A Review of the Complement Membrane Attack Complex
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A Diverse Host Thrombospondin-Type-1
RESEARCH ARTICLE A diverse host thrombospondin-type-1 repeat protein repertoire promotes symbiont colonization during establishment of cnidarian-dinoflagellate symbiosis Emilie-Fleur Neubauer1, Angela Z Poole2,3, Philipp Neubauer4, Olivier Detournay5, Kenneth Tan3, Simon K Davy1*, Virginia M Weis3* 1School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand; 2Department of Biology, Western Oregon University, Monmouth, United States; 3Department of Integrative Biology, Oregon State University, Corvallis, United States; 4Dragonfly Data Science, Wellington, New Zealand; 5Planktovie sas, Allauch, France Abstract The mutualistic endosymbiosis between cnidarians and dinoflagellates is mediated by complex inter-partner signaling events, where the host cnidarian innate immune system plays a crucial role in recognition and regulation of symbionts. To date, little is known about the diversity of thrombospondin-type-1 repeat (TSR) domain proteins in basal metazoans or their potential role in regulation of cnidarian-dinoflagellate mutualisms. We reveal a large and diverse repertoire of TSR proteins in seven anthozoan species, and show that in the model sea anemone Aiptasia pallida the TSR domain promotes colonization of the host by the symbiotic dinoflagellate Symbiodinium minutum. Blocking TSR domains led to decreased colonization success, while adding exogenous *For correspondence: Simon. TSRs resulted in a ‘super colonization’. Furthermore, gene expression of TSR proteins was highest [email protected] (SKD); weisv@ at early time-points during symbiosis establishment. Our work characterizes the diversity of oregonstate.edu (VMW) cnidarian TSR proteins and provides evidence that these proteins play an important role in the Competing interests: The establishment of cnidarian-dinoflagellate symbiosis. authors declare that no DOI: 10.7554/eLife.24494.001 competing interests exist. -
Thrombospondin-1, Human (ECM002)
Thrombospondin-1, human recombinant, expressed in HEK 293 cells suitable for cell culture Catalog Number ECM002 Storage Temperature –20 C Synonyms: THBS1, THBS, TSP1, TSP This product is supplied as a powder, lyophilized from phosphate buffered saline. It is aseptically filled. Product Description Thrombospondin-1 (TSP1) is believed to play a role in The biological activity of recombinant human cell migration and proliferation, during embryogenesis thrombospondin-1 was tested in culture by measuring and wound repair.1-2 TSP1 expression is highly the ability of immobilized DTT-treated regulated by different hormones and cytokines, and is thrombospondin-1 to support adhesion of SVEC4-10 developmentally controlled. TSP1 stimulates the growth cells. of vascular smooth muscle cells and human foreskin fibroblasts. A combination of interferon and tumor Uniprot: P07996 necrosis factor inhibits TSP1 production in these cells.3 In endothelial cells, it controls adhesion and Purity: 95% (SDS-PAGE) migration as well as proliferation. It also exhibits antiangiogenic properties and regulates immune Endotoxin level: 1.0 EU/g FN (LAL) processes.4-5 TSP1 binds to various cell surface receptors, such as integrins and integrin-associated Precautions and Disclaimer protein CD47.1 It also plays a crucial role in This product is for R&D use only, not for drug, inflammatory processes and post-inflammatory tissue household, or other uses. Please consult the Safety dynamics.6 TSP1 has been used as a potential Data Sheet for information regarding hazards and safe regulator of tumor growth and metastasis.5 It is handling practices. upregulated in rheumatoid synovial tissues and might be associated with rheumatoid arthritis.7 Variants of this Preparation Instructions gene might be linked with increased risk of autism.8 Briefly centrifuge the vial before opening. -
Role of Perforin-2 in Regulating Type I Interferon Signaling
https://www.scientificarchives.com/journal/journal-of-cellular-immunology Journal of Cellular Immunology Review Article Role of Perforin-2 in Regulating Type I Interferon Signaling Gregory V Plano, Noula Shembade* Department of Microbiology and Immunology, Sylvester Comprehensive Cancer Center Miller School of Medicine, University of Miami, Miami, FL 33136, USA *Correspondence should be addressed to Noula Shembade; [email protected] Received date: November 21, 2020, Accepted date: February 02, 2021 Copyright: © 2021 Plano G, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Abstract Sepsis is a systemic inflammatory response caused by a harmful host immune reaction that is activated in response to microbial infections. Infection-induced type I interferons (IFNs) play critical roles during septic shock. Type I IFNs initiate their biological effects by binding to their transmembrane interferon receptors and initiating the phosphorylation and activation of tyrosine kinases TYK2 and JAK1, which promote phosphorylation and activation of STAT molecules. Type I IFN-induced activation of JAK/STAT pathways is a complex process and not well understood. Improper regulation of type I IFN responses can lead to the development of infectious and inflammation-related diseases, including septic shock, autoimmune diseases, and inflammatory syndromes. This review is mainly focused on the possible mechanistic roles of the transmembrane Perforin-2 molecule in the regulation of type I IFN- induced signaling. Keywords: JAK/STAT, Interferons, TYK2, STATs, Perforin-2, IFNAR1, IFNAR2 and Signaling Introduction and activator of transcription 2), respectively, under normal physiological conditions [4,5]. -
Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins
Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins. Robert Frangež, Dušan Šuput, Jordi Molgó, Evelyne Benoit To cite this version: Robert Frangež, Dušan Šuput, Jordi Molgó, Evelyne Benoit. Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins.. Toxins, MDPI, 2017, 9 (4), 10.3390/toxins9040128. hal-01572247 HAL Id: hal-01572247 https://hal.archives-ouvertes.fr/hal-01572247 Submitted on 20 May 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. toxins Review Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins Robert Frangež 1, Dušan Šuput 2, Jordi Molgó 3 and Evelyne Benoit 3,* 1 Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana; 1115-Ljubljana, Slovenia; [email protected] 2 Laboratory for Cell Physiology and Toxinology, Institute of Pathophysiology, School of Medicine, University of Ljubljana, P.O. Box 11, 1105-Ljubljana, Slovenia; [email protected] 3 DRF/Institut de Sciences de la Vie Frédéric Joliot/SIMOPRO, CEA de Saclay, and Institut des Neurosciences Paris-Saclay (Neuro-PSI), UMR 9197 CNRS/Université Paris-Sud, 91190 Gif-sur-Yvette, France; [email protected] * Correspondence: [email protected]; Tel.: +33-169-085-685 Academic Editor: Michel R. -
Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins
Review Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins Wei Yuen Yap 1 and Jung Shan Hwang 2,* 1 Department of Biological Sciences, School of Science and Technology, Sunway University, No. 5 Jalan Universiti, Bandar Sunway, Selangor Darul Ehsan 47500, Malaysia; [email protected] 2 Department of Medical Sciences, School of Healthcare and Medical Sciences, Sunway University, No. 5 Jalan Universiti, Bandar Sunway, Selangor Darul Ehsan 47500, Malaysia * Correspondence: [email protected]; Tel.: +603-7491-8622 (ext. 7414) Academic Editor: Jean-Marc Sabatier Received: 23 August 2018; Accepted: 28 September 2018; Published: 4 October 2018 Abstract: A group of stable, water-soluble and membrane-bound proteins constitute the pore forming toxins (PFTs) in cnidarians. They interact with membranes to physically alter the membrane structure and permeability, resulting in the formation of pores. These lesions on the plasma membrane causes an imbalance of cellular ionic gradients, resulting in swelling of the cell and eventually its rupture. Of all cnidarian PFTs, actinoporins are by far the best studied subgroup with established knowledge of their molecular structure and their mode of pore-forming action. However, the current view of necrotic action by actinoporins may not be the only mechanism that induces cell death since there is increasing evidence showing that pore-forming toxins can induce either necrosis or apoptosis in a cell-type, receptor and dose-dependent manner. In this review, we focus on the response of the cellular immune system to the cnidarian pore-forming toxins and the signaling pathways that might be involved in these cellular responses. -
Stonefish Toxin Defines an Ancient Branch of the Perforin-Like Superfamily
Stonefish toxin defines an ancient branch of the perforin-like superfamily Andrew M. Ellisdona,b, Cyril F. Reboula,b, Santosh Panjikara,c, Kitmun Huynha, Christine A. Oelliga, Kelly L. Wintera,d, Michelle A. Dunstonea,b,e, Wayne C. Hodgsond, Jamie Seymourf, Peter K. Deardeng, Rodney K. Twetenh, James C. Whisstocka,b,1,2, and Sheena McGowane,1,2 aBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; bAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia; cAustralian Synchrotron, Macromolecular Crystallography, Melbourne, VIC, 3168, Australia; dBiomedicine Discovery Institute and Department of Pharmacology, Monash University, Melbourne, VIC, 3800, Australia; eBiomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia; fCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD, 4870, Australia; gDepartment of Biochemistry and Genetics Otago, University of Otago, Dunedin, 9054 Aotearoa–New Zealand; and hDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104 Edited by Brenda A. Schulman, St. Jude Children’s Research Hospital, Memphis, TN, and approved November 3, 2015 (received for review April 19, 2015) The lethal factor in stonefish venom is stonustoxin (SNTX), a parallel interface along their entire 115-Å length (2,908 Å2 heterodimeric cytolytic protein that induces cardiovascular collapse buried surface area) (Fig. 1 A–D and Fig. S1). Fold recognition in humans and native predators. Here, using X-ray crystallography, searches reveal that each SNTX protein comprises four do- we make the unexpected finding that SNTX is a pore-forming mains (Fig. -
Measuring Kinetic Drivers of Pneumolysin Pore Structure
Eur Biophys J (2016) 45:365–376 DOI 10.1007/s00249-015-1106-x ORIGINAL ARTICLE Measuring kinetic drivers of pneumolysin pore structure Robert J. C. Gilbert1 · Andreas F.-P. Sonnen2 Received: 7 October 2015 / Revised: 1 December 2015 / Accepted: 7 December 2015 / Published online: 23 February 2016 © The Author(s) 2016. This article is published with open access at Springerlink.com Abstract Most membrane attack complex-perforin/ Keywords Pore formation · Kinetics · MACPF/CDC · cholesterol-dependent cytolysin (MACPF/CDC) proteins Toroidal pore · Oligomerization · Membrane structure are thought to form pores in target membranes by assem- bling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into Introduction both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by The membrane attack complex-perforin/cholesterol- a mechanism dependent on protein concentration in which dependent cytolysin (MACPF/CDC) family is the largest- arc pores arise due to kinetic trapping of the pre-pore forms known group of pore-forming proteins (Anderluh and by the depletion of free protein subunits during oligomeri- Gilbert 2014; Gilbert et al. 2013). Members have been zation. Here we describe the use of a kinetic assay to study identified in every kind of cellular life form apart from the pore formation in red blood cells by the MACPF/CDC Archaebacteria, and within their producing organisms they pneumolysin from Streptococcus pneumoniae. We show enact a plethora of different biological functions (Ander- that cell lysis displays two kinds of dependence on pro- luh et al. -
Matrix Mechanotransduction Mediated by Thrombospondin-1/Integrin/YAP in the Vascular Remodeling
Matrix mechanotransduction mediated by thrombospondin-1/integrin/YAP in the vascular remodeling Yoshito Yamashiroa,1, Bui Quoc Thangb, Karina Ramireza,c, Seung Jae Shina,d, Tomohiro Kohatae, Shigeaki Ohataf, Tram Anh Vu Nguyena,c, Sumio Ohtsukie, Kazuaki Nagayamaf, and Hiromi Yanagisawaa,g,1 aLife Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance, University of Tsukuba, Ibaraki 305-8577, Japan; bDepartment of Cardiovascular Surgery, University of Tsukuba, Ibaraki 305-8575, Japan; cPh.D. Program in Human Biology, School of Integrative and Global Majors, University of Tsukuba, Ibaraki 305-8577, Japan; dGraduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8577, Japan; eFaculty of Life Sciences, Kumamoto University, Kumamoto 862-0973, Japan; fGraduate School of Mechanical Systems Engineering, Ibaraki University, Ibaraki 316-8511, Japan; and gDivision of Biomedical Science, Faculty of Medicine, University of Tsukuba, Ibaraki 305-8577, Japan Edited by Kun-Liang Guan, University of California San Diego, La Jolla, CA, and accepted by Editorial Board Member Christine E. Seidman March 15, 2020 (received for review November 9, 2019) The extracellular matrix (ECM) initiates mechanical cues that highly context dependent, and extracellular regulators are not activate intracellular signaling through matrix–cell interactions. fully understood (6, 9). In blood vessels, additional mechanical cues derived from the pul- Thrombospondin-1 (Thbs1) is a homotrimeric glycoprotein satile blood flow and pressure play a pivotal role in homeostasis with a complex multidomain structure capable of interacting with and disease development. Currently, the nature of the cues from a variety of receptors such as integrins, cluster of differentiation the ECM and their interaction with the mechanical microenviron- (CD) 36, and CD47 (10). -
Cell Surface-Localized Matrix Metalloproteinase-9 Proteolytically Activates TGF- and Promotes Tumor Invasion and Angiogenesis
Downloaded from genesdev.cshlp.org on September 23, 2021 - Published by Cold Spring Harbor Laboratory Press Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF- and promotes tumor invasion and angiogenesis Qin Yu and Ivan Stamenkovic1 Molecular Pathology Unit, Massachusetts General Hospital, and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02129 USA We have uncovered a novel functional relationship between the hyaluronan receptor CD44, the matrix metalloproteinase-9 (MMP-9) and the multifunctional cytokine TGF- in the control of tumor-associated tissue remodeling. CD44 provides a cell surface docking receptor for proteolytically active MMP-9 and we show here that localization of MMP-9 to cell surface is required for its ability to promote tumor invasion and angiogenesis. Our observations also indicate that MMP-9, as well as MMP-2, proteolytically cleaves latent TGF-, providing a novel and potentially important mechanism for TGF- activation. In addition, we show that MMP-9 localization to the surface of normal keratinocytes is CD44 dependent and can activate latent TGF-. These observations suggest that coordinated CD44, MMP-9, and TGF- function may provide a physiological mechanism of tissue remodeling that can be adopted by malignant cells to promote tumor growth and invasion. [Key Words: MMP-9; CD44; TGF-; tumor angiogenesis; tumor invasion] Received September 10, 1999; revised version accepted December 7, 1999. The ability of tumor cells to establish a functional rela- nals transduced by integrins following engagement by tionship with their host tissue microenvironment and to ligands may provide tumor cells with critical survival utilize the local resources to their advantage are key fac- signals within the host tissue microenvironment (Frisch tors in determining tumor cell survival, local tumor de- and Ruoslahti 1997). -
Extracellular Matrix Retention of Thrombospondin 1 Is Controlled by Its Conserved C-Terminal Region
784 Research Article Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region Josephine C. Adams1,2,*, Amber A. Bentley1, Marc Kvansakul3,‡, Deborah Hatherley4 and Erhard Hohenester3 1Department of Cell Biology, Lerner Research Institute, and 2Department of Molecular Medicine, Cleveland Clinic Lerner College of Medicine, Cleveland Clinic Foundation, Cleveland, OH 44195, USA 3Division of Cell and Molecular Biology, Imperial College London, Biophysics Section, Blackett Laboratory, London, SW7 2AZ, UK 4Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, UK *Author for correspondence (e-mail: [email protected]) ‡Present address: Structural Biology Division, The Walter and Eliza Hall Institute, 3050 Parkville, Victoria, Australia Accepted 3 December 2007 J. Cell Sci. 121, 784-795 Published by The Company of Biologists 2008 doi:10.1242/jcs.021006 Summary Thrombospondins (TSPs) are an evolutionarily ancient family domain or type 1 repeats. Using a novel mRFP-tagged TSP1 of extracellular calcium-binding glycoproteins. The five C-terminal trimer, we demonstrate that ECM retention involves mammalian TSPs collectively have important roles in the RGD site and a novel site in the L-lectin domain with angiogenesis and vascular biology, synaptogenesis, wound repair structural similarity to the ligand-binding site of cargo transport and connective tissue organisation. Their complex functions proteins. CD47 and 1 integrins are dispensable for ECM relate to the multiple postsecretion fates of TSPs that can involve retention, but 1 integrins enhance activity. These novel data endocytic uptake, proteolysis or retention within the advance concepts of the molecular processes that lead to ECM extracellular matrix (ECM). -
Thrombospondin-1 Peptides Signaling by Thrombospondin-1
b 1 Integrin- and Proteoglycan-Mediated Stimulation of T Lymphoma Cell Adhesion and Mitogen-Activated Protein Kinase Signaling by Thrombospondin-1 and Thrombospondin-1 Peptides Katherine E. Wilson,1 Zhuqing Li, Murat Kara, Kevin L. Gardner, and David D. Roberts2 Cell-cell and cell-matrix interactions play important regulatory roles in lymphocyte homeostasis. Thrombospondin-1 (TSP1) is a matricellular protein that differentially promotes the adhesion of resting and activated T cells. In this work, we show that adhesion b of Jurkat T cells on substrates coated with TSP1 or TSP1-derived peptides is mediated by 1 integrins, CD47, and heparan sulfate proteoglycans. Interactions with TSP1 or TSP1 peptides stimulated CD3-induced Ras activation and tyrosine phosphorylation of several T cell proteins. The signals from TSP1 and its derived peptides differentially synergized with activation of the TCR to induce phosphorylation of linker for activation of T cells (LAT) and extracellular signal-regulated kinase (ERK) 1/2, c-Jun N-terminal kinase, and p38 kinases. The phosphorylation of ERK in the presence of full-length TSP1 was transient and dependent b on a 1 integrin receptor. Interestingly, peptides derived from the type 1 repeats of TSP1 and a CD47-binding peptide from the carboxyl-terminal domain of TSP1 also stimulated mitogen-activated protein (MAP) kinase phosphorylation. Moreover, the TSP1 heparin-binding peptide synergized with Ab-ligated TCR to transduce signals to the nucleus, detected by activation of AP-1- and Elk-dependent transcription. This TSP1 peptide-dependent activation of AP-1 was inhibited by both heparin and the MAP/ERK kinase inhibitor PD98059, providing a functional link between adhesion molecule interaction and nuclear transactivation events via the MAP kinase pathways. -
The Kinetics of C9, Vitronectin and the Terminal Complement
CERTIFICATE OF ORIGINALITY I hereby declare that this submission is my own work and that, to the best of my knowledge and belief, it contains no material previously published or written by another person nor material which to a substantial extent has been accepted for the award of any other degree or diploma of a university or other institute of higher learning, except where due acknowledgement is made in the text. I also declare that the intellectual content of this thesis is the product of my own work, even though I may have received assistance from others on style, presentation and language expression. (Signee THE KINETICS OF C9, VITRONECTIN AND THE TERMINAL COMPLEMENT COMPLEX by James David Greenstein Department of Nephrology, Prince Henry Hospital, Sydney, Australia and Faculty of Medicine, University of New South Wales, Sydney, Australia Submitted/or the degree ofDoctor ofPhilosophy 1997 u i'J s vv 1 4 MAY 1998 LlBHARY A n ABSTRACT The primary pathways of complement activation converge to produce the terminal complement complex (TCC). Assembly of the TCC on a cell surface may result in the formation of a cytolytic pore, or membrane attack complex (MAC, i.e. C5b- 9(m)), composed of the five terminal complement components. Alternatively, complement activation in the plasma produces the soluble form, SC5b-9, which by the inclusion of regulatory proteins, vitronectin (S-protein) and clusterin, is rendered unable to disrupt cells. Activation of the complement system occurs in several autoimmune diseases although the role of the terminal complex in their pathogenesis remains uncertain. Measurement of its concentration in the plasma, or that of its components, provides limited information about terminal complement pathway activity.