Calreticulin—Multifunctional Chaperone in Immunogenic Cell Death: Potential Significance As a Prognostic Biomarker in Ovarian
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Calreticulin Controlling the Membrane Translocation of Immunogenicity Of
ERP57 Membrane Translocation Dictates the Immunogenicity of Tumor Cell Death by Controlling the Membrane Translocation of Calreticulin This information is current as of September 25, 2021. Michel Obeid J Immunol 2008; 181:2533-2543; ; doi: 10.4049/jimmunol.181.4.2533 http://www.jimmunol.org/content/181/4/2533 Downloaded from References This article cites 26 articles, 11 of which you can access for free at: http://www.jimmunol.org/content/181/4/2533.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 25, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2008 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology ERP57 Membrane Translocation Dictates the Immunogenicity of Tumor Cell Death by Controlling the Membrane Translocation of Calreticulin1 Michel Obeid2 Several pieces of experimental evidence indicate the following: 1) the most efficient antitumor treatments (this principle applies on both chemotherapy and radiotherapy) are those that induce immunogenic cell death and are able to trigger a specific antitumor immune response; and 2) the immunogenicity of cell death depends very closely on the plasma membrane quantity of calreticulin (CRT), an endoplasmic reticulum (ER) stress protein exposed to the cell membrane after immunogenic treatment. -
The Impact of Endogenous Annexin A1 on Glucocorticoid Control of Infl Ammatory Arthritis
Basic and translational research Ann Rheum Dis: first published as 10.1136/annrheumdis-2011-201180 on 5 May 2012. Downloaded from EXTENDED REPORT The impact of endogenous annexin A1 on glucocorticoid control of inß ammatory arthritis Hetal B Patel,1 Kristin N Kornerup,1 AndreÕ LF Sampaio,1 Fulvio DÕAcquisto,1 Michael P Seed,1 Ana Paula Girol,2 Mohini Gray,3 Costantino Pitzalis,1 Sonia M Oliani,2 Mauro Perretti1 ▶ Additional (Þ gures and tables) ABSTRACT Annexin A1 (AnxA1) is an effector of resolution.4 are published online only. To view Objectives To establish the role and effect of Highly expressed in immune cells (eg, polymorpho- these Þ les please visit the journal nuclear cells and macrophages), this protein is exter- online (http://ard.bmj.com/ glucocorticoids and the endogenous annexin A1 (AnxA1) content/early/recent). pathway in inß ammatory arthritis. nalised to exert paracrine and juxtacrine effects, the vast majority of which are mediated by the formyl- 1William Harvey Research Methods Ankle joint mRNA and protein expression Institute, Barts and The London of AnxA1 and its receptors were analysed in peptide receptor type 2 (FPR2/ALX ([Lipoxin A4 School of Medicine, London UK naive and arthritic mice by real-time PCR and receptor]) or FPR2, in rodents).5 Intriguingly, FPR2/ 2Department of Biology; 6 immunohistochemistry. Inß ammatory arthritis was ALX is also the lipoxin A4 receptor indicating the Instituto de Bioci•ncias, Letras +/+ existence of important – yet not fully appreci- e Ci•ncias Exatas (IBILCE), S‹o induced with the K/BxN arthritogenic serum in AnxA1 −/− ated – networks in resolution.7 Paulo State University, S‹o JosŽ and AnxA1 mice; in some experiments, animals Another receptor do Rio Preto, Brazil were treated with dexamethasone (Dex) or with human is also advocated to mediate the effects of AnxA1, 3Medical Research Council recombinant AnxA1 or a protease-resistant mutant the formyl-peptide receptor type 1 or FPR1 (FPR1 Centre for Inß ammation, (termed SuperAnxA1). -
Profiling of Transcripts and Proteins Modulated by the E7 Oncogene in the Lung Tissue of E7-Tg Mice by the Omics Approach
MOLECULAR MEDICINE REPORTS 2: 129-137, 2009 129 Profiling of transcripts and proteins modulated by the E7 oncogene in the lung tissue of E7-Tg mice by the omics approach EUNJIN KIM1*, JEONGWOO KANG1,3*, MINCHUL CHO1, SOJUNG LEE1, EUNHEE SEO1, HEESOOK CHOI1, YUMI KIM1, JUNGHEE KIM1, KUM YONG KANG2, KWANG PYO KIM2, JAEYONG HAN3, YHUNYHONG SHEEN4, YOUNG NA YUM5, SUE-NIE PARK5 and DO-YOUNG YOON1 Departments of 1Bioscience and Biotechnology, and 2Molecular Biotechnology, Konkuk University, Hwayang-dong 1, Gwangjin-gu, Seoul 143-701; 3Laboratory of Animal Genetic Engineering, Department of Food and Animal Biotechnology, Seoul National University, Seoul 151-742; 4School of Pharmacy, Ewha Womans University, Seoul 120-750; 5Korea Food and Drug Administration, #194 Tongil-ro, Eunpyung-gu, Seoul 122-704, Korea Received August 18, 2008; Accepted November 10, 2008 DOI: 10.3892/mmr_00000073 Abstract. The E6 and E7 oncoproteins of human papilloma suggest that the E7 oncogene modulates the expression levels virus (HPV) type 16 have been known to cooperatively induce of cell cycle-related (cyclin B1, cyclin E2) and cell adhesion- the immortalization and transformation of primary keratino- and migration-related (actinin ·1, CD166) factors, which may cytes. We established an E7 transgenic mouse model to play important roles in cellular transformation in cancer. In screen HPV-related biomakers using the omics approach. addition, the solubilization of the rigid intermediate filament The methods used to identify HPV-modulated factors were network by specific proteolysis mediated via up-regulating genomics analysis by microarray using the Affymetrix 430 gelsolin and down-regulating cofilin-1, as well as increased 2.0 array to screen E7-modulated genes, and proteomics levels of endoplasmic reticulum protein calnexin with chap- analysis using nano-LC-ESI-MS/MS to screen E7-modulated erone functions, might also be involved in E7-lung epithelial proteins with the lung tissue of E7 transgenic mice. -
Annexin A1 Expression Is Associated with Epithelial–Mesenchymal Transition (EMT), Cell Proliferation, Prognosis, and Drug Response in Pancreatic Cancer
cells Article Annexin A1 Expression Is Associated with Epithelial–Mesenchymal Transition (EMT), Cell Proliferation, Prognosis, and Drug Response in Pancreatic Cancer Masanori Oshi 1,2 , Yoshihisa Tokumaru 1,3 , Swagoto Mukhopadhyay 1, Li Yan 4, Ryusei Matsuyama 2, Itaru Endo 2 and Kazuaki Takabe 1,2,5,6,7,8,* 1 Department of Surgical Oncology, Roswell Park Comprehensive Cancer Center, Buffalo, NY 14263, USA; [email protected] (M.O.); [email protected] (Y.T.); [email protected] (S.M.) 2 Department of Gastroenterological Surgery, Yokohama City University School of Medicine, Yokohama, Kanagawa 236-0004, Japan; [email protected] (R.M.); [email protected] (I.E.) 3 Department of Surgical Oncology, Graduate School of Medicine, Gifu University, 1-1 Yanagido, Gifu 501-1194, Japan 4 Department of Biostatistics & Bioinformatics, Roswell Park Comprehensive Cancer Center, Buffalo, NY 14263, USA; [email protected] 5 Department of Gastrointestinal Tract Surgery, Fukushima Medical University School of Medicine, Fukushima 960-1295, Japan 6 Department of Surgery, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo the State University of New York, Buffalo, NY 14263, USA 7 Department of Surgery, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8510, Japan Citation: Oshi, M.; Tokumaru, Y.; 8 Department of Breast Surgery and Oncology, Tokyo Medical University, Tokyo 160-8402, Japan Mukhopadhyay, S.; Yan, L.; * Correspondence: [email protected]; Tel.: +1-716-8-455-540; Fax: +1-716-8-451-668 Matsuyama, R.; Endo, I.; Takabe, K. Annexin A1 Expression Is Associated Abstract: Annexin A1 (ANXA1) is a calcium-dependent phospholipid-binding protein overexpressed with Epithelial–Mesenchymal in pancreatic cancer (PC). -
The Atf6β-Calreticulin Axis Promotes Neuronal Survival Under Endoplasmic Reticulum Stress and Excitotoxicity
bioRxiv preprint doi: https://doi.org/10.1101/2021.02.01.429116; this version posted February 2, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 1 The ATF6β-calreticulin axis promotes neuronal survival under 2 endoplasmic reticulum stress and excitotoxicity 3 4 Dinh Thi Nguyen1, Thuong Manh Le1, Tsuyoshi Hattori1, Mika Takarada-Iemata1, 5 Hiroshi Ishii1, Jureepon Roboon1, Takashi Tamatani1, Takayuki Kannon2, 6 Kazuyoshi Hosomichi2, Atsushi Tajima2, Shusuke Taniuchi3, Masato Miyake3, Seiichi 7 Oyadomari3, Shunsuke Saito4, Kazutoshi Mori4, Osamu Hori1* 8 9 10 1.Department of Neuroanatomy, Graduate School of Medical Sciences, Kanazawa 11 University, Kanazawa, Japan 12 2.Department of Bioinformatics and Genomics, Graduate School of Advanced Preventive 13 Medical Sciences, Kanazawa University, Kanazawa, Japan 14 3.Division of Molecular Biology, Institute for Genome Research, Institute of Advanced 15 Medical Sciences, Tokushima University, Tokushima, Japan 16 4.Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan 17 18 19 Running title: Neuroprotective role of the ATF6β-calreticulin axis 20 21 22 23 24 25 26 * Corresponding author: 27 Dr. Osamu Hori 28 Department of Neuroanatomy, Kanazawa University Graduate School of Medical 29 Sciences, 30 13-1 Takara-Machi, Kanazawa City, 31 Ishikawa 920-8640, Japan 32 Tel: +81-76-265-2162 33 Fax: +81-76-234-4222 34 E-mail: [email protected] 35 36 37 38 39 Key words: neurodegeneration, Ca2+ homeostasis, ER stress 40 bioRxiv preprint doi: https://doi.org/10.1101/2021.02.01.429116; this version posted February 2, 2021. -
Comparative Analysis of a Teleost Skeleton Transcriptome Provides Insight Into Its Regulation
Accepted Manuscript Comparative analysis of a teleost skeleton transcriptome provides insight into its regulation Florbela A. Vieira, M.A.S. Thorne, K. Stueber, M. Darias, R. Reinhardt, M.S. Clark, E. Gisbert, D.M. Power PII: S0016-6480(13)00264-5 DOI: http://dx.doi.org/10.1016/j.ygcen.2013.05.025 Reference: YGCEN 11541 To appear in: General and Comparative Endocrinology Please cite this article as: Vieira, F.A., Thorne, M.A.S., Stueber, K., Darias, M., Reinhardt, R., Clark, M.S., Gisbert, E., Power, D.M., Comparative analysis of a teleost skeleton transcriptome provides insight into its regulation, General and Comparative Endocrinology (2013), doi: http://dx.doi.org/10.1016/j.ygcen.2013.05.025 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. 1 Comparative analysis of a teleost skeleton transcriptome 2 provides insight into its regulation 3 4 Florbela A. Vieira1§, M. A. S. Thorne2, K. Stueber3, M. Darias4,5, R. Reinhardt3, M. 5 S. Clark2, E. Gisbert4 and D. M. Power1 6 7 1Center of Marine Sciences, Universidade do Algarve, Faro, Portugal. 8 2British Antarctic Survey – Natural Environment Research Council, High Cross, 9 Madingley Road, Cambridge, CB3 0ET, UK. -
Intracellular Ca2&Plus
Cell Death and Differentiation (2009) 16, 1126–1134 & 2009 Macmillan Publishers Limited All rights reserved 1350-9047/09 $32.00 www.nature.com/cdd Intracellular Ca2 þ operates a switch between repair and lysis of streptolysin O-perforated cells EB Babiychuk*,1, K Monastyrskaya1, S Potez1 and A Draeger1 Pore-forming (poly)peptides originating from invading pathogens cause plasma membrane damage in target cells, with consequences as diverse as proliferation or cell death. However, the factors that define the outcome remain unknown. We show 2 þ 2 þ that in cells maintaining an intracellular Ca concentration [Ca ]i below a critical threshold of 10 lM, repair mechanisms seal 2 þ 2 þ off ‘hot spots’ of Ca entry and shed them in the form of microparticles, leading to [Ca ]i reduction and cell recovery. Cells 2 þ that are capable of preventing an elevation of [Ca ]i above the critical concentration, yet are unable to complete plasma 2 þ membrane repair, enter a prolonged phase of [Ca ]i oscillations, accompanied by a continuous shedding of microparticles. 2 þ When [Ca ]i exceeds the critical concentration, an irreversible formation of ceramide platforms within the plasma membrane 2 þ and their internalisation drives the dying cells beyond the ‘point of no return’. These findings show that the extent of [Ca ]i elevation determines the fate of targeted cells and establishes how different Ca2 þ -dependent mechanisms facilitate either cell survival or death. Cell Death and Differentiation (2009) 16, 1126–1134; doi:10.1038/cdd.2009.30; published online 27 March 2009 Plasma membrane pores formed by cytotoxic proteins modulators, which, in turn, amplify an ongoing inflammatory and peptides disrupt the permeability barrier in a target response.3,11 The authors further hypothesised that a more 2 þ cell. -
Immunopharmacology
Institute of Pharmacology http://www.pki.unibe.ch/ PKI Immunopharmacology Prof. Dr. Stephan von Gunten MD PhD MME Lectures: Clinical Immunology Immunomodulation Endogenous or exogenous molecules that influence immune responses positively (immunostimulation) or negatively (immunoregulation) DC Based Vaccination Freund complete adjuvans (FCA) Freund incomplete adjuvans (FIA) (mycobacteria + mineral oils) (mineral oils, without mycobacteria) differential maturation alum (hydrated alumina) dendritic cell (DC) mycobacteria Toll-like Receptors alum, mineral NLR-Inflammasome oils in FCA/FIA Toll-Like Receptors PAMPs 2 major adapters: MyD88 and TRIF protein kinases transcription factor (NFkB, IRF-3/-7) [IRF: Interferon regulatory factor] gene transcription: inflammatory cytokines, IFNa/b, others BMSc Pharma Immuno Manicassamy S & Pulendran B, Seminars in Immunology 2009 (modified) TLR Agonists and Cancer Immunotherapy: BCG-CWS BCG: Bacillus Calmette-Guérin, attenuated form of Mycobacterium bovis CWS (cell-wall skeleton ): major adjuvant–active part of mycobacterial cells; contains muramyldipeptide (MDP) -> activation of TLR-2 and -4 and NOD2 BCG-CWS TLR-2 MyD88-pathway mDC cytokines CTL tumour cell killing Carbohydrate-based vaccines in development Infectious disease Infectious Cancer Astronomo RD & Burton DR Nat Rev Drug Discov 2016 (modified) Antibody repertoire: glycan immunogenicity linked to structure Schneider et al. Sci Transl Med 2015 Cancer Immunotherapy Galluzi L et al. Oncotarget 2014 Siglec expression on immune cells Jandus C et al. Biochem Pharmacol 2011 Illustration by Aldona von Gunten The sialoglycan shield Jandus C & Boligan KF et al. J Clin Invest. 2014 Siglecs on CD8 T cells? May 2019 Cover Story American Association of Cancer Research (AACR) Immunomodulation Endogenous or exogenous molecules that influence immune responses positively (immunostimulation) or negatively (immunoregulation) Antiinflammatory vs. -
A Selective ER-Phagy Exerts Procollagen Quality Control Via a Calnexin-FAM134B Complex
Article A selective ER-phagy exerts procollagen quality control via a Calnexin-FAM134B complex Alison Forrester1,†, Chiara De Leonibus1,†, Paolo Grumati2,†, Elisa Fasana3,†, Marilina Piemontese1, Leopoldo Staiano1, Ilaria Fregno3,4, Andrea Raimondi5, Alessandro Marazza3,6, Gemma Bruno1, Maria Iavazzo1, Daniela Intartaglia1, Marta Seczynska2, Eelco van Anken7, Ivan Conte1, Maria Antonietta De Matteis1,8, Ivan Dikic2,9,* , Maurizio Molinari3,10,** & Carmine Settembre1,11,*** Abstract The EMBO Journal (2019) 38:e99847 Autophagy is a cytosolic quality control process that recognizes substrates through receptor-mediated mechanisms. Procollagens, Introduction the most abundant gene products in Metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain Macroautophagy (hereafter referred to as autophagy) is a homeostatic the native structure is cleared by autophagy. However, how auto- catabolic process devoted to the sequestration of cytoplasmic material phagy selectively recognizes misfolded procollagens in the ER in double-membrane vesicles (autophagic vesicles, AVs) that eventu- lumen is still unknown. We performed siRNA interference, CRISPR- ally fuse with lysosomes where cargo is degraded (Mizushima, 2011). Cas9 or knockout-mediated gene deletion of candidate autophagy Autophagy is essential to maintain tissue homeostasis and counter- and ER proteins in collagen producing cells. We found that the ER- acts both the onset and progression of many disease conditions, such resident lectin chaperone Calnexin (CANX) and the ER-phagy as ageing, neurodegeneration and cancer (Levine et al, 2015). receptor FAM134B are required for autophagy-mediated quality Substrates can be selectively delivered to AVs through receptor- control of endogenous procollagens. Mechanistically, CANX acts as mediated processes. Autophagy receptors harbour a LC3 or GABARAP co-receptor that recognizes ER luminal misfolded procollagens and interaction motif (LIR or GIM, respectively) that facilitate binding of interacts with the ER-phagy receptor FAM134B. -
Annexin A1 Is a New Functional Linker Between Actin Filaments and Phagosomes During Phagocytosis
578 Research Article Annexin A1 is a new functional linker between actin filaments and phagosomes during phagocytosis Devang M. Patel1, Syed Furquan Ahmad1, Dieter G. Weiss1, Volker Gerke2 and Sergei A. Kuznetsov1,* 1Institute of Biological Sciences, Cell Biology and Biosystems Technology, University of Rostock, Albert-Einstein Straße 3, Rostock 18059, Germany 2Institute of Medical Biochemistry, Centre for Molecular Biology of Inflammation, University of Münster, Von-Esmarch-Straße 56, Münster 48149, Germany *Author for correspondence ([email protected]) Accepted 19 October 2010 Journal of Cell Science 124, 578-588 © 2011. Published by The Company of Biologists Ltd doi:10.1242/jcs.076208 Summary Remodelling of the actin cytoskeleton plays a key role in particle internalisation and the phagosome maturation processes. Actin- binding proteins (ABPs) are the main players in actin remodelling but the precise role of these proteins in phagocytosis needs to be clarified. Annexins, a group of ABPs, are known to be present on phagosomes. Here, we identified annexin A1 as a factor that binds to isolated latex bead phagosomes (LBPs) in the presence of Ca2+ and facilitates the F-actin–LBP interaction in vitro. In macrophages the association of endogenous annexin A1 with LBP membranes was strongly correlated with the spatial and temporal accumulation of F-actin at the LBP. Annexin A1 was found on phagocytic cups and around early phagosomes, where the F-actin was prominently concentrated. After uptake was completed, annexin A1, along with F-actin, dissociated from the nascent LBP surface. At later stages of phagocytosis annexin A1 transiently concentrated only around those LBPs that showed transient F-actin accumulation (‘actin flashing’). -
The Immunophilins, Fk506 Binding Protein and Cyclophilin, Are Discretely Localized in the Brain: Relationship to Calcineurin
NeuroscienceVol. 62,NO. 2, pp. 569-580,1994 Elsevier Sctence Ltd Copyright 0 1994 IBRO Pergamon 0306-4522(94)E0182-4 Printed in Great Britain. All rights reserved 0306-4522194 $7.00 + 0.00 THE IMMUNOPHILINS, FK506 BINDING PROTEIN AND CYCLOPHILIN, ARE DISCRETELY LOCALIZED IN THE BRAIN: RELATIONSHIP TO CALCINEURIN T. M. DAWSON,*t J. P. STEINER,* W. E. LYONS,*11 M. FOTUHI,* M. BLUE? and S. H. SNYDER*f§l Departments of *Neuroscience, tNeurology, $Pharmacology and Molecular Sciences, and §Psychiatry, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, U.S.A. (IDivision of Toxicological Science, Johns Hopkins University School of Hygiene and Public Health Abstract-The immunosuppressant drugs cyclosporin A and FK506 bind to small, predominantly soluble proteins cyclophilin and FK506 binding protein, respectively, to mediate their pharmacological actions. The immunosuppressant actions of these drugs occur through binding of cyclophilin-cyclosporinA and FK506 binding protein-FK506 complexes to the calcium-calmodulin-dependent protein phosphatase, calcineurin, inhibiting phosphatase activity, Utilizing immunohistcchemistry, in situ hybridization and autoradiography, we have localized protein and messenger RNA for FKS06 binding protein, cyclophilin and calcineurin. All three proteins and/or messages exhibit a heterogenous distribution through the brain and spinal cord, with the majority of the localizations being neuronal. We observe a striking co-localiz- ation of FK506 binding protein and calcineurin in most -
Detection of Pro Angiogenic and Inflammatory Biomarkers in Patients With
www.nature.com/scientificreports OPEN Detection of pro angiogenic and infammatory biomarkers in patients with CKD Diana Jalal1,2,3*, Bridget Sanford4, Brandon Renner5, Patrick Ten Eyck6, Jennifer Laskowski5, James Cooper5, Mingyao Sun1, Yousef Zakharia7, Douglas Spitz7,9, Ayotunde Dokun8, Massimo Attanasio1, Kenneth Jones10 & Joshua M. Thurman5 Cardiovascular disease (CVD) is the most common cause of death in patients with native and post-transplant chronic kidney disease (CKD). To identify new biomarkers of vascular injury and infammation, we analyzed the proteome of plasma and circulating extracellular vesicles (EVs) in native and post-transplant CKD patients utilizing an aptamer-based assay. Proteins of angiogenesis were signifcantly higher in native and post-transplant CKD patients versus healthy controls. Ingenuity pathway analysis (IPA) indicated Ephrin receptor signaling, serine biosynthesis, and transforming growth factor-β as the top pathways activated in both CKD groups. Pro-infammatory proteins were signifcantly higher only in the EVs of native CKD patients. IPA indicated acute phase response signaling, insulin-like growth factor-1, tumor necrosis factor-α, and interleukin-6 pathway activation. These data indicate that pathways of angiogenesis and infammation are activated in CKD patients’ plasma and EVs, respectively. The pathways common in both native and post-transplant CKD may signal similar mechanisms of CVD. Approximately one in 10 individuals has chronic kidney disease (CKD) rendering CKD one of the most common diseases worldwide1. CKD is associated with a high burden of morbidity in the form of end stage kidney disease (ESKD) requiring dialysis or transplantation 2. Furthermore, patients with CKD are at signifcantly increased risk of death from cardiovascular disease (CVD)3,4.