Transcriptomic and Proteomic Analysis of the Tentacles and Mucus of Anthopleura Dowii Verrill, 1869
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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. -
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). -
Sea Anemone (Cnidaria, Anthozoa, Actiniaria) Toxins: an Overview
Mar. Drugs 2012, 10, 1812-1851; doi:10.3390/md10081812 OPEN ACCESS Marine Drugs ISSN 1660-3397 www.mdpi.com/journal/marinedrugs Review Sea Anemone (Cnidaria, Anthozoa, Actiniaria) Toxins: An Overview Bárbara Frazão 1,2, Vitor Vasconcelos 1,2 and Agostinho Antunes 1,2,* 1 CIMAR/CIIMAR, Centro Interdisciplinar de Investigação Marinha e Ambiental, Universidade do Porto, Rua dos Bragas 177, 4050-123 Porto, Portugal; E-Mails: [email protected] (B.F.); [email protected] (V.V.) 2 Departamento de Biologia, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, 4169-007 Porto, Portugal * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +351-22-340-1813; Fax: +351-22-339-0608. Received: 31 May 2012; in revised form: 9 July 2012 / Accepted: 25 July 2012 / Published: 22 August 2012 Abstract: The Cnidaria phylum includes organisms that are among the most venomous animals. The Anthozoa class includes sea anemones, hard corals, soft corals and sea pens. The composition of cnidarian venoms is not known in detail, but they appear to contain a variety of compounds. Currently around 250 of those compounds have been identified (peptides, proteins, enzymes and proteinase inhibitors) and non-proteinaceous substances (purines, quaternary ammonium compounds, biogenic amines and betaines), but very few genes encoding toxins were described and only a few related protein three-dimensional structures are available. Toxins are used for prey acquisition, but also to deter potential predators (with neurotoxicity and cardiotoxicity effects) and even to fight territorial disputes. Cnidaria toxins have been identified on the nematocysts located on the tentacles, acrorhagi and acontia, and in the mucous coat that covers the animal body. -
A Review of Toxins from Cnidaria
marine drugs Review A Review of Toxins from Cnidaria Isabella D’Ambra 1,* and Chiara Lauritano 2 1 Integrative Marine Ecology Department, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121 Napoli, Italy 2 Marine Biotechnology Department, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121 Napoli, Italy; [email protected] * Correspondence: [email protected]; Tel.: +39-081-5833201 Received: 4 August 2020; Accepted: 30 September 2020; Published: 6 October 2020 Abstract: Cnidarians have been known since ancient times for the painful stings they induce to humans. The effects of the stings range from skin irritation to cardiotoxicity and can result in death of human beings. The noxious effects of cnidarian venoms have stimulated the definition of their composition and their activity. Despite this interest, only a limited number of compounds extracted from cnidarian venoms have been identified and defined in detail. Venoms extracted from Anthozoa are likely the most studied, while venoms from Cubozoa attract research interests due to their lethal effects on humans. The investigation of cnidarian venoms has benefited in very recent times by the application of omics approaches. In this review, we propose an updated synopsis of the toxins identified in the venoms of the main classes of Cnidaria (Hydrozoa, Scyphozoa, Cubozoa, Staurozoa and Anthozoa). We have attempted to consider most of the available information, including a summary of the most recent results from omics and biotechnological studies, with the aim to define the state of the art in the field and provide a background for future research. Keywords: venom; phospholipase; metalloproteinases; ion channels; transcriptomics; proteomics; biotechnological applications 1. -
Character Evolution in Light of Phylogenetic Analysis and Taxonomic Revision of the Zooxanthellate Sea Anemone Families Thalassianthidae and Aliciidae
CHARACTER EVOLUTION IN LIGHT OF PHYLOGENETIC ANALYSIS AND TAXONOMIC REVISION OF THE ZOOXANTHELLATE SEA ANEMONE FAMILIES THALASSIANTHIDAE AND ALICIIDAE BY Copyright 2013 ANDREA L. CROWTHER Submitted to the graduate degree program in Ecology and Evolutionary Biology and the Graduate Faculty of the University of Kansas in partial fulfillment of the requirements for the degree of Doctor of Philosophy. ________________________________ Chairperson Daphne G. Fautin ________________________________ Paulyn Cartwright ________________________________ Marymegan Daly ________________________________ Kirsten Jensen ________________________________ William Dentler Date Defended: 25 January 2013 The Dissertation Committee for ANDREA L. CROWTHER certifies that this is the approved version of the following dissertation: CHARACTER EVOLUTION IN LIGHT OF PHYLOGENETIC ANALYSIS AND TAXONOMIC REVISION OF THE ZOOXANTHELLATE SEA ANEMONE FAMILIES THALASSIANTHIDAE AND ALICIIDAE _________________________ Chairperson Daphne G. Fautin Date approved: 15 April 2013 ii ABSTRACT Aliciidae and Thalassianthidae look similar because they possess both morphological features of branched outgrowths and spherical defensive structures, and their identification can be confused because of their similarity. These sea anemones are involved in a symbiosis with zooxanthellae (intracellular photosynthetic algae), which is implicated in the evolution of these morphological structures to increase surface area available for zooxanthellae and to provide protection against predation. Both -
Tentacle Morphological Variation Coincides with Differential Expression of Toxins in Sea Anemones
toxins Article Tentacle Morphological Variation Coincides with Differential Expression of Toxins in Sea Anemones Lauren M. Ashwood 1,* , Michela L. Mitchell 2,3,4,5 , Bruno Madio 6, David A. Hurwood 1,7, Glenn F. King 6,8 , Eivind A. B. Undheim 9,10,11 , Raymond S. Norton 2,12 and Peter J. Prentis 1,7 1 School of Biology and Environmental Science, Faculty of Science, Queensland University of Technology, Brisbane, QLD 4000, Australia; [email protected] (D.A.H.); [email protected] (P.J.P.) 2 Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia; [email protected] (M.L.M.); [email protected] (R.S.N.) 3 Sciences Department, Museum Victoria, G.P.O. Box 666, Melbourne, VIC 3001, Australia 4 Queensland Museum, P.O. Box 3000, South Brisbane, QLD 4101, Australia 5 Bioinformatics Division, Walter & Eliza Hall Institute of Research, 1G Royal Parade, Parkville, VIC 3052, Australia 6 Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; [email protected] (B.M.); [email protected] (G.F.K.) 7 Centre for Agriculture and the Bioeconomy, Queensland University of Technology, Brisbane, QLD 4000, Australia 8 ARC Centre for Innovations in Peptide and Protein Science, The University of Queensland, St Lucia, QLD 4072, Australia 9 Centre for Advanced Imaging, The University of Queensland, St Lucia, QLD 4072, Australia; [email protected] 10 Centre for Biodiversity Dynamics, Department of Biology, Norwegian University of Science and Technology, NO-7491 Trondheim, Norway 11 Centre for Ecological and Evolutionary Synthesis, Department of Biosciences, University of Oslo, Blindern, NO-0316 Oslo, Norway Citation: Ashwood, L.M.; Mitchell, 12 ARC Centre for Fragment-Based Design, Monash University, Parkville, VIC 3052, Australia M.L.; Madio, B.; Hurwood, D.A.; * Correspondence: [email protected] King, G.F.; Undheim, E.A.B.; Norton, R.S.; Prentis, P.J. -
New Records of Actiniarian Sea Anemones in Andaman and Nicobar Islands, India
Proceedings of the International Academy of Ecology and Environmental Sciences, 2018, 8(2): 83-98 Article New records of Actiniarian sea anemones in Andaman and Nicobar Islands, India Smitanjali Choudhury1, C. Raghunathan2 1Zoological Survey of India, Andaman and Nicobar Regional Centre, Port Blair-744 102, A & N Islands, India 2Zoological Survey of India, M-Block, New Alipore, Kolkata-700 053, India E-mail: [email protected] Received 18 December 2017; Accepted 20 January 2018; Published 1 June 2018 Abstract The present paper provides the descriptive features of three newly recorded Actiniarian sea anemones Actinoporus elegans Carlgren, 1900, Heterodactyla hemprichii Ehrenberg, 1834, Thalassianthus aster Rüppell & Leuckart, 1828 from Indian waters and two newly recorded species Stichodactyla tapetum (Hemprich & Ehrenberg in Ehrenberg, 1834), Pelocoetes exul (Annandale, 1907) from Andaman and Nicobar Islands. This paper also accounts two genera, namely Heterodactyla and Thalassianthus as new records to India waters. Keywords sea anemone; new record; distribution; Andaman and Nicobar Islands; India. Proceedings of the International Academy of Ecology and Environmental Sciences ISSN 22208860 URL: http://www.iaees.org/publications/journals/piaees/onlineversion.asp RSS: http://www.iaees.org/publications/journals/piaees/rss.xml Email: [email protected] EditorinChief: WenJun Zhang Publisher: International Academy of Ecology and Environmental Sciences 1 Introduction The actiniarian sea anemones are convened under the class Anthozoa that comprises about 1107 described species occurring in all oceans (Fautin, 2008). These benthic anemones are biologically significant animals for their promising associations with other macrobenthoes such as clown fishes, shrimps and hermit crabs (Gohar, 1934, 1948; Bach and Herrnkind, 1980; Fautin and Allen, 1992). -
1 §4-71-6.5 List of Restricted Animals [ ] Part A: For
§4-71-6.5 LIST OF RESTRICTED ANIMALS [ ] PART A: FOR RESEARCH AND EXHIBITION SCIENTIFIC NAME COMMON NAME INVERTEBRATES PHYLUM Annelida CLASS Hirudinea ORDER Gnathobdellida FAMILY Hirudinidae Hirudo medicinalis leech, medicinal ORDER Rhynchobdellae FAMILY Glossiphoniidae Helobdella triserialis leech, small snail CLASS Oligochaeta ORDER Haplotaxida FAMILY Euchytraeidae Enchytraeidae (all species in worm, white family) FAMILY Eudrilidae Helodrilus foetidus earthworm FAMILY Lumbricidae Lumbricus terrestris earthworm Allophora (all species in genus) earthworm CLASS Polychaeta ORDER Phyllodocida FAMILY Nereidae Nereis japonica lugworm PHYLUM Arthropoda CLASS Arachnida ORDER Acari FAMILY Phytoseiidae 1 RESTRICTED ANIMAL LIST (Part A) §4-71-6.5 SCIENTIFIC NAME COMMON NAME Iphiseius degenerans predator, spider mite Mesoseiulus longipes predator, spider mite Mesoseiulus macropilis predator, spider mite Neoseiulus californicus predator, spider mite Neoseiulus longispinosus predator, spider mite Typhlodromus occidentalis mite, western predatory FAMILY Tetranychidae Tetranychus lintearius biocontrol agent, gorse CLASS Crustacea ORDER Amphipoda FAMILY Hyalidae Parhyale hawaiensis amphipod, marine ORDER Anomura FAMILY Porcellanidae Petrolisthes cabrolloi crab, porcelain Petrolisthes cinctipes crab, porcelain Petrolisthes elongatus crab, porcelain Petrolisthes eriomerus crab, porcelain Petrolisthes gracilis crab, porcelain Petrolisthes granulosus crab, porcelain Petrolisthes japonicus crab, porcelain Petrolisthes laevigatus crab, porcelain Petrolisthes -
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). -
Hidden Among Sea Anemones: the First Comprehensive Phylogenetic Reconstruction of the Order Actiniaria
Hidden among Sea Anemones: The First Comprehensive Phylogenetic Reconstruction of the Order Actiniaria (Cnidaria, Anthozoa, Hexacorallia) Reveals a Novel Group of Hexacorals Estefanı´a Rodrı´guez1*, Marcos S. Barbeitos2,3, Mercer R. Brugler1,2,4, Louise M. Crowley1, Alejandro Grajales1,4, Luciana Gusma˜o5, Verena Ha¨ussermann6, Abigail Reft7, Marymegan Daly8 1 Division of Invertebrate Zoology, American Museum of Natural History, New York City, New York, United States of America, 2 Sackler Institute for Comparative Genomics, American Museum of Natural History, New York City, New York, United States of America, 3 Departamento de Zoologia, Universidade Federal do Parana´, Curitiba, Brazil, 4 Richard Gilder Graduate School, American Museum of Natural History, New York City, New York, United States of America, 5 Departamento de Zoologia, Universidade de Sa˜o Paulo, Sa˜o Paulo, Brazil, 6 Escuela de Ciencias del Mar, Pontificia Universidad Cato´lica de Valparaı´so, Valparaı´so, Chile, 7 Department of Molecular Evolution and Genomics, University of Heidelberg, Heidelberg, Germany, 8 Department of Evolution, Ecology, and Organismal Biology, Ohio State University, Columbus, Ohio, United States of America Abstract Sea anemones (order Actiniaria) are among the most diverse and successful members of the anthozoan subclass Hexacorallia, occupying benthic marine habitats across all depths and latitudes. Actiniaria comprises approximately 1,200 species of solitary and skeleton-less polyps and lacks any anatomical synapomorphy. Although monophyly is anticipated based on higher-level molecular phylogenies of Cnidaria, to date, monophyly has not been explicitly tested and at least some hypotheses on the diversification of Hexacorallia have suggested that actiniarians are para- or poly-phyletic.