MIF Family Cytokines in Innate Immunity and Homeostasis PDF
Preview MIF Family Cytokines in Innate Immunity and Homeostasis
Progress in Infl ammation Research Series Editors: Michael J. Parnham · Achim Schmidtko Richard Bucala Jürgen Bernhagen Editors MIF Family Cytokines in Innate Immunity and Homeostasis Progress in Inflammation Research Series Editors Michael J. Parnham Fraunhofer IME & Goethe University Frankfurt, Germany Achim Schmidtko Goethe University Frankfurt, Germany More information about this series at http://www.springer.com/series/4983 Richard Bucala • Jürgen Bernhagen Editors MIF Family Cytokines in Innate Immunity and Homeostasis Editors Richard Bucala Jürgen Bernhagen The Anlyan Center Department of Vascular Biology Yale School of Medicine Institute for Stroke and Dementia Research Yale University Ludwig-Maximilians-University (LMU) New Haven, CT Munich USA Germany Series Editors Michael J. Parnham Achim Schmidtko Fraunhofer IME & Goethe University Goethe University Frankfurt Frankfurt Germany Germany Progress in Inflammation Research ISBN 978-3-319-52352-1 ISBN 978-3-319-52354-5 (eBook) DOI 10.1007/978-3-319-52354-5 Library of Congress Control Number: 2017943027 © Springer International Publishing AG 2017 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. Printed on acid-free paper This Springer imprint is published by Springer Nature The registered company is Springer International Publishing AG The registered company address is: Gewerbestrasse 11, 6330 Cham, Switzerland The Editors, Profs. Bucala and Bernhagen, dedicate this volume to their spouses, Anne and Aphrodite, with thanks for their long- standing support to their scientific work on MIF. Contents MIF- and CD74-Dependent Mechanisms ........................... 1 Shirly Becker-Herman, Naama Gil, Lihi Radomir, and Idit Shachar HSP90-Stabilized MIF in Oncogenesis and Cell Growth Control ....... 21 Ramona Schulz-Heddergott and Ute M. Moll CD74, MIF and Breast Tumorigenesis: Insights from Recent Large-Scale Tumour Genomics and Proteomics Studies ............... 43 Metodi V. Metodiev MIF-Dependent Regulation of Monocyte/Macrophage Polarization ..... 59 Kavitha Yaddanapudi and Robert A. Mitchell Advances in Understanding the Role of MIF in the Pathogenesis of Autoimmune Diseases ......................................... 77 Saisha A. Nalawade, Yousef Al-Abed, and Thomas G. Forsthuber Role of MIF in Experimental Autoimmune Encephalomyelitis and Multiple Sclerosis ........................................... 97 Gil Benedek, Roberto Meza-Romero, and Arthur A. Vandenbark Role of MIF in Hepatic Inflammatory Diseases and Fibrosis ........... 109 Veronica Marin, Gemma Odena, Kyle Poulsen, Claudio Tiribelli, Stefano Bellentani, Andrea Barchetti, Pau Sancho Bru, Natalia Rosso, Ramon Bataller, and Laura E. Nagy MIF and Pulmonary Disease ..................................... 135 Timothy Baker, Patty J. Lee, and Maor Sauler MIF Mediates Pelvic Inflammation and Pain ....................... 145 Fei Ma, Katherine L. Meyer-Siegler, Karin N. Westlund, and Pedro L. Vera MIF Family Proteins in Cardiac Ischemia/Reperfusion Injury ......... 157 Christian Stoppe and Jürgen Bernhagen viii Contents The MIF-CD74 Inflammatory Axis in Alphaviral Infection ............ 175 Lara J. Herrero, Ali Zaid, Margit Mutso, and Suresh Mahalingam MIF in Eosinophilic Inflammation ................................ 189 Marcelo T. Bozza, Claudia N. Paiva, and Priscilla C. Olsen The Role of MIF in Parasitic Infections ............................ 203 Cesar Terrazas, James C. Stock, Jeniffer Kimble, Ellen Moretti, Sanjay Varikuti, and Abhay R. Satoskar Parasite MIF Orthologs ......................................... 221 Thomas Holowka and Richard Bucala Index ......................................................... 241 MIF- and CD74-Dependent Mechanisms Shirly Becker-Herman, Naama Gil, Lihi Radomir, and Idit Shachar Abstract CD74 is a type II cell surface protein that was previously shown to play a role in antigen presentation and as a receptor for the cytokine macrophage migra- tion inhibitory factor (MIF). Studies from recent years demonstrate an important role for CD74 in maintenance of innate and adaptive immune cells. This chapter discusses the MIF/CD74-dependent role in regulating cell survival, metabolism, adhesion, and response to hypoxia in health and disease. 1 CD74 The CD74 gene is located on human chromosome 5 (q32), and was first identified in 1979 by Jones et al. [1]. However, it was not until 1989 that CD74 was shown to have a role in antigen presentation [2]. CD74 is a non-polymorphic type II integral membrane protein (thus also called invariant chain), which exists in different iso- forms defined by its primary amino acid sequence. There are four isoforms of CD74 in humans: p33, p35, p41, and p43. CD74 p33 and p41 are distinguished by alternative splicing of the CD74 transcript, where the p41 isoform contains an extra exon (exon 6b). These two isoforms yield two additional protein products due to an N-terminal cytoplasmic extension of 16 residues, which results from an alternative translation initiation site. The major human p33 isoform has an N-terminal cytosolic tail of 30 amino acids, a transmembrane (TM) domain consisting of amino acid 31–56, and a C-terminal 160 residue luminal domain [3]. This chapter discusses MIF’s receptor CD74 and their central position in linking innate and adaptive immune response in health and disease. S. Becker-Herman • N. Gil • L. Radomir • I. Shachar, Ph.D. (*) Department of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel e-mail: [email protected] © Springer International Publishing AG 2017 1 R. Bucala, J. Bernhagen (eds.), MIF Family Cytokines in Innate Immunity and Homeostasis, Progress in Inflammation Research, DOI 10.1007/978-3-319-52354-5_1 2 S. Becker-Herman et al. The murine CD74 gene encodes two polypeptide chains, one of relative molecu- lar mass of 31 kD (p31) and another less abundant 41 kD (p41) species [4, 5]. Exon 6b is alternatively spliced into the mRNA coding for the p41 isoform [6]. 2 CD74 Function Two main functions were described for CD74: 1. An MHC class II chaperone 2. Cell surface receptor for MIF 2.1 MHCII Chaperone MHC class II molecules are heterodimeric complexes that present foreign antigenic peptides on the cell surface of antigen-presenting cells (APCs) to CD4+ T cells [7–9]. MHC class II synthesis and assembly begins in the endoplasmic reticulum (ER) with the non-covalent association of the MHC α and β chains with trimers of CD74. Three MHC class II αß dimers bind sequentially to a trimer of CD74 to form a nona- meric complex (αßCD74)3, which then exits the ER [10]. After being transported to the trans-Golgi, the αßCD74 complex is diverted from the secretory pathway to the endocytic system and ultimately to acidic endosome/lysosome-like structures called MHC class II compartments (MIIC or CIIV) or to the cell surface. Cell surface CD74 is modified by the addition of chondroitin sulfate (CD74-CS) at amino acid position 201, and this form of CD74 is associated with MHC class II on the surface of antigen- presenting cells [11–13]. Surface expression of newly synthesized CD74 followed by its rapid internalization to the endosomal pathway has also been known for many years. Experiments investigating cell surface CD74 are complicated by the fact that CD74 on the cell surface is characterized by a very rapid turnover [14–16]. The N-terminal cytoplasmic tail of CD74 contains two extensively characterized dileucine-based endosomal targeting motifs [17–19]. These motifs mediate its inter- nalization from the plasma membrane and from the trans Golgi network. In the endocytic compartments, CD74 is gradually proteolytically processed, leaving only a small fragment, the class II-associated Ii chain peptide (CLIP), bound to the released αß dimers. The final step for MHC class II expression requires interaction of αßCLIP complexes with another class II-related αß dimer, called HLA-DM in the human system, and H2-M in mice. Binding of this molecule drives out the residual CLIP, rendering the αß dimers ultimately competent to bind antigenic peptides, which are mainly derived from internalized antigens and are also delivered to the endocytic pathway [20, 21]. The peptide-loaded class II molecules then leave this compartment, by an unknown route, to be expressed on the cell surface and surveyed by CD4+ T cells. Thus, CD74 was thought to function mainly as MHC class II chaperone, which promotes ER exit of MHC class II molecules, directs them to
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