the physicochemical properties of its components (ferredoxin, thioredoxin reductase, and thioredoxins). He has also studied the molecular properties of its target enzymes (NADP-MDH and FBPase). More recent work of his concerns the study of plant glutaredoxins and their involvement in stress response and iron–sulfur assembly processes. Mirko Zaffagnini, Dr., currently works at the Department of Pharmacy and Biotechnology (FaBiT), University of Bologna. Dr. Zaffagnnini conducts research in plant physiology and biochemistry. His current projects are mainly focused on the role of thiol-based redox modifications in photosynthetic organisms. vii Fog rolling over the french Ormont mountain in the Vosges near Nayemont les Fosses in the fall of 2018. This was taken on a clear and very cold and sunny day, conditions favorable for generating reactive oxygen species in plants. The article of Dreyer and Dietz in this issue deals with cold and light stress in plants and the research done in the Rouhier group in Nancy addresses the physiology of trees in relation with their interacting with microorganisms and also in response to stress. Jean-Pierre Jacquot Guest Editor antioxidants Editorial Thioredoxin and Glutaredoxin Systems Antioxidants Special Issue Jean-Pierre Jacquot 1,* and Mirko Zaffagnini 2 1 Université de Lorraine, Inra, IAM, F-54000 Nancy, France 2 Laboratory of Molecular Plant Physiology, Department of Pharmacy and Biotechnology, University of Bologna, via Irnerio 42, 40126 Bologna, Italy; [email protected] * Correspondence: [email protected] Received: 14 March 2019; Accepted: 16 March 2019; Published: 18 March 2019 The special issue on Thioredoxin and Glutaredoxin systems (http://www.mdpi.com/journal/ antioxidants/special_issues/Thioredoxin_and_Glutaredoxin_Systems) was initiated in response to solicitations from Antioxidants after discussing with colleagues at two successive redox meetings sponsored by European Molecular Biology Organization (EMBO) and held in July 2017 in Moscow/St. Petersburg (http://redox.vub.ac.be/events/embo-redox-biology-conference.html) and in September of the same year in San Feliu de Guixols (Spain) (http://meetings.embo.org/event/17-thiol-ox). We could then submit the idea to long time collaborators and redox friends but also to other colleagues with whom we had the chance to get in touch with at these meetings. In general, although Antioxidants is a rather recent creation and its credentials were at the time not so well known, the idea of participating in a special issue was very well received
Load more

Recommended publications
  • Peroxiredoxins in Neurodegenerative Diseases
    antioxidants Review Peroxiredoxins in Neurodegenerative Diseases Monika Szeliga Mossakowski Medical Research Centre, Department of Neurotoxicology, Polish Academy of Sciences, 5 Pawinskiego Street, 02-106 Warsaw, Poland; [email protected]; Tel.: +48-(22)-6086416 Received: 31 October 2020; Accepted: 27 November 2020; Published: 30 November 2020 Abstract: Substantial evidence indicates that oxidative/nitrosative stress contributes to the neurodegenerative diseases. Peroxiredoxins (PRDXs) are one of the enzymatic antioxidant mechanisms neutralizing reactive oxygen/nitrogen species. Since mammalian PRDXs were identified 30 years ago, their significance was long overshadowed by the other well-studied ROS/RNS defense systems. An increasing number of studies suggests that these enzymes may be involved in the neurodegenerative process. This article reviews the current knowledge on the expression and putative roles of PRDXs in neurodegenerative disorders such as Alzheimer’s disease, Parkinson’s disease and dementia with Lewy bodies, multiple sclerosis, amyotrophic lateral sclerosis and Huntington’s disease. Keywords: peroxiredoxin (PRDX); oxidative stress; nitrosative stress; neurodegenerative disease 1. Introduction Under physiological conditions, reactive oxygen species (ROS, e.g., superoxide anion, O2 -; · hydrogen peroxide, H O ; hydroxyl radical, OH; organic hydroperoxide, ROOH) and reactive nitrogen 2 2 · species (RNS, e.g., nitric oxide, NO ; peroxynitrite, ONOO-) are constantly produced as a result of normal · cellular metabolism and play a crucial role in signal transduction, enzyme activation, gene expression, and regulation of immune response [1]. The cells are endowed with several enzymatic (e.g., glutathione peroxidase (GPx); peroxiredoxin (PRDX); thioredoxin (TRX); catalase (CAT); superoxide dismutase (SOD)), and non-enzymatic (e.g., glutathione (GSH); quinones; flavonoids) antioxidant systems that minimize the levels of ROS and RNS.
    [Show full text]
  • Targeted Genes and Methodology Details for Neuromuscular Genetic Panels
    Targeted Genes and Methodology Details for Neuromuscular Genetic Panels Reference transcripts based on build GRCh37 (hg19) interrogated by Neuromuscular Genetic Panels Next-generation sequencing (NGS) and/or Sanger sequencing is performed Motor Neuron Disease Panel to test for the presence of a mutation in these genes. Gene GenBank Accession Number Regions of homology, high GC-rich content, and repetitive sequences may ALS2 NM_020919 not provide accurate sequence. Therefore, all reported alterations detected ANG NM_001145 by NGS are confirmed by an independent reference method based on laboratory developed criteria. However, this does not rule out the possibility CHMP2B NM_014043 of a false-negative result in these regions. ERBB4 NM_005235 Sanger sequencing is used to confirm alterations detected by NGS when FIG4 NM_014845 appropriate.(Unpublished Mayo method) FUS NM_004960 HNRNPA1 NM_031157 OPTN NM_021980 PFN1 NM_005022 SETX NM_015046 SIGMAR1 NM_005866 SOD1 NM_000454 SQSTM1 NM_003900 TARDBP NM_007375 UBQLN2 NM_013444 VAPB NM_004738 VCP NM_007126 ©2018 Mayo Foundation for Medical Education and Research Page 1 of 14 MC4091-83rev1018 Muscular Dystrophy Panel Muscular Dystrophy Panel Gene GenBank Accession Number Gene GenBank Accession Number ACTA1 NM_001100 LMNA NM_170707 ANO5 NM_213599 LPIN1 NM_145693 B3GALNT2 NM_152490 MATR3 NM_199189 B4GAT1 NM_006876 MYH2 NM_017534 BAG3 NM_004281 MYH7 NM_000257 BIN1 NM_139343 MYOT NM_006790 BVES NM_007073 NEB NM_004543 CAPN3 NM_000070 PLEC NM_000445 CAV3 NM_033337 POMGNT1 NM_017739 CAVIN1 NM_012232 POMGNT2
    [Show full text]
  • Role of Oxidative Stress in the Pathogenesis of Amyotrophic Lateral Sclerosis: Antioxidant Metalloenzymes and Therapeutic Strategies
    biomolecules Review Role of Oxidative Stress in the Pathogenesis of Amyotrophic Lateral Sclerosis: Antioxidant Metalloenzymes and Therapeutic Strategies Pavlína Hemerková * and Martin Vališ Department of Neurology, Charles University, Faculty of Medicine and University Hospital Hradec Kralove, 500 05 Hradec Kralove, Czech Republic; [email protected] * Correspondence: [email protected]; Tel.: +420-731-304-371 Abstract: Amyotrophic lateral sclerosis (ALS) affects motor neurons in the cerebral cortex, brainstem and spinal cord and leads to death due to respiratory failure within three to five years. Although the clinical symptoms of this disease were first described in 1869 and it is the most common motor neuron disease and the most common neurodegenerative disease in middle-aged individuals, the exact etiopathogenesis of ALS remains unclear and it remains incurable. However, free oxygen radicals (i.e., molecules containing one or more free electrons) are known to contribute to the pathogenesis of this disease as they very readily bind intracellular structures, leading to functional impairment. Antioxidant enzymes, which are often metalloenzymes, inactivate free oxygen radicals by converting them into a less harmful substance. One of the most important antioxidant enzymes is Cu2+Zn2+ superoxide dismutase (SOD1), which is mutated in 20% of cases of the familial form of ALS (fALS) and up to 7% of sporadic ALS (sALS) cases. In addition, the proper functioning of catalase and glutathione peroxidase (GPx) is essential for antioxidant protection. In this review article, we focus on the mechanisms through which these enzymes are involved in the antioxidant response to oxidative Citation: Hemerková, P.; Vališ, M. Role of Oxidative Stress in the stress and thus the pathogenesis of ALS and their potential as therapeutic targets.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Corynebacterium Glutamicum Mycoredoxin 3 Protects Against Multiple Oxidative Stresses
    Advance Publication J. Gen. Appl. Microbiol. doi 10.2323/jgam.2019.10.003 ©2020 Applied Microbiology, Molecular and Cellular Biosciences Research Foundation Full Paper 1 Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses 2 and displays thioredoxin-like activity 3 (Received September 24, 2019; Accepted October 28, 2019; J-STAGE Advance publication date: October 30, 2020) 4 Tao Su#, Chengchuan Che#, Ping Sun, Xiaona Li, Zhijin Gong, Jinfeng Liu, Ge Yang * 5 6 College of Life Sciences, Qufu Normal University, Qufu, Shandong 273165, China; 7 8 Running title: Feature of C. glutamicum mycoredoxin 3 9 10 11 # These authors contributed equally to this work. 12 13 * Corresponding authors: 14 Ge Yang 15 16 E-mail [email protected] 17 Tel: 86-13953760056 18 19 20 21 22 23 24 25 26 27 Abstract 28 Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative 29 conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a 30 high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. 31 Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection 32 against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in 33 ribonucleotide reductase (RNR), insulin and 5, 5’-dithiobis-(2-nitro-benzoicacid) (DTNB), but 34 also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was 35 exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol 36 mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 37 were necessary to maintain its activity.
    [Show full text]
  • Generate Metabolic Map Poster
    Authors: Peter D. Karp Suzanne Paley Julio Collado-Vides John L Ingraham Ingrid Keseler Markus Krummenacker Cesar Bonavides-Martinez Robert Gunsalus An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Carol Fulcher Ian Paulsen Socorro Gama-Castro Robert LaRossa Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. EcoCyc: Escherichia coli K-12 substr. MG1655 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari Amanda Mackie Alberto Santos-Zavaleta succinate phosphate succinate N-acetyl-DL-methionine + L-ornithine glutathione + L-methionine S-oxide D-fructofuranose γ Ag+ molybdate ferroheme b L,L-homocystine asp lys cys L-alanyl- -D- D-mannopyranose 6-phosphate 2+ 2+ H D-methionine 2-deoxy-D-glucose succinate formate formate succinate D-tartrate putrescine agmatine cadaverine L-tartrate D-fructofuranose 6-phosphate + nitrate nitrate Cu thiosulfate deoxycholate L,L-homocystine D-cystine D-cycloserine methyl β-D-glucoside putrescine asp spermidine (S)-2-hydroxybutanoate (S)-2-hydroxybutanoate arg L-homoserine lactone magnesium hydrogenphosphate magnesium hydrogenphosphate antimonous acid glutamyl-meso- Co2+ Cd2+ lactulose poly-β-1,6- met cob(I)inamide 2,3-dioxo-
    [Show full text]
  • PRDX4 (Human) ELISA Kit 1
    PRDX4 (Human) ELISA Kit 1. The Association of Peroxiredoxin 4 with the Initiation and Progression of Hepatocellular Carcinoma. Guo X, Catalog Number: KA2121 Noguchi H, Ishii N, Homma T, Hamada T, Hiraki T, Zhang J, Matsuo K, Yokoyama S, Ishibashi H, Regulatory Status: For research use only (RUO) Fukushige T, Kanekura T, Fujii J, Uramoto H, Tanimoto A, Yamada S. Antioxid Redox Signal. 2018 Apr 24. Product Description: PRDX4 (Human) ELISA Kit is a [Epub ahead of print] sandwich enzyme immunoassay for the quantitative 2. Galectin-3 downregulates antioxidant peroxiredoxin-4 measurement of human PRDX4. in human cardiac fibroblasts: a new pathway to induce cardiac damage? Ibarrola J, Arrieta V, Sadaba R, Suitable Sample: Buffered solution Martinez-Martinez E, Garcia-Pena A, Alvarez V, Fernandez-Celis A, Gainza A, Santamaria E, Sample Volume: 100 uL Fernandez-Irigoyen J, Cachofeiro V, Zalba G, Fay R, Label: HRP-conjugated Rossignol P, Lopez-Andres N. Clin Sci (Lond). 2018 Apr 19. pii: CS20171389. [Epub ahead of print] Detection Method: Colorimetric 3. Overexpression of Peroxiredoxin 4 Affects Intestinal Function in a Dietary Mouse Model of Nonalcoholic Fatty Calibration Range: 78.13 to 5000 pg/mL Liver Disease. Nawata A, Noguchi H, Mazaki Y, Kurahashi T, Izumi H, Wang KY, Guo X, Uramoto H, Limit of Detection: 6.77 pg/mL Kohno K, Taniguchi H, Tanaka Y, Fujii J, Sasaguri Y, Tanimoto A, Nakayama T, Yamada S. PLoS One. 2016 Reactivity: Human Apr 1;11(4):e0152549. Applications: Quant (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product page for detailed protocols Storage Instruction: Store the kit at 4°C.
    [Show full text]
  • Dissecting the Transcriptional Phenotype of Ribosomal Protein Deficiency: Implications for Diamond-Blackfan Anemia
    Gene 545 (2014) 282–289 Contents lists available at ScienceDirect Gene journal homepage: www.elsevier.com/locate/gene Short Communication Dissecting the transcriptional phenotype of ribosomal protein deficiency: implications for Diamond-Blackfan Anemia Anna Aspesi a, Elisa Pavesi a, Elisa Robotti b, Rossella Crescitelli a,IleniaBoriac, Federica Avondo a, Hélène Moniz d, Lydie Da Costa d, Narla Mohandas e,PaolaRoncagliaf, Ugo Ramenghi g, Antonella Ronchi h, Stefano Gustincich f,SimoneMerlina,EmilioMarengob, Steven R. Ellis i, Antonia Follenzi a, Claudio Santoro a, Irma Dianzani a,⁎ a Department of Health Sciences, University of Eastern Piedmont, Novara, Italy b Department of Sciences and Technological Innovation, University of Eastern Piedmont, Alessandria, Italy c Department of Chemistry, University of Milan, Italy d U1009, AP-HP, Service d'Hématologie Biologique, Hôpital Robert Debré, Université Paris VII-Denis Diderot, Sorbonne Paris Cité, F-75475 Paris, France e New York Blood Center, NY, USA f International School for Advanced Studies (SISSA/ISAS), Trieste, Italy g Department of Pediatric Sciences, University of Torino, Torino, Italy h Department of Biotechnologies and Biosciences, Milano-Bicocca University, Italy i University of Louisville, KY, USA article info abstract Article history: Defects in genes encoding ribosomal proteins cause Diamond Blackfan Anemia (DBA), a red cell aplasia often as- Received 3 December 2013 sociated with physical abnormalities. Other bone marrow failure syndromes have been attributed to defects in Received in revised form 4 April 2014 ribosomal components but the link between erythropoiesis and the ribosome remains to be fully defined. Several Accepted 29 April 2014 lines of evidence suggest that defects in ribosome synthesis lead to “ribosomal stress” with p53 activation and Available online 15 May 2014 either cell cycle arrest or induction of apoptosis.
    [Show full text]
  • Targeting Glioblastoma Stem Cells Through Disruption of the Circadian Clock
    Published OnlineFirst August 27, 2019; DOI: 10.1158/2159-8290.CD-19-0215 RESEARCH ARTICLE Targeting Glioblastoma Stem Cells through Disruption of the Circadian Clock Zhen Dong1, Guoxin Zhang1, Meng Qu2, Ryan C. Gimple1,3, Qiulian Wu1, Zhixin Qiu1, Briana C. Prager1,3, Xiuxing Wang1, Leo J.Y. Kim1,3, Andrew R. Morton3, Deobrat Dixit1, Wenchao Zhou4, Haidong Huang4, Bin Li5, Zhe Zhu1, Shideng Bao4, Stephen C. Mack6, Lukas Chavez7, Steve A. Kay2, and Jeremy N. Rich1 Downloaded from cancerdiscovery.aacrjournals.org on September 24, 2021. © 2019 American Association for Cancer Research. Published OnlineFirst August 27, 2019; DOI: 10.1158/2159-8290.CD-19-0215 ABSTRACT Glioblastomas are highly lethal cancers, containing self-renewing glioblastoma stem cells (GSC). Here, we show that GSCs, differentiated glioblastoma cells (DGC), and nonmalignant brain cultures all displayed robust circadian rhythms, yet GSCs alone displayed exquisite dependence on core clock transcription factors, BMAL1 and CLOCK, for optimal cell growth. Downregulation of BMAL1 or CLOCK in GSCs induced cell-cycle arrest and apoptosis. Chromatin immu- noprecipitation revealed that BMAL1 preferentially bound metabolic genes and was associated with active chromatin regions in GSCs compared with neural stem cells. Targeting BMAL1 or CLOCK attenu- ated mitochondrial metabolic function and reduced expression of tricarboxylic acid cycle enzymes. Small-molecule agonists of two independent BMAL1–CLOCK negative regulators, the cryptochromes and REV-ERBs, downregulated stem cell factors and reduced GSC growth. Combination of cryp- tochrome and REV-ERB agonists induced synergistic antitumor effi cacy. Collectively, these fi ndings show that GSCs co-opt circadian regulators beyond canonical circadian circuitry to promote stemness maintenance and metabolism, offering novel therapeutic paradigms.
    [Show full text]
  • Lung Proteomic Biomarkers Associated with Chronic Obstructive Pulmonary Disease
    medRxiv preprint doi: https://doi.org/10.1101/2021.04.07.21255030; this version posted April 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission. Lung proteomic biomarkers associated with chronic obstructive pulmonary disease Yu-Hang Zhang1, Michael R. Hoopmann2, Peter J. Castaldi1, Kirsten A. Simonsen2, Mukul K. Midha2, Michael H. Cho1, Gerard J. Criner3, Raphael Bueno4, Jiangyuan Liu1, Robert L. Moritz2*, Edwin K. Silverman1* 1Channing Division of Network Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA 2Institute for Systems Biology, Seattle, WA, USA 3Temple University School of Medicine, Philadelphia, PA, USA 4Division of Thoracic Surgery, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA * These senior authors contributed equally to this work Corresponding Authors: Edwin K. Silverman, Email: [email protected] Robert L. Moritz, Email: [email protected] Keywords: chronic obstructive pulmonary disease, proteomics, biomarkers, mass spectrometry, machine learning NOTE: This preprint reports new research that has not been certified by peer review and should not be used to guide clinical practice. medRxiv preprint doi: https://doi.org/10.1101/2021.04.07.21255030; this version posted April 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission. ABSTRACT Background: Identifying protein biomarkers for chronic obstructive pulmonary disease (COPD) has been challenging.
    [Show full text]
  • Lapatinib Activates the Kelch-Like ECH- Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 Pathway in Hepg2 Cells
    Updates in Pharmacology Book Chapter Lapatinib Activates the Kelch-Like ECH- Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 Pathway in HepG2 Cells Noëmi Johanna Roos1,2,3, Diell Aliu1,2, Jamal Bouitbir1,2,3 and Stephan Krähenbühl1,2,3* 1Division of Clinical Pharmacology & Toxicology, University Hospital, Switzerland 2Department of Biomedicine, University of Basel, Switzerland 3Swiss Centre for Applied Human Toxicology (SCAHT), Switzerland *Corresponding Author: Stephan Krähenbühl, Division of Clinical Pharmacology & Toxicology, University Hospital, Basel, Switzerland Published October 26, 2020 This Book Chapter is a republication of an article published by Stephan Krähenbühl, et al. at Frontiers in Pharmacology in June 2020. (Roos NJ, Aliu D, Bouitbir J and Krähenbühl S (2020) Lapatinib Activates the Kelch-Like ECH-Associated Protein 1- Nuclear Factor Erythroid 2-Related Factor 2 Pathway in HepG2 Cells. Front. Pharmacol. 11:944. doi: 10.3389/fphar.2020.00944) How to cite this book chapter: Noëmi Johanna Roos, Diell Aliu, Jamal Bouitbir, Stephan Krähenbühl. Lapatinib Activates the Kelch-Like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 Pathway in HepG2 Cells. In: Nosheen Akhtar, editor. Updates in Pharmacology. Hyderabad, India: Vide Leaf. 2020. © The Author(s) 2020. This article is distributed under the terms of the Creative Commons Attribution 4.0 International 1 www.videleaf.com Updates in Pharmacology License(http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Data Availability Statement: All datasets for this study are included in the figshare repository: https://doi.org/10.6084/m9.figshare.12034608.v1.
    [Show full text]
  • Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases
    University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Vadim Gladyshev Publications Biochemistry, Department of February 2004 Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases Hwa-Young Kim University of Nebraska-Lincoln Vadim Gladyshev University of Nebraska-Lincoln, [email protected] Follow this and additional works at: https://digitalcommons.unl.edu/biochemgladyshev Part of the Biochemistry, Biophysics, and Structural Biology Commons Kim, Hwa-Young and Gladyshev, Vadim, "Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases" (2004). Vadim Gladyshev Publications. 7. https://digitalcommons.unl.edu/biochemgladyshev/7 This Article is brought to you for free and open access by the Biochemistry, Department of at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Vadim Gladyshev Publications by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Molecular Biology of the Cell Vol. 15, 1055–1064, March 2004 Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases Hwa-Young Kim and Vadim N. Gladyshev* Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588 Submitted August 28, 2003; Revised November 14, 2003; Accepted November 29, 2003 Monitoring Editor: Guido Guidotti Methionine residues in proteins are susceptible to oxidation by reactive oxygen species, but can be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide reduc- tase (MsrB). However, the identity of all methionine sulfoxide reductases involved, their cellular locations and relative contributions to the overall pathway are poorly understood. Here, we describe a methionine-R-sulfoxide reduction system in mammals, in which two MsrB homologues were previously described.
    [Show full text]