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Ubiquitination, Ubiquitin-Like Modifiers, and Deubiquitination in Viral Infection
Ubiquitination, Ubiquitin-like Modifiers, and Deubiquitination in Viral Infection The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Isaacson, Marisa K., and Hidde L. Ploegh. “Ubiquitination, Ubiquitin- like Modifiers, and Deubiquitination in Viral Infection.” Cell Host & Microbe 5, no. 6 (June 2009): 559-570. Copyright © 2009 Elsevier Inc. As Published http://dx.doi.org/10.1016/j.chom.2009.05.012 Publisher Elsevier Version Final published version Citable link http://hdl.handle.net/1721.1/84989 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. Cell Host & Microbe Review Ubiquitination, Ubiquitin-like Modifiers, and Deubiquitination in Viral Infection Marisa K. Isaacson1 and Hidde L. Ploegh1,* 1Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA *Correspondence: [email protected] DOI 10.1016/j.chom.2009.05.012 Ubiquitin is important for nearly every aspect of cellular physiology. All viruses rely extensively on host machinery for replication; therefore, it is not surprising that viruses connect to the ubiquitin pathway at many levels. Viral involvement with ubiquitin occurs either adventitiously because of the unavoidable usur- pation of cellular processes, or for some specific purpose selected for by the virus to enhance viral replica- tion. Here, we review current knowledge of how the ubiquitin pathway alters viral replication and how viruses influence the ubiquitin pathway to enhance their own replication. Introduction own ubiquitin ligases or ubiquitin-specific proteases, it seems Ubiquitin is a small 76 amino acid protein widely expressed in reasonable to infer functional relevance, but even in these cases, eukaryotic cells. -
The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections
toxins Review The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections Patience Shumba 1, Srikanth Mairpady Shambat 2 and Nikolai Siemens 1,* 1 Center for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, University of Greifswald, D-17489 Greifswald, Germany; [email protected] 2 Division of Infectious Diseases and Hospital Epidemiology, University Hospital Zurich, University of Zurich, CH-8091 Zurich, Switzerland; [email protected] * Correspondence: [email protected]; Tel.: +49-3834-420-5711 Received: 20 May 2019; Accepted: 10 June 2019; Published: 11 June 2019 Abstract: Necrotizing soft tissue infections (NSTIs) are critical clinical conditions characterized by extensive necrosis of any layer of the soft tissue and systemic toxicity. Group A streptococci (GAS) and Staphylococcus aureus are two major pathogens associated with monomicrobial NSTIs. In the tissue environment, both Gram-positive bacteria secrete a variety of molecules, including pore-forming exotoxins, superantigens, and proteases with cytolytic and immunomodulatory functions. The present review summarizes the current knowledge about streptococcal and staphylococcal toxins in NSTIs with a special focus on their contribution to disease progression, tissue pathology, and immune evasion strategies. Keywords: Streptococcus pyogenes; group A streptococcus; Staphylococcus aureus; skin infections; necrotizing soft tissue infections; pore-forming toxins; superantigens; immunomodulatory proteases; immune responses Key Contribution: Group A streptococcal and Staphylococcus aureus toxins manipulate host physiological and immunological responses to promote disease severity and progression. 1. Introduction Necrotizing soft tissue infections (NSTIs) are rare and represent a more severe rapidly progressing form of soft tissue infections that account for significant morbidity and mortality [1]. -
Manner Via Caspase-8 in an RIP3
Cutting Edge: FAS (CD95) Mediates Noncanonical IL-1 β and IL-18 Maturation via Caspase-8 in an RIP3-Independent Manner This information is current as of October 2, 2021. Lukas Bossaller, Ping-I Chiang, Christian Schmidt-Lauber, Sandhya Ganesan, William J. Kaiser, Vijay A. K. Rathinam, Edward S. Mocarski, Deepa Subramanian, Douglas R. Green, Neal Silverman, Katherine A. Fitzgerald, Ann Marshak-Rothstein and Eicke Latz Downloaded from J Immunol 2012; 189:5508-5512; Prepublished online 9 November 2012; doi: 10.4049/jimmunol.1202121 http://www.jimmunol.org/content/189/12/5508 http://www.jimmunol.org/ Supplementary http://www.jimmunol.org/content/suppl/2012/11/12/jimmunol.120212 Material 1.DC1 References This article cites 30 articles, 9 of which you can access for free at: http://www.jimmunol.org/content/189/12/5508.full#ref-list-1 by guest on October 2, 2021 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 *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 © 2012 by The American Association of Immunologists, Inc. All rights reserved. -
(12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002
USOO6395889B1 (12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002 (54) NUCLEIC ACID MOLECULES ENCODING WO WO-98/56804 A1 * 12/1998 ........... CO7H/21/02 HUMAN PROTEASE HOMOLOGS WO WO-99/0785.0 A1 * 2/1999 ... C12N/15/12 WO WO-99/37660 A1 * 7/1999 ........... CO7H/21/04 (75) Inventor: fish E. Robison, Wilmington, MA OTHER PUBLICATIONS Vazquez, F., et al., 1999, “METH-1, a human ortholog of (73) Assignee: Millennium Pharmaceuticals, Inc., ADAMTS-1, and METH-2 are members of a new family of Cambridge, MA (US) proteins with angio-inhibitory activity', The Journal of c: - 0 Biological Chemistry, vol. 274, No. 33, pp. 23349–23357.* (*) Notice: Subject to any disclaimer, the term of this Descriptors of Protease Classes in Prosite and Pfam Data patent is extended or adjusted under 35 bases. U.S.C. 154(b) by 0 days. * cited by examiner (21) Appl. No.: 09/392, 184 Primary Examiner Ponnathapu Achutamurthy (22) Filed: Sep. 9, 1999 ASSistant Examiner William W. Moore (51) Int. Cl." C12N 15/57; C12N 15/12; (74) Attorney, Agent, or Firm-Alston & Bird LLP C12N 9/64; C12N 15/79 (57) ABSTRACT (52) U.S. Cl. .................... 536/23.2; 536/23.5; 435/69.1; 435/252.3; 435/320.1 The invention relates to polynucleotides encoding newly (58) Field of Search ............................... 536,232,235. identified protease homologs. The invention also relates to 435/6, 226, 69.1, 252.3 the proteases. The invention further relates to methods using s s s/ - - -us the protease polypeptides and polynucleotides as a target for (56) References Cited diagnosis and treatment in protease-mediated disorders. -
The Role of Cyclooxygenase-2 in Cell Proliferation and Cell Death in Human Malignancies
Hindawi Publishing Corporation International Journal of Cell Biology Volume 2010, Article ID 215158, 21 pages doi:10.1155/2010/215158 Review Article TheRoleofCyclooxygenase-2inCellProliferationandCell Death in Human Malignancies Cyril Sobolewski,1 Claudia Cerella,1 Mario Dicato,1 Lina Ghibelli,2 and Marc Diederich1 1 LaboratoiredeBiologieMol´eculaire et Cellulaire du Cancer, Hopitalˆ Kirchberg, 9 rue Edward Steichen, 2540 Luxembourg, Luxembourg 2 Dipartimento di Biologia, Universita` di Roma di Roma Tor Vergata, Via Ricerca Scientifica snc, 00133 Rome, Italy Correspondence should be addressed to Marc Diederich, [email protected] Received 16 July 2009; Accepted 18 December 2009 Academic Editor: Simone Fulda Copyright © 2010 Cyril Sobolewski et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. It is well admitted that the link between chronic inflammation and cancer involves cytokines and mediators of inflammatory pathways, which act during the different steps of tumorigenesis. The cyclooxygenases (COXs) are a family of enzymes, which catalyze the rate-limiting step of prostaglandin biosynthesis. This family contains three members: ubiquitously expressed COX- 1, which is involved in homeostasis; the inducible COX-2 isoform, which is upregulated during both inflammation and cancer; and COX-3, expressed in brain and spinal cord, whose functions remain to be elucidated. COX-2 was described to modulate cell proliferation and apoptosis mainly in solid tumors, that is, colorectal, breast, and prostate cancers, and, more recently, in hematological malignancies. These findings prompt us to analyze here the effects of a combination of COX-2 inhibitors together with different clinically used therapeutic strategies in order to further improve the efficiency of future anticancer treatments. -
Solutions to Detect Apoptosis and Pyroptosis
Powerful Tools for In vitro Fluorescent Imaging in Cancer Research Jackie Carville May 11, 2016 About Us Products and Services • Custom Assay Services – Immunoassay design and development – Antibody purification/conjugation • Consumable Reagents – ELISA Solutions – Cell-permeant Fluorescent Probes for detection of cell death • Products for research use only. Not for use in diagnostic procedures. ELISA Solutions • ELISA Wash Buffer • PBS • Substrates • Stop Solutions • Plates • Coating Buffers • Blocking Buffers • Conjugate Stabilizers • Assay Diluents • Sample Diluents Custom Services • Antibody Conjugation • Immunoassay Design • Immunoassay Development • Lyophilization • Plate Coating Overview of ICT’s Fluorescent Probes FOR DETECTION OF: • Active caspases • Caspases/Cathepsins in real time • Mitochondrial Health • Cytotoxicity • Serine Proteases Today’s Agenda • FLICA • FLISP • Magic Red • Cell Viability • Mito PT • Oxidative Stress • Cytotoxicity FLICA • FLICA – Fluorescent Labeled Inhibitor of Caspases • In vitro, whole cell detection of caspase activity in apoptotic or caspase-positive cells • Available in green, red, and far red assays FLICA Cancer Research Applications • FLICA is the most accurate and sensitive method of apoptosis detection • Can identify four stages of cell death in one sample • Detect poly caspase activity or individual caspase enzymes How FLICA A. INACTIVE CASPASE (ZYMOGEN) works… prodomain B. CASPASE PROCESSING FMK Fluorescent Reporter YVAD tag C. ACTIVATED CASPASE (HETERO-TETRAMER) D. BINDING OF FLICA Sample -
The Osteoclast-Associated Protease Cathepsin K Is Expressed in Human Breast Carcinoma1
CANCER RESEARCH57. 5386-5390. December I, 19971 The Osteoclast-associated Protease Cathepsin K Is Expressed in Human Breast Carcinoma1 Amanda J. Littlewood-Evans,' Graeme Bilbe, Wayne B. Bowler, David Farley, Brenda Wlodarski, Toshio Kokubo, Tetsuya Inaoka, John Sloane, Dean B. Evans, and James A. Gallagher Novartis Pharina AG, CH-4002 Base!. Switzerland (A. I. L-E., G. B., D. F., D. B. El; Human Bone Cell Research Group, Department of Human Anatomy and Cell Biology 1W. B. B., B. W., J. A. G.J, and Department of Pathology If. S.), University of Liverpool, Liverpool 5.69 3BX, United Kingdom [W. B. B., B. W., J. S., J. A. G.]; and Takarazuka Research Institute, Novartis Pharma lid., Takarazuka 665, Japan IT. K., T. LI ABSTRACT (ZR75—l,Hs578Tduct, BT474, ZR75—30,BT549, and T-47D), adenocarci noma (MDA-MB-231, SK-BR3, MDA-MB-468, and BT2O), and breast car Human cathepsin K is a novel cysteine protease previously reported cinoma[MVLNandMTLN,transfectedMCF-7-derivedclonesobtainedfrom to be restricted in its expression to osteoclasts. Immunolocalization of Dr. J. C. Nicolas (Unit de Recherches sur Ia Biochemie des Steroides Insern cathepsin K in breast tumor bone metastases revealed that the invading U58, Montpelier, France), and MCF-7]. The MCF-7 cells were obtained from breast cancer cells expressed this protease, albeit at a lower intensity two different sources, ATCC and Dr. Roland Schuele (Tumor Klinik, Freiburg, than in osteoclasts. In situ hybridization and immunolocalization stud Germany). These are indicated in the figure legend as clone 1 (ATCC) and ies were subsequently conducted to demonstrate cathepsin K mRNA clone 2 (Dr. -
Molecular Markers of Serine Protease Evolution
The EMBO Journal Vol. 20 No. 12 pp. 3036±3045, 2001 Molecular markers of serine protease evolution Maxwell M.Krem and Enrico Di Cera1 ment and specialization of the catalytic architecture should correspond to signi®cant evolutionary transitions in the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St Louis, history of protease clans. Evolutionary markers encoun- MO 63110-1093, USA tered in the sequences contributing to the catalytic apparatus would thus give an account of the history of 1Corresponding author e-mail: [email protected] an enzyme family or clan and provide for comparative analysis with other families and clans. Therefore, the use The evolutionary history of serine proteases can be of sequence markers associated with active site structure accounted for by highly conserved amino acids that generates a model for protease evolution with broad form crucial structural and chemical elements of applicability and potential for extension to other classes of the catalytic apparatus. These residues display non- enzymes. random dichotomies in either amino acid choice or The ®rst report of a sequence marker associated with serine codon usage and serve as discrete markers for active site chemistry was the observation that both AGY tracking changes in the active site environment and and TCN codons were used to encode active site serines in supporting structures. These markers categorize a variety of enzyme families (Brenner, 1988). Since serine proteases of the chymotrypsin-like, subtilisin- AGY®TCN interconversion is an uncommon event, it like and a/b-hydrolase fold clans according to phylo- was reasoned that enzymes within the same family genetic lineages, and indicate the relative ages and utilizing different active site codons belonged to different order of appearance of those lineages. -
Biochemical Society Focused Meetings Proteases A
ORE Open Research Exeter TITLE Proteases and caspase-like activity in the yeast Saccharomyces cerevisiae. AUTHORS Wilkinson, D; Ramsdale, M JOURNAL Biochemical Society Transactions DEPOSITED IN ORE 18 November 2013 This version available at http://hdl.handle.net/10871/13957 COPYRIGHT AND REUSE Open Research Exeter makes this work available in accordance with publisher policies. A NOTE ON VERSIONS The version presented here may differ from the published version. If citing, you are advised to consult the published version for pagination, volume/issue and date of publication Biochemical Society Transactions (2011) XX, (XX-XX) (Printed in Great Britain) Biochemical Society Focused Meetings Proteases and caspase-like activity in the yeast Saccharomyces cerevisiae Derek Wilkinson and Mark Ramsdale1 Biosciences, University of Exeter, Geoffrey Pope Building, Stocker Road, Exeter, EX4 4QD Key words: Programmed cell death, apoptosis, necrosis, proteases, caspases, Saccharomyces cerevisiae. Abbreviations used: PCD, programmed cell death; ROS, reactive oxygen species; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; ER, endoplasmic reticulum; MS, mass spectrometry. 1email [email protected] Abstract A variety of proteases have been implicated in yeast PCD including the metacaspase, Mca1 and the separase Esp1, the HtrA-like serine protease Nma111, the cathepsin-like serine carboxypeptideases and a range of vacuolar proteases. Proteasomal activity is also shown to have an important role in determining cell fate, with both pro- and anti-apoptotic roles. Caspase-3, -6- and -8 like activities are detected upon stimulation of yeast PCD, but not all of this activity is associated with Mca1, implicating other proteases with caspase-like activity in the yeast cell death response. -
Calpain Inhibitors Prevent Nitric Oxide-Triggered Excitotoxic Apoptosis
Calpain inhibitors prevent nitric oxide- triggered excitotoxic apoptosis Christiane Volbracht,1,2 Eugenio Fava,1,3 Marcel Leist1,4 and Pierluigi Nicotera1,3,CA 1Molecular Toxicology, University of Konstanz, Konstanz, Germany; 2Institute of Molecular and Cell Biology, Singapore 117609, Singapore; 3MRC Toxicology Unit, University of Leicester, PO Box 138, Lancaster Road, Leicester LE1 9HN; 4Department of Neurobiology, H. Lundbeck A/S, 2500 Valby, Denmark CACorresponding Author The pathogenesis of some neurodegenerative disorders has potential, chromatin breakdown, and subsequent death of been linked to excitotoxicity, excess generation of nitric oxide cerebellar granule neurons exposed to NO donors (S-nitroso- (NO) and apoptosis. Here, we used a model of NO-triggered L-glutathione, S-nitroso-N-acetyl-D,L-penicillamine, and diethy- neuronal apoptosis that was strictly dependent on autocrine lamino-diazenolate-2-oxide). Since inhibitors did not interfere 2 NMDA receptor (NMDA-R) activation and intracellular Ca with NMDA-R activation, we suggest that block of calpains increase. We investigated the ef®ciency and potentially bene- blunts NO-triggered neuronal apoptosis by stopping the ®cial effects of calpain inhibition. Three calpain inhibitors that cascade downstream of primary autocrine excitotoxic events. prevented intracellular fodrin proteolysis also blocked apopto- NeuroReport 12:3645±3648 & 2001 Lippincott Williams & tic features such as decrease in mitochondrial membrane Wilkins. Key words: Apoptosis; Calpains; Excitotoxicity; Mitochondria; Nitric oxide INTRODUCTION MATERIALS AND METHODS Massive generation of the pleiotropic messenger molecule Cell culture: Murine CGC were isolated from 8-day-old nitric oxide (NO) has been implicated in many neuro- speci®c pathogen free BALB/e mice obtained from the pathological conditions including ischemia [1]. -
Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag
biomolecules Article Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag Removal: Cloning, Expression in Escherichia coli, Purification, and Characterization 1,2, 1,2, , 1,3 1,3 Monika Cserjan-Puschmann y , Nico Lingg * y , Petra Engele , Christina Kröß , Julian Loibl 1, Andreas Fischer 1, Florian Bacher 1, Anna-Carina Frank 1,2, Christoph Öhlknecht 1,4,Cécile Brocard 5, Chris Oostenbrink 1,4 , Matthias Berkemeyer 5, Rainer Schneider 1,3, Gerald Striedner 1,2 and Alois Jungbauer 1,2,* 1 ACIB-Austrian Centre of Industrial Biotechnology, Muthgasse 18, 1190 Vienna, Austria; [email protected] (M.C.-P.); [email protected] (P.E.); [email protected] (C.K.); [email protected] (J.L.); andreas.fi[email protected] (A.F.); fl[email protected] (F.B.); [email protected] (A.-C.F.); [email protected] (C.Ö.); [email protected] (C.O.); [email protected] (R.S.); [email protected] (G.S.) 2 Department of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria 3 Institute of Biochemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, 6020 Innsbruck, Austria 4 Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria 5 Biopharma Process Science Austria, Boehringer Ingelheim RCV GmbH & Co KG, Dr. Boehringer-Gasse 5-11, 1121 Vienna, Austria; [email protected] (C.B.); [email protected] (M.B.) * Correspondence: [email protected] (N.L.); [email protected] (A.J.) These authors have contributed equally to the manuscript. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants.