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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. -
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. -
The Role of Caspase-2 in Regulating Cell Fate
cells Review The Role of Caspase-2 in Regulating Cell Fate Vasanthy Vigneswara and Zubair Ahmed * Neuroscience and Ophthalmology, Institute of Inflammation and Ageing, University of Birmingham, Birmingham B15 2TT, UK; [email protected] * Correspondence: [email protected] Received: 15 April 2020; Accepted: 12 May 2020; Published: 19 May 2020 Abstract: Caspase-2 is the most evolutionarily conserved member of the mammalian caspase family and has been implicated in both apoptotic and non-apoptotic signaling pathways, including tumor suppression, cell cycle regulation, and DNA repair. A myriad of signaling molecules is associated with the tight regulation of caspase-2 to mediate multiple cellular processes far beyond apoptotic cell death. This review provides a comprehensive overview of the literature pertaining to possible sophisticated molecular mechanisms underlying the multifaceted process of caspase-2 activation and to highlight its interplay between factors that promote or suppress apoptosis in a complicated regulatory network that determines the fate of a cell from its birth and throughout its life. Keywords: caspase-2; procaspase; apoptosis; splice variants; activation; intrinsic; extrinsic; neurons 1. Introduction Apoptosis, or programmed cell death (PCD), plays a pivotal role during embryonic development through to adulthood in multi-cellular organisms to eliminate excessive and potentially compromised cells under physiological conditions to maintain cellular homeostasis [1]. However, dysregulation of the apoptotic signaling pathway is implicated in a variety of pathological conditions. For example, excessive apoptosis can lead to neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease, whilst insufficient apoptosis results in cancer and autoimmune disorders [2,3]. Apoptosis is mediated by two well-known classical signaling pathways, namely the extrinsic or death receptor-dependent pathway and the intrinsic or mitochondria-dependent pathway. -
Preclinical Characterization of Dostarlimab, a Therapeutic Anti-PD
MABS 2021, VOL. 13, NO. 1, e1954136 (12 pages) https://doi.org/10.1080/19420862.2021.1954136 REPORTS Preclinical characterization of dostarlimab, a therapeutic anti-PD-1 antibody with potent activity to enhance immune function in in vitro cellular assays and in vivo animal models Sujatha Kumara*, Srimoyee Ghoshb, Geeta Sharmac, Zebin Wangd, Marilyn R. Kehrye, Margaret H. Marinof, Tamlyn Y. Nebenf, Sharon Lug, Shouqi Luoh, Simon Robertsi, Sridhar Ramaswamyj, Hadi Danaeek, and David Jenkinsl aTranslational Research, Immuno-Oncology, Checkmate Pharmaceuticals, Cambridge, MA, USA; bOncology Experimental Medicine Unit, GlaxoSmithKline, Waltham, MA, USA; cSynthetic Lethal Research Unit, Oncolog, GlaxoSmithKline, Waltham, MA, USA; dTranslational Strategy & Research, GlaxoSmithKline,Waltham, MA, USA; eCell Biology, AnaptysBio, Inc,San Diego, CA, USA; fProgram Management, AnaptysBio, Inc, San Diego, CA, USA; gClinical Pharmacology, Scholar Rock, Cambridge, MA, USA; hToxicology, Atea Pharmaceuticals, Boston, MA, USA; iNonclinical Development, Research In Vivo/In Vitro Translation, GlaxoSmithKline, Waltham, MA, USA; jGoogle Ventures, Cambridge, MA, USA; kTranslational Medicine, Blue Print Medicines, Cambridge, MA, USA; lExternal Innovations, IPSEN, Cambridge, MA, USA ABSTRACT ARTICLE HISTORY Inhibitors of programmed cell death protein 1 (PD-1) and its ligand (PD-L1) have dramatically changed the Received 17 December 2020 treatment landscape for patients with cancer. Clinical activity of anti-PD-(L)1 antibodies has resulted in Revised 2 July 2021 increased median overall survival and durable responses in patients across selected tumor types. To date, Accepted 7 July 2021 6 PD-1 and PD-L1, here collectively referred to as PD-(L)1, pathway inhibitors are approved by the US Food KEYWORDS and Drug Administration for clinical use. -
Quantikine® ELISA
Quantikine® ELISA Human Granzyme B Immunoassay Catalog Number DGZB00 For the quantitative determination of human Granzyme B concentrations in culture supernates. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................3 PRECAUTIONS .........................................................................................................................................................................4 SAMPLE COLLECTION & STORAGE .................................................................................................................................4 -
Death by Granzyme B
RESEARCH HIGHLIGHTS APOPTOSIS Death by granzyme B DOI: 10.1038/nri1951 The death of effector T cells following pro-apoptotic ligands and effector lysosomal-associated membrane pro- Link activation is an important process molecules in AICD of T 1 cells and tein 1 (LAMP1; a marker of granules) Granzyme B H http://www.ncbi.nlm.nih.gov/ in the termination of an immune TH2 cells. Blocking the pro-apoptotic was observed in both resting TH1 entrez/viewer.fcgi?db=protein response. However, the mechanisms molecule CD95 ligand (also known cells and resting TH2 cells. However, &val=1247451 that are involved in this activation- as FAS ligand) with specific agents following TCR engagement, colocali- induced cell death (AICD) through inhibited AICD of TH1 cells, as previ- zation was observed only in TH1 cells, engagement of the T-cell receptor ously reported. However, these agents indicating that granzyme B is released (TCR) are not well understood. Now, had no effect on the death of TH2 from the granules on activation of TH2 new research published in Immunity cells. Similarly, blocking the activity of cells but not TH1 cells. Interestingly, shows that granzyme B has an impor- several caspases affected only TH1-cell the amount of SPI6, which is a tant role in AICD of T helper 2 (TH2) death, whereas inhibition of TRAIL protease inhibitor that specifically cells. (tumour-necrosis-factor-related inhibits the activity of granzyme B, Examination of the kinetics of apoptosis-inducing ligand) did not was found to be increased in activated AICD, by staining for annexin V affect either cell type. -
The Role of Serratiopeptidase in the Resolution of Inflammation
ARTICLE IN PRESS asian journal of pharmaceutical sciences ■■ (2017) ■■– ■■ Available online at www.sciencedirect.com ScienceDirect journal homepage: www.elsevier.com/locate/ajps Review The role of serratiopeptidase in the resolution of inflammation Manju Tiwari * Department of Biochemistry and Genetics, Barkatullah University, Bhopal, Madhya Pradesh, India ARTICLE INFO ABSTRACT Article history: Inflammation remains a key event during most of the diseases and physiological imbal- Received 26 October 2016 ance. Acute inflammation is an essential physiological event by immune system for a protective Received in revised form 9 measure to remove cause of inflammation and failure of resolution lead to chronic inflam- December 2016 mation. Over a period of time, a number of drugs mostly chemical have been deployed to Accepted 16 January 2017 combat acute and chronic inflammation. Recently, enzyme based anti-inflammatory drugs Available online became popular over conventional chemical based drugs. Serratiopeptidase, a proteolytic enzyme from trypsin family, possesses tremendous scope in combating inflammation. Serine Keywords: protease possesses a higher affinity for cyclooxygenase (COX-I and COX-II), a key enzyme Inflammation associated with production of different inflammatory mediators including interleukins (IL), Cyclooxygenase prostaglandins (PGs) and thromboxane (TXs) etc. Currently, arthritis, sinusitis, bronchitis, NSAIDs fibrocystic breast disease, and carpal tunnel syndrome, etc. are the leading inflammatory Serratiopeptidase disorders that affected the entire the globe. In order to conquer inflammation, both acute Steroids and chronic world, physician mostly relies on conventional drugs. The most common drugs Enzyme therapeutics to combat acute inflammation are Nonsteroidal anti-inflammatory drugs (NSAIDs) alone and or in combination with other drugs. However, during chronic inflammation, NSAIDs are often used with steroidal drugs such as autoimmune disorders. -
WO 2017/143026 Al 24 August 2017 (24.08.2017) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2017/143026 Al 24 August 2017 (24.08.2017) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every C12N 9/52 (2006.0 1) C12N 9/64 (2006.0 1) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (21) International Application Number: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, PCT/US2017/0181 16 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KH, KN, 16 February 2017 (16.02.2017) KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, (25) Filing Language: English NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, (26) Publication Language: English RU, RW, SA, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, (30) Priority Data: ZA, ZM, ZW. 62/295,636 16 February 2016 (16.02.2016) US (84) Designated States (unless otherwise indicated, for every (71) Applicant: RESEARCH DEVELOPMENT FOUNDA¬ kind of regional protection available): ARIPO (BW, GH, TION [US/US]; 402 North Division Street, Carson City, GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, NV 89703 (US). -
The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin
The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin. Christine Gaboriaud, Rajesh Kumar Gupta, Lydie Martin, Monique Lacroix, Laurence Serre, Florence Teillet, Gérard J Arlaud, Véronique Rossi, Nicole Thielens To cite this version: Christine Gaboriaud, Rajesh Kumar Gupta, Lydie Martin, Monique Lacroix, Laurence Serre, et al.. The serine protease domain of MASP-3: enzymatic properties and crystal structure in complex with ecotin.. PLoS ONE, Public Library of Science, 2013, 8 (7), pp.e67962. 10.1371/journal.pone.0067962. inserm-00868926 HAL Id: inserm-00868926 https://www.hal.inserm.fr/inserm-00868926 Submitted on 2 Oct 2013 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. The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin Christine Gaboriaud1,2,3*, Rajesh Kumar Gupta1,2,3¤a, Lydie Martin1,2,3, Monique Lacroix1,2,3, Laurence Serre3,1¤b, Florence Teillet1,2,3,Ge´rard J. Arlaud1,2,3,Ve´ronique Rossi1,2,3, Nicole M. Thielens1,2,3 1 Institut de Biologie Structurale (IBS), Direction des Sciences du Vivant, Commissariat a` l’Energie Atomique et aux Energies Alternatives, Grenoble, France, 2 IBS, Centre National de la Recherche Scientifique, Grenoble, France, 3 IBS, Universite´ Grenoble Alpes, Grenoble, France Abstract Mannan-binding lectin (MBL), ficolins and collectin-11 are known to associate with three homologous modular proteases, the MBL-Associated Serine Proteases (MASPs). -
Molecular Mechanisms Underlying Toxicant Effects on Mast Cell Signaling and Mitochondria Juyoung Katherine Shim University of Maine, [email protected]
The University of Maine DigitalCommons@UMaine Electronic Theses and Dissertations Fogler Library Summer 8-17-2018 Molecular Mechanisms Underlying Toxicant Effects on Mast Cell Signaling and Mitochondria Juyoung Katherine Shim University of Maine, [email protected] Follow this and additional works at: https://digitalcommons.library.umaine.edu/etd Part of the Molecular Biology Commons, and the Toxicology Commons Recommended Citation Shim, Juyoung Katherine, "Molecular Mechanisms Underlying Toxicant Effects on Mast Cell Signaling and Mitochondria" (2018). Electronic Theses and Dissertations. 2909. https://digitalcommons.library.umaine.edu/etd/2909 This Open-Access Thesis is brought to you for free and open access by DigitalCommons@UMaine. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of DigitalCommons@UMaine. For more information, please contact [email protected]. MOLECULAR MECHANISMS UNDERLYING TOXICANT EFFECTS ON MAST CELL SIGNALING AND MITOCHONDRIA By Juyoung K. Shim B.A. Hankook University of Foreign Studies, 1994 B.S. Bates College, 2005 A DISSERTATION Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy (in Biochemistry and Molecular Biology) The Graduate School The University of Maine August 2018 Advisory Committee: Julie A. Gosse, Associate Professor of Biochemistry; Advisor John T. Singer, Professor of Microbiology Paul J. Millard, Associate Professor of Chemical and Biological Engineering Rebecca J. Van Beneden, Professor of Biochemistry and Marine Sciences, Director for School of Marine Sciences Robert E. Gundersen, Chair of Molecular and Biomedical Sciences © 2018 Juyoung Katherine Shim All Rights Reserved ii MOLECULAR MECHANISMS UNDERLYING TOXICANT EFFECTS ON MAST CELL SIGNALING AND MITOCHONDRIA By Juyoung K.