DOCSLIB.ORG

Regulation and Functions of Acute Phase Proteins

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Regulation and Functions of Acute Phase Proteins ACUTE PHASE ROTEI REG ULATION AND FUNCTIONS OF ACUTE PHASE PROTEINS Edited by Fra cisco Veas INTECH ACUTE PHASE PROTEINS – REGULATION AND FUNCTIONS OF ACUTE PHASE PROTEINS Edited by Francisco Veas Acute Phase Proteins – Regulation and Functions of Acute Phase Proteins Edited by Francisco Veas Published by InTech Janeza Trdine 9, 51000 Rijeka, Croatia Copyright © 2011 InTech All chapters are Open Access articles distributed under the Creative Commons Non Commercial Share Alike Attribution 3.0 license, which permits to copy, distribute, transmit, and adapt the work in any medium, so long as the original work is properly cited. After this work has been published by InTech, authors have the right to republish it, in whole or part, in any publication of which they are the author, and to make other personal use of the work. Any republication, referencing or personal use of the work must explicitly identify the original source. Statements and opinions expressed in the chapters are these of the individual contributors and not necessarily those of the editors or publisher. No responsibility is accepted for the accuracy of information contained in the published articles. The publisher assumes no responsibility for any damage or injury to persons or property arising out of the use of any materials, instructions, methods or ideas contained in the book. Publishing Process Manager Davor Vidic Technical Editor Teodora Smiljanic Cover Designer Jan Hyrat Image Copyright Ali Mazraie Shadi, 2011. Used under license from Shutterstock.com First published September, 2011 Printed in Croatia A free online edition of this book is available at www.intechopen.com Additional hard copies can be obtained from [email protected] Acute Phase Proteins – Regulation and Functions of Acute Phase Proteins, Edited by Francisco Veas p. cm. ISBN 978-953-307-252-4 free online editions of InTech Books and Journals can be found at www.intechopen.com Contents Preface IX Chapter 1 Transcriptional Regulation of Acute Phase Protein Genes 1 Claude Asselin and Mylène Blais Chapter 2 Acute Phase Proteins: Structure and Function Relationship 25 Sabina Janciauskiene, Tobias Welte and Ravi Mahadeva Chapter 3 Regulatory Mechanisms Controlling Inflammation and Synthesis of Acute Phase Proteins 61 Jolanta Jura and Aleksander Koj Chapter 4 IL-22 Induces an Acute-Phase Response Associated to a Cohort of Acute Phase Proteins and Antimicrobial Peptides as Players of Homeostasis 85 Francisco Veas and Gregor Dubois Chapter 5 Hemostatic Soluble Plasma Proteins During Acute-Phase Response and Chronic Inflammation 105 Irina I. Patalakh Chapter 6 Brain Barriers and the Acute-Phase Response 137 Fernanda Marques, Margarida Correia-Neves, João Carlos Sousa, Nuno Sousa and Joana Almeida Palha Chapter 7 Acute Phase Proteins: Ferritin and Ferritin Isoforms 153 Alida Maria Koorts and Margaretha Viljoen Chapter 8 The Hepatic Acute Phase Response to Thermal Injury 185 Marc G. Jeschke Chapter 9 Adipocytokines in Severe Sepsis and Septic Shock 211 Hanna Dückers, Frank Tacke, Christian Trautwein and Alexander Koch VI Contents Chapter 10 Haptoglobin Function and Regulation in Autoimmune Diseases 229 Georgina Galicia and Jan L. Ceuppens Chapter 11 Acute-Phase Proteins: Alpha -1- Acid Glycoprotein 247 C. Tesseromatis, A. Alevizou, E. Tigka and A. Kotsiou Chapter 12 Haptoglobin and Hemopexin in Heme Detoxification and Iron Recycling 261 Deborah Chiabrando, Francesca Vinchi, Veronica Fiorito and Emanuela Tolosano Chapter 13 Haptoglobin is an Exercise-Responsive Acute-Phase Protein 289 Cheng-Yu Chen, Wan-Ling Hsieh, Po-Ju Lin, Yung-Liang Chen and Simon J. T. Mao Chapter 14 Acute Phase Proteins in Prototype Rheumatic Inflammatory Diseases 303 Katja Lakota, Mojca Frank, Olivio Buzan, Matija Tomsic, Blaz Rozman and Snezna Sodin-Semrl Chapter 15 Role of Fetuin-A in Injury and Infection 329 Haichao Wang, Wei Li, Shu Zhu, Ping Wang and Andrew E. Sama Chapter 16 Neutrophil Gelatinase Associated Lipocalin: Structure, Function and Role in Human Pathogenesis 345 Subhankar Chakraborty, Sukhwinder Kaur, Zhimin Tong, Surinder K. Batra and Sushovan Guha Preface A dynamic physiological equilibrium known under the name of homeostasis is determined by endogenous factors and by interactions of organisms with their exogenous environment. To preserve this equilibrium state, which reflects a healthy state of the individual, the organism is constantly sensing and adjusting levels of factors involved in these mechanisms participating to the equilibrium. Most of these homeostatic factors are well preserved because of their highly relevant functional importance for life. Depending on species, some of them could vary in their expression, and will be adapted to the encountered situations. These conserved innate strategies will not only have effects on individuals, but also on populations and moreover in their relations with the environmental stimuli (temperature, humidity, chemical, infections, diet). A broad and conserved response to internal or external stimuli will very quickly be induced, in a matter of minutes, to generate a cascade of inflammatory processes in order to reestablish the homeostatic state in the organism as soon as possible. Stimuli inducing homeostatic changes can be of different nature: trauma, toxin, infection, genetic dysfunction, childbirth, etc. The process of acute inflammation is initiated by cells already present in all tissues, including macrophages, dendritic cells, Kupffer cells. These cells harbor surfaces pattern recognition receptors (PRRs), which recognize at the beginning of the infectious process, exogenous molecules broadly shared by pathogens (pathogen- associated molecular patterns, PAMPs), but not by the host. Important addition to PAMPs, but to a lesser extent, are non-pathogenic microorganisms which also harbor the highly conserved molecules recognized as non-self that will induce a very low level of local inflammation. This response is amplified by endogenously released mediators and by co-factors or concomitant stressful events (burn, trauma, apoptosis, etc.) as well as molecular mechanisms involved in the vicious circle of destruction- reconstruction of vessels and tissues, acting through injury-associated signals known as Damage-Associated Molecular Patterns (DAMPs or Alarmins) and acute phase proteins. Moreover, some of the APP are also antimicrobials exhibiting a wide range of defensive functions, that alongside their repair functions help to reduce pathologic damage, and consequently help to restore the homeostasis. X Preface The maintaining of homeostasis requires rapid and short acute inflammatory responsiveness. Inflammatory mediators, including APP, exhibit short half-lives, which ensures that the inflammatory phenomenon ceases as soon as the stimulus disappears. In contrast, the presence of APP at increased levels can be considered as sensitive sensor of homeostasis disruption. Persisting levels of APP are observed in chronic diseases. The inflammation process is strongly associated with vascular changes as vasodilation and its resulting increased blood flow causes the redness (rubor) and increased heat (calor) as well as an augmented permeability resulting in a plasma protein leakage into the tissue causing edema, observed as swelling (tumor) and pain (dolor). Activated cells will then migrate the injury site. Depending on the intensity of inflammation and the organ in question, it is possible to observe the fifth component of inflammation as described by Aulus Cornelius Celsus in his treatise On Medicine (1st century BC) - loss of function (functio laesa) that results from cross talk between inflammation process and the central nervous system. The two volumes of Acute Phase Proteins book consist of chapters that give a large panel of fundamental and applied knowledge on one of the major elements of the inflammatory process during the acute phase response, i.e., the acute phase proteins expression and functions that regulate homeostasis. We have organized this book in two volumes - the first volume, mainly containing chapters on structure, biology and functions of APP, the second volume discussing different uses of APP as diagnostic tools in human and veterinary medicine. By using an open access publishing model, we wanted to facilitate a large access to readers from different places all over the world, notably developing countries, with the aim of contributing to a better world of knowledge. We also wanted to dedicate this book to our colleagues from both academia and industry in order to create values of knowledge in the field of control of inflammatory processes occurring in diverse diseases to improve the management efficacy of a more personalized medicine. At present, CRP and SAA are the most responsive APP during inflammatory processes in humans. In most cases they are associated with the erythrocyte sedimentation rate (ESR) marker, which strongly depends on high fibrinogen concentration allowing the sticking between erythrocytes. In mice, some changes are also reported for SAA. Despite the fact that the field of inflammation and its associated factors, including APP, cytokines antimicrobial peptides, etc., have been observed and studied from very ancient times, a detailed and updated knowledge is urgently needed as well as pivotal in future research for an integrative personalized medicine that takes into account several parameters including nutritional and systemic factors. Particularly, with the help of large-scale identification methods, such as proteomics, transcriptomics,
Load more

Recommended publications
  • Cysteine Proteinases of Microorganisms and Viruses
    ISSN 00062979, Biochemistry (Moscow), 2008, Vol. 73, No. 1, pp. 113. © Pleiades Publishing, Ltd., 2008. Original Russian Text © G. N. Rudenskaya, D. V. Pupov, 2008, published in Biokhimiya, 2008, Vol. 73, No. 1, pp. 317. REVIEW Cysteine Proteinases of Microorganisms and Viruses G. N. Rudenskaya1* and D. V. Pupov2 1Faculty of Chemistry and 2Faculty of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 9393181; Email: [email protected] Received May 7, 2007 Revision received July 18, 2007 Abstract—This review considers properties of secreted cysteine proteinases of protozoa, bacteria, and viruses and presents information on the contemporary taxonomy of cysteine proteinases. Literature data on the structure and physicochemical and enzymatic properties of these enzymes are reviewed. High interest in cysteine proteinases is explained by the discovery of these enzymes mostly in pathogenic organisms. The role of the proteinases in pathogenesis of several severe diseases of human and animals is discussed. DOI: 10.1134/S000629790801001X Key words: cysteine proteinases, properties, protozoa, bacteria, viruses Classification and Catalytic Mechanism papain and related peptidases showed that the catalytic of Cysteine Proteinases residues are arranged in the following order in the polypeptide chain: Cys, His, and Asn. Also, a glutamine Cysteine proteinases are peptidyl hydrolases in residue preceding the catalytic cysteine is also important which the role of the nucleophilic group of the active site for catalysis. This residue is probably involved in the for is performed by the sulfhydryl group of a cysteine residue. mation of the oxyanion cavity of the enzyme. The cat Cysteine proteinases were first discovered and investigat alytic cysteine residue is usually followed by a residue of ed in tropic plants.
    [Show full text]
  • Characterization of Cathepsin L Genes and Their Cdnas in the Brine Shrimp, Artemia Franciscana
    University of Windsor Scholarship at UWindsor Electronic Theses and Dissertations Theses, Dissertations, and Major Papers 2006 Characterization of cathepsin L genes and their cDNAs in the brine shrimp, Artemia franciscana. Jian Ping Cao University of Windsor Follow this and additional works at: https://scholar.uwindsor.ca/etd Recommended Citation Cao, Jian Ping, "Characterization of cathepsin L genes and their cDNAs in the brine shrimp, Artemia franciscana." (2006). Electronic Theses and Dissertations. 1398. https://scholar.uwindsor.ca/etd/1398 This online database contains the full-text of PhD dissertations and Masters’ theses of University of Windsor students from 1954 forward. These documents are made available for personal study and research purposes only, in accordance with the Canadian Copyright Act and the Creative Commons license—CC BY-NC-ND (Attribution, Non-Commercial, No Derivative Works). Under this license, works must always be attributed to the copyright holder (original author), cannot be used for any commercial purposes, and may not be altered. Any other use would require the permission of the copyright holder. Students may inquire about withdrawing their dissertation and/or thesis from this database. For additional inquiries, please contact the repository administrator via email ([email protected]) or by telephone at 519-253-3000ext. 3208. CHARACTERIZATION OF CATHEPSIN L GENES AND THEIR cDNAs IN THE BRINE SHRIMP, ARTEMIA FRANCISCANA By: JianPing Cao A Thesis Submitted to the Faculty of Graduate Studies and Research through the Department of Biological Sciences in Partial Fulfillment of the Requirements for the Degree of Master of Science at the University of Windsor Windsor, Ontario, Canada 2006 Reproduced with permission of the copyright owner.
    [Show full text]
  • Proteolytic Enzymes in Grass Pollen and Their Relationship to Allergenic Proteins
    Proteolytic Enzymes in Grass Pollen and their Relationship to Allergenic Proteins By Rohit G. Saldanha A thesis submitted in fulfilment of the requirements for the degree of Masters by Research Faculty of Medicine The University of New South Wales March 2005 TABLE OF CONTENTS TABLE OF CONTENTS 1 LIST OF FIGURES 6 LIST OF TABLES 8 LIST OF TABLES 8 ABBREVIATIONS 8 ACKNOWLEDGEMENTS 11 PUBLISHED WORK FROM THIS THESIS 12 ABSTRACT 13 1. ASTHMA AND SENSITISATION IN ALLERGIC DISEASES 14 1.1 Defining Asthma and its Clinical Presentation 14 1.2 Inflammatory Responses in Asthma 15 1.2.1 The Early Phase Response 15 1.2.2 The Late Phase Reaction 16 1.3 Effects of Airway Inflammation 16 1.3.1 Respiratory Epithelium 16 1.3.2 Airway Remodelling 17 1.4 Classification of Asthma 18 1.4.1 Extrinsic Asthma 19 1.4.2 Intrinsic Asthma 19 1.5 Prevalence of Asthma 20 1.6 Immunological Sensitisation 22 1.7 Antigen Presentation and development of T cell Responses. 22 1.8 Factors Influencing T cell Activation Responses 25 1.8.1 Co-Stimulatory Interactions 25 1.8.2 Cognate Cellular Interactions 26 1.8.3 Soluble Pro-inflammatory Factors 26 1.9 Intracellular Signalling Mechanisms Regulating T cell Differentiation 30 2 POLLEN ALLERGENS AND THEIR RELATIONSHIP TO PROTEOLYTIC ENZYMES 33 1 2.1 The Role of Pollen Allergens in Asthma 33 2.2 Environmental Factors influencing Pollen Exposure 33 2.3 Classification of Pollen Sources 35 2.3.1 Taxonomy of Pollen Sources 35 2.3.2 Cross-Reactivity between different Pollen Allergens 40 2.4 Classification of Pollen Allergens 41 2.4.1
    [Show full text]
  • Developing Methods to Understand and Engineer Protease Cleavage Specificity
    Developing methods to understand and engineer protease cleavage specificity A Dissertation SUBMITTED TO THE FACULTY OF THE UNIVERSITY OF MINNESOTA BY Michael Douglas Lane IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY Burckhard Seelig September 2016 © Michael D Lane, 2016 Acknowledgements I would like to thank the many people who supported me along the way towards completing my thesis. Above all, I thank my advisor, Dr. Burckhard Seelig, who gave me the opportunity to pursue my ideas, embraced my research with thoughtful criticism and relentless optimism, and shaped my scientific approach through challenging me to be the best I can be. I also would like to thank previous members of the Seelig lab, Dr. Misha Golynskiy, Dr. John Haugner, Dr. Dana Morrone, and Dr. Aleardo Morelli, for being good friends and the many scientific discussions we had that guided me through the rough experiments. To the new Seelig lab members, especially Dr. Matilda Newton, Dr. Yari Cabezas, and Dr. Nisha Kanwar, thank you for your critical feedback, friendship, and taking away all my lab responsibilities. To the MSTP, I would like to thank Dr. Yoji Shimizu, Susan Shurson, and Nicholas Berg for their unending help guiding through the woven MD/PhD program. In particular, I thank the MSTP leadership for allowing me to pursue the program tailored to my interests. To my thesis committee, thank you for your support through the years. From annual reviews, to informal discussions, to grant application drafts, your feedback molded my abilities and experience. To my friends and family, especially my wife, Dr.
    [Show full text]
  • "2N Ó - H a A.N () -Si-'-RH "',O '-S'a AO Or Patent Application Publication Jul
    US 2006O154325A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2006/0154325 A1 Bogyo et al. (43) Pub. Date: Jul. 13, 2006 (54) SYNTHESIS OF EPOXIDE BASED Publication Classification INHIBITORS OF CYSTEINE PROTEASES (51) Int. Cl. CI2O I/37 (2006.01) (76) Inventors: Matthew Bogyo, Redwood City, CA C07K 7/08 (2006.01) (US); Steven H.L. Verhelst, Stanford, C07D 303/08 (2006.01) CA (US) (52) U.S. Cl. ............................. 435/23: 530/402; 549/551 Correspondence Address: (57) ABSTRACT PETERS VERNY JONES & SCHMITT, L.L.P. 425 SHERMANAVENUE SUTE 230 Epoxide based cysteine protease inhibitors containing pep PALO ALTO, CA 94.306 (US) tide derivatives and methods for synthesizing them in sold phase are disclosed. Preferably, an epoxy succinyl “war head' (for binding to the enzyme) is prepared, having two (21) Appl. No.: 11/329,818 amino acid residues or residue-like structures on either side. Natural and non-natural amino acids may be used. The present process may be carried out entirely on a solid (22) Filed: Jan. 10, 2006 Support, with the proviso that a dipeptide like group is prepared prior to coupling to one side of the Supported Related U.S. Application Data complex. The method lends itself to more efficient inhibitor synthesis, and may be employed with mixtures of peptide (60) Provisional application No. 60/642,891, filed on Jan. compounds, and various modifications of epoxides to create 10, 2005. diverse libraries of inhibitors. Fmoc-NH-AA-OH 1) 20%diorari Piperdine all- AA A 1 0 2 O N-Fmoc di H 1 AA if m RNK Tentage Resin Step 1 2)) Fmoc-NH-AA-OH2 2 1) 20% Piperdine Step 2 Step 3 2) epoxide-NP ester NaOH (): N AA 1 N o al- S H AA O H O O S1NÓ H A A.
    [Show full text]
  • Epidemiology and Pathogenesis of Moraxella Catarrhalis Colonization
    Chirality: The Key to Specific Bacterial Protease-Based Diagnosis? Wendy E. Kaman ISBN 978-94-6169-451-5 © W.E. Kaman, Rotterdam, 2014 All rights reserved. No part of this thesis may be reproduced or transmitted in any form or by means without prior permission of the author, or where appropriate, the publisher of the articles. The printing of this thesis was financially supported by the Nederlandse Vereniging voor Medische Microbiologie. Layout and printing: Optima Grafische Communicatie Cover design: Suede Design (www.suededesign.nl) Chirality: The Key to Specific Bacterial Protease-Based Diagnosis? Chiraliteit: de sleutel tot bacterie-specifieke protease-gebaseerde diagnostiek? Proefschrift ter verkrijging van de graad van doctor aan de Erasmus Universiteit Rotterdam op gezag van de Rector Magnificus Prof. dr. H.A.P. Pols en volgens besluit van het College voor Promoties De openbare verdediging zal plaats vinden op 24 januari om 9:30 uur door Wendy Esmeralda Kaman geboren te `s-Gravenhage Promotiecommissie Promotor: Prof. dr. H.P. Endtz Overige leden: Prof. dr. E.C.I. Veerman Prof. dr. W. Crielaard Prof. dr. dr. A. van Belkum Co-promotoren: Dr. F.J. Bikker Dr. J.P. Hays It`s all about cleavage! Contents Amino acids 11 Introduction Chapter 1. General introduction, aim and outline of the thesis. 15 Diagnosis Chapter 2. Evaluation of a D-amino-acid-containing fluorescence resonance 39 energy transfer (FRET-) peptide library for profiling prokaryotic proteases. Chapter 3. Highly specific protease-based approach for detection ofPorphy- 59 romonas gingivalis in diagnosis of periodontitis. Chapter 4. Comparing culture, real-time PCR and FRET-technology for de- 81 tection of Porphyromonas gingivalis in patients with or without peri-implant infections.
    [Show full text]
  • Families and Clans of Cysteine Peptidases
    Families and clans of eysteine peptidases Alan J. Barrett* and Neil D. Rawlings Peptidase Laboratory. Department of Immunology, The Babraham Institute, Cambridge CB2 4AT,, UK. Summary The known cysteine peptidases have been classified into 35 sequence families. We argue that these have arisen from at least five separate evolutionary origins, each of which is represented by a set of one or more modern-day families, termed a clan. Clan CA is the largest, containing the papain family, C1, and others with the Cys/His catalytic dyad. Clan CB (His/Cys dyad) contains enzymes from RNA viruses that are distantly related to chymotrypsin. The peptidases of clan CC are also from RNA viruses, but have papain-like Cys/His catalytic sites. Clans CD and CE contain only one family each, those of interleukin-ll3-converting enz3wne and adenovirus L3 proteinase, respectively. A few families cannot yet be assigned to clans. In view of the number of separate origins of enzymes of this type, one should be cautious in generalising about the catalytic mechanisms and other properties of cysteine peptidases as a whole. In contrast, it may be safer to gener- alise for enzymes within a single family or clan. Introduction Peptidases in which the thiol group of a cysteine residue serves as the nucleophile in catalysis are defined as cysteine peptidases. In all the cysteine peptidases discovered so far, the activity depends upon a catalytic dyad, the second member of which is a histidine residue acting as a general base. The majority of cysteine peptidases are endopeptidases, but some act additionally or exclusively as exopeptidases.
    [Show full text]
  • Emerging Evidence in IBD
    International Journal of Molecular Sciences Review Gut Serpinome: Emerging Evidence in IBD Héla Mkaouar 1, Vincent Mariaule 1, Soufien Rhimi 1, Juan Hernandez 2 , Aicha Kriaa 1, Amin Jablaoui 1, Nizar Akermi 1, Emmanuelle Maguin 1 , Adam Lesner 3 , Brice Korkmaz 4 and Moez Rhimi 1,* 1 Microbiota Interaction with Human and Animal Team (MIHA), Micalis Institute, AgroParisTech, Université Paris-Saclay, INRAE, 78350 Jouy-en-Josas, France; [email protected] (H.M.); [email protected] (V.M.); soufi[email protected] (S.R.); [email protected] (A.K.); [email protected] (A.J.); [email protected] (N.A.); [email protected] (E.M.) 2 Department of Clinical Sciences, Nantes-Atlantic College of Veterinary Medicine and Food Sciences (Oniris), University of Nantes, 101 Route de Gachet, 44300 Nantes, France; [email protected] 3 Faculty of Chemistry, University of Gdansk, Uniwersytet Gdanski, Chemistry, Wita Stwosza 63, PL80-308 Gdansk, Poland; [email protected] 4 INSERM UMR-1100, “Research Center for Respiratory Diseases” and University of Tours, 37032 Tours, France; [email protected] * Correspondence: [email protected] Abstract: Inflammatory bowel diseases (IBD) are incurable disorders whose prevalence and global socioeconomic impact are increasing. While the role of host genetics and immunity is well docu- mented, that of gut microbiota dysbiosis is increasingly being studied. However, the molecular basis of the dialogue between the gut microbiota and the host remains poorly understood. Increased activity of serine proteases is demonstrated in IBD patients and may contribute to the onset and the maintenance of the disease.
    [Show full text]
  • Stembook 2018.Pdf
    The use of stems in the selection of International Nonproprietary Names (INN) for pharmaceutical substances FORMER DOCUMENT NUMBER: WHO/PHARM S/NOM 15 WHO/EMP/RHT/TSN/2018.1 © World Health Organization 2018 Some rights reserved. This work is available under the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 IGO licence (CC BY-NC-SA 3.0 IGO; https://creativecommons.org/licenses/by-nc-sa/3.0/igo). Under the terms of this licence, you may copy, redistribute and adapt the work for non-commercial purposes, provided the work is appropriately cited, as indicated below. In any use of this work, there should be no suggestion that WHO endorses any specific organization, products or services. The use of the WHO logo is not permitted. If you adapt the work, then you must license your work under the same or equivalent Creative Commons licence. If you create a translation of this work, you should add the following disclaimer along with the suggested citation: “This translation was not created by the World Health Organization (WHO). WHO is not responsible for the content or accuracy of this translation. The original English edition shall be the binding and authentic edition”. Any mediation relating to disputes arising under the licence shall be conducted in accordance with the mediation rules of the World Intellectual Property Organization. Suggested citation. The use of stems in the selection of International Nonproprietary Names (INN) for pharmaceutical substances. Geneva: World Health Organization; 2018 (WHO/EMP/RHT/TSN/2018.1). Licence: CC BY-NC-SA 3.0 IGO. Cataloguing-in-Publication (CIP) data.
    [Show full text]
  • (INN) for Biological and Biotechnological Substances
    WHO/EMP/RHT/TSN/2019.1 International Nonproprietary Names (INN) for biological and biotechnological substances (a review) 2019 WHO/EMP/RHT/TSN/2019.1 International Nonproprietary Names (INN) for biological and biotechnological substances (a review) 2019 International Nonproprietary Names (INN) Programme Technologies Standards and Norms (TSN) Regulation of Medicines and other Health Technologies (RHT) Essential Medicines and Health Products (EMP) International Nonproprietary Names (INN) for biological and biotechnological substances (a review) FORMER DOCUMENT NUMBER: INN Working Document 05.179 © World Health Organization 2019 All rights reserved. Publications of the World Health Organization are available on the WHO website (www.who.int) or can be purchased from WHO Press, World Health Organization, 20 Avenue Appia, 1211 Geneva 27, Switzerland (tel.: +41 22 791 3264; fax: +41 22 791 4857; e-mail: [email protected]). Requests for permission to reproduce or translate WHO publications –whether for sale or for non-commercial distribution– should be addressed to WHO Press through the WHO website (www.who.int/about/licensing/copyright_form/en/index.html). The designations employed and the presentation of the material in this publication do not imply the expression of any opinion whatsoever on the part of the World Health Organization concerning the legal status of any country, territory, city or area or of its authorities, or concerning the delimitation of its frontiers or boundaries. Dotted and dashed lines on maps represent approximate border lines for which there may not yet be full agreement. The mention of specific companies or of certain manufacturers’ products does not imply that they are endorsed or recommended by the World Health Organization in preference to others of a similar nature that are not mentioned.
    [Show full text]
  • Ides and Speb
    Studies on secreted cysteine proteases of Streptococcus pyogenes - IdeS and SpeB Reine Vindebro Department of Molecular Biology Umeå University Umeå 2014 Responsible publisher under swedish law: the Dean of the Medical Faculty This work is protected by the Swedish Copyright Legislation (Act 1960:729) ISBN: 978-91-7601-048-8 ISSN: 0346-6612 New series nr: 1646 Electronic version available at http://umu.diva-portal.org/ Printed by: KBC printing service (Umeå University) Umeå, Sweden 2014 To Sofia and Rasmus. i ii Table of Contents Abstract iv List of Publications and Manuscripts v Abbreviations vi 1 Introduction 1 1.1 Streptococcus pyogenes 1 1.1.1 Virulence factors 2 1.2 Proteases in general 3 1.3 Immunoglobulin G (IgG) 3 1.4 IdeS 5 1.4.1 Discovery 5 1.4.2 Protein properties and structure 6 1.4.3 Substrate specificity and binding site on IgG 7 1.4.4 Enzymatic constants 9 1.4.5 Effect of IgG cleavage 10 1.4.6 IdeS as a dimer 11 1.4.7 Allelic Variation 12 1.4.8 Other functions of IdeS 13 1.4.9 Prevalence of IdeS in S. pyogenes strains 14 1.4.10 Regulatory control 14 1.4.11 Importance as a virulence factor 15 1.4.12 Homologues in other bacterial species 16 1.4.13 Therapeutic potential 17 1.4.14 Use as a laboratory tool 17 1.5 SpeB 18 1.5.1 Discovery 18 1.5.2 Regulatory control 18 1.5.3 Structure of SpeB and the potential dimer 18 1.5.4 Functions of, and substrates for, SpeB 19 1.5.5 IgG as a substrate for SpeB 20 1.5.6 SpeB is, or is not, an important virulence factor 21 1.6 IdeS and SpeB as virulence factors 22 2 Methods 24 2.1 General methods 24 2.2 Detecting degradation of IgG by IdeS 25 3 Results and discussion 28 3.1 Paper I 28 3.2 Paper II 30 3.3 Paper III 31 3.4 Paper IV 33 3.5 Paper V 34 Conclusions 36 Acknowledgements 37 References 38 iii Abstract The pathogen Streptococcus pyogenes is a significant cause of human morbidity and mortality.
    [Show full text]
  • Molecular Mechanisms of Streptococcus Pyogenes Tissue Colonization and Invasion Antonin Weckel
    Molecular mechanisms of Streptococcus pyogenes tissue colonization and invasion Antonin Weckel To cite this version: Antonin Weckel. Molecular mechanisms of Streptococcus pyogenes tissue colonization and invasion. Microbiology and Parasitology. Université Sorbonne Paris Cité, 2018. English. NNT : 2018US- PCB097. tel-02984777 HAL Id: tel-02984777 https://tel.archives-ouvertes.fr/tel-02984777 Submitted on 1 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Université Paris Descartes Ecole doctorale BioSPC Institut Cochin INSERM U1016 / Equipe Barrières et Pathogènes Molecular mechanisms of Streptococcus pyogenes tissue colonization and invasion By Antonin WECKEL PhD Thesis in Microbiology Directed by Agnès Fouet Thesis defense: 30th of October 2018 Jury members: Pr Anna NORRBY-TEGLUND Reviewer Dr Pascale SERROR Reviewer Pr François VANDENESCH Examiner Dr Philippe BOUSSO Examiner Dr Agnès FOUET PhD supervisor “We have to remember that what we observe is not nature herself, but nature exposed to our method of questioning” Werner Heisenberg Physics and Philosophy: The Revolution in Modern Science (1958) Acknowledgements I would like to thank Pascale Serror, Anna Norrby-Teglund, François Vandenesch and Philippe Bousso for having kindly accepted to be part of my defense jury, in particular to Anna Norrby- Teglund who came from Sweden for my defense.
    [Show full text]