Uptake in Cultured Neurones 243-4 Acetylcholine Recep

Total Page:16

File Type:pdf, Size:1020Kb

Uptake in Cultured Neurones 243-4 Acetylcholine Recep Index acetylcholine 1-3 biogenic amines 124-6 release of 3-4; responses of see also monoamines cultured neurones to 246-9; quantitative measurement of uptake in cultured neurones 129-31 243-4 black widow spider venom 272-5 acetylcholine receptor crustacean specific factors 296-8 mixed type 26; muscarinic 20-6 botulinum toxin 4 distinction between M J and M2 Bracon venom 265-7 23; drug specificity 20-6; purification oftoxins 266-7 structure of 22 abungarotoxin (BGT) 13-17, 247, nicotinic 4, 8-20 263 drug sensitivity of 11-18; effects j3bungarotoxin 261-2 of toxins on 263; genetics of butyrylcholinesterase (BuChE) 6 19-20; immunological see also cholinesterase, properties of 10-11; location acetylcholinesterase, of 8-9; on cultured neurones pseudocholinesterase 247, 249; structure of 9-11 acetylcholinesterase (AChE) 6-8 CAAT boxes 198 see also cholinesterase, cage convulsants 111 pseudocholinesterase, calcium channel toxins 260-1 butyrlcholinesterase isoenzymes calmodulin 21, 147, 155 of 7 catecholamines see monoamines aconitine 258-9 catechol-O-methyl transferase adenylate cyclase 20-1, 145, 147-50 (COMT) 139-41 adipokinetic hormone see AKH charatoxin 17 AKH 185-7, 211, 215 charybdotoxin 260 y-aminobutyric acid (GABA) 90-2 choline 8 in cultured neurones 244-6; uptake in cultured neurones 243-4 responses of cultured neurones choline acetyltransferase (ChAT) 4-5 to 249; synthesis of 93-9; antibodies to 5 uptake systems 101-5 cholinesterase (ChE) 5-8 y-aminobutyric acid receptor 105-13 see also acetylcholinesterase, bicuculline sensitivity of 107-8; pseudocholinesterase, interaction with pesticides butyry1cholinesterase 113-14; on cultured neurones ciguatoxin 260 109 COMT see catechol-O-methyl 4-aminobutyrate-2-oxoglutamate transferase transaminase (GABA-T) 99-101 conotoxins 263-2 anatoxin-a 15 crotoxin 261-2 apamin 260 crustacean hyperglycaemic hormone aromatic aminoacid decarboxylase (CHH) 212 136-8 cyclic AMP 147-50, 154-6, 211-12 cyclic GMP 150-1, 212 bag cell peptide (BCP) 195-7, 213 DARPP see dopamine and adenosine batrachotoxin 258-9 3' ;5' -monophosphate-regulated BCP see bag cell peptide phosphorylation benzodiazepine receptors 110-11 dendrotoxin 4 325 INDEX L-dopa 135-5 maitotoxin 260-1 dopamine 134-8 MAO see monoamine oxidase stimulation of adenylate cyclase N-methyl-D-aspartate (NMDA) 73, 148-9 75 dopamine and adenosine monoamine oxidase 139-42 3' :5' -monophosphate-regulated monoamines phosphorylation (DARPP) 160-1 biosynthesis of 133-9; effects of reserpine 132; inactivation of egg laying hormone see ELH 139-42; storage and release of ELH (egg laying hormone) 193-8, 131-2; synaptic location 127-9; 213 uptake systems 139 genetic aspects 194-8 MRCH (melanisation and reddish enkephalins 191 colouration hormone) 189 FMR Famide 187, 211-12, 213 nemertine venoms 300-4 . genetic aspects 199-200 nereistoxin 17 neuromodulators 126-7 G-proteins 20-1 neuronal cell culture see also acetylcholine receptor of Aplysia californica 232-3; of muscarinic Drosophila 228-30; electrical C .\BA see aaminobutyric acid properties of cells 235-8; of GABA-T see Helisoma trivolvis 230; of 4-aminobutyrate-2-oxoglutarate Hirudo medicinalis 230-2; transaminase neurite outgrowth 233-5; of GAD see glutamate decarboxylase Periplaneta americana 228-30; glutamate 42-3 synapse formation 239-43 in subcellular fractions 55-6, 63; neuronal growth factors 233-5 localisation of uptake 53-4; neuropeptidases 214-15 release of 57-65; synthesis of neuropeptides 176-7 44-8; uptake 48-58 assay of 201-3; co-localisation with glutamate decarboxylase (GAD) 94-9 other transmitters 208-9; effects invertebrate-vertebrate on cyclic AMP 211-12; families comparisons 97-8; purification of 185-7; immunochemistry of of 94-6 205-6; inactivation of 214-15; glutamate receptors 65-77 localisation of 203-5; receptors classification of 67; desensitisation for 209-11; sequencing of of 76-7; effects of toxins 264-5; 178-85 in central nervous system 68-70; neurotoxins in muscle 70-7; sub-populations species selectivity 306-8; see also of 73-4 individual toxins guanylate cyclase 150-1 nicotine 15-17 NMDA see N-methyl-D-aspartate haemocytes notexin 261-2 glutamate content of 49 haemolymph octopamine 133-7 glutamate content of 49-50 receptor sites 144, 148-50; histrionicotoxin (HTX) 11-12, 17 stimulation 0 adenylate cyclase Hydra head activating peptide 190-1 147-8; stimulation of protein inositol triphosphate 151-3,213 phosphorylation 161 insulin 188, 210-11 opioid peptides 210-11 latrotoxin 262-3, 274-5 pertussis toxin 152 326 INDEX philanthotoxin 76, 270-2 depressant 282-3; excitatory Philanthus venom 267-72 277-82 phosphatidyl inositol 20-1, 147, 151-3 mode of action 280-2 stimulated hydrolysis of 147 target site for 286-90 phosphodiesterase 20-1 sea anemone toxins 259-60 phospholipase A2 toxins 261-3 crustacean specific factors 298-300 photoreceptors 152-3 second messengers 144-6, 211-13 picrotoxin receptor 111 serotonin 138-9 potassium channel toxins 260 in cultured neurones 241, 244; proctolin 191-2, 208-9, 211, 215 receptors for 144; responses of protein kinase C 159 cultured neurones to 249-51; protein kinases 147 stimulation of adenylate cyclase Ca++ / calmodulin dependent 148 157-8; cyclic AMP dependent sodium channel toxins 257-60 153-6; cyclic GMP dependent spider toxins 76 156-7 see also black widow spider venom prothoracicotrophic hormone see synapsin 154, 157-8, 160 PTfH synaptosomes 3-4, 8, 64, 104-5, 132 pseudocholinesterase 6 see also acetylcholinesterase, taipoxin 261-2 cholinesterase TATA boxes 198 PTTH (prothoracicotrophic hormone) tetrodotoxin (TTX) 257-8 189-90 tyramine 134-7 tyramine 13 hydroxylase 138 scorpion toxins 259-60, 276-7, 284-5 chactoid group 283-4, 294-6; veratridine 258-9 crustacean specific 291-4; VIP 191, 192 327 .
Recommended publications
  • The Anxiomimetic Properties of Pentylenetetrazol in the Rat
    University of Rhode Island DigitalCommons@URI Open Access Dissertations 1980 THE ANXIOMIMETIC PROPERTIES OF PENTYLENETETRAZOL IN THE RAT Gary Terence Shearman University of Rhode Island Follow this and additional works at: https://digitalcommons.uri.edu/oa_diss Recommended Citation Shearman, Gary Terence, "THE ANXIOMIMETIC PROPERTIES OF PENTYLENETETRAZOL IN THE RAT" (1980). Open Access Dissertations. Paper 165. https://digitalcommons.uri.edu/oa_diss/165 This Dissertation is brought to you for free and open access by DigitalCommons@URI. It has been accepted for inclusion in Open Access Dissertations by an authorized administrator of DigitalCommons@URI. For more information, please contact [email protected]. THE ANXIOMIMETIC PROPERTIES OF PENTYLENETETRAZOL IN THE RAT BY GARY TERENCE SHEARMAN A DISSERTATION SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY IN PHARMACEUTICAL SCIENCES (PHARMACOLOGY AND TOXICOLOGY) UNIVERSITY OF RHODE ISLAND 19 80 DOCTOR OF PHILOSOPHY DISSERT.A.TION OF GARY TERENCE SHEAffiil.AN Approved: Dissertation Cormnittee \\ Major Professor ~~-L_-_._dd__· _... _______ _ -~ar- Dean of the Graduate School UNIVERSITY OF RHODE ISLAND 1980 ABSTRACT Investigation of the biological basis of anxiety is ham­ pered by the lack of an appropriate animal model for research purposes. There are no known drugs that cause anxiety in laboratory animals. Pentylenetetrazol (PTZ) produces intense anxiety in human volunteers (Rodin, 1958; Rodin and Calhoun, 1970). Therefore, it was the major objective of this disser- tation to test the hypothesis that the discriminative stimu­ lus produced by PTZ in the rat was related to its anxiogenic action in man. It was also an objective to suggest the neuro- chemical basis for the discriminative stimulus property of PTZ through appropriate drug interactions.
    [Show full text]
  • ARTICLE Using Tinbergen's Four Questions As the Framework for A
    The Journal of Undergraduate Neuroscience Education (JUNE), Fall 2015, 14(1):A46-A55 ARTICLE Using Tinbergen’s Four Questions as the Framework for a Neuroscience Capstone Course John Meitzen Department of Biological Sciences, W.M. Keck Center for Behavioral Biology, Center for Human Health and the Environment, Center for Comparative Medicine and Translational Research, North Carolina State University, Raleigh, NC 27695. Capstone courses for upper-division students are a ultimate/evolutionary view, providing an excellent base common feature of the undergraduate neuroscience upon which to teach students an integrative approach to curriculum. Here is described a method for adapting understanding neuroscientific phenomena. For example, a Nikolaas Tinbergen’s four questions to use as a framework particular neurotoxin can be examined from the proximate for a neuroscience capstone course, in this case with a level (i.e., mechanism: how does this toxin specifically particular emphasis on neurotoxins. This course is impact neural physiology) to the ultimate/evolutionary level intended to be a challenging opportunity for students to (i.e., adaptation: why and to what extent did this toxin integrate and apply knowledge and skills gained from their evolve naturally or the reason that it was initially invented major study, a B.S. in Biological Sciences with a by humans). The mechanics, goals, and objectives of the Concentration in Integrative Physiology and Neurobiology. course are presented as we believe that it will serve as a In particular, a broad, integrative approach is favored, with flexible and useful model for neuroscience capstone emphasis placed on primary literature, scientific process courses concerning a wide variety of topics across multiple and effective, professional communication.
    [Show full text]
  • Neurotoxins from Snake Venom Mojave Toxin from Crotalus Scututa- Tus Is Also Structurally Similar to Crotoxin Anthony T
    BIOLOGICALLY ACTIVE AGENTS IN NATURE 56 CHIMIA 52 (1998) NT. 1/2 (lnnu'T/FehruaT) Chimia 52 (1998) 56-62 and also on the postsynaptic membrane © Neue Schweizerische Chemische Gesellschaft [7], in addition to the presynaptic binding ISSN 0009-4293 site. From a structural viewpoint, both subunits A and B are in the isoforms [8a- c]. Neurotoxins from Snake Venom Mojave toxin from Crotalus scututa- tus is also structurally similar to crotoxin Anthony T. Tu* and is composed of two subunits [9a, b]. There are considerable amino-acid se- quence homologies between the two tox- Abstract. Found within snake venoms are a variety oftoxic and nontoxic proteins. The ins [lOa, b]. Mojave toxin inhibits calci- effects of snake venoms depend on all of the components of that venom. However, the um-channel dihydropyridine receptor bind- lethal effects are usually related to the most potent toxins found within the venom; the ing in rat brain [1 I]. two most toxic proteins found in snake venom are neuro- and cardiotoxins. This article Crotoxin's neurotoxic action is very reviews a variety of neurotoxins found in snake venom. The range of neurotoxins similar to t3-btx, but has some difference. present in snake venom is varied and includes: peripheral and noncentral, presynaptic, For instance, crotoxin and its subunit B postsynaptic, potassium-channel inhibiting, muscarinic transmission inhibiting, and have a postsynaptic effect, whereas t3-btx anticholinesterase types. has no such activity [7]. The acidic and basic subunit-types pre- Because a snake venom contains many turn causes the exocytosis of the nerve synaptic toxins are fairly common in neu- different proteins, some are highly toxic, transmitter.
    [Show full text]
  • Natural Neurotoxins with Targeting T0 Cholinergic Nervous System (Cholinotoxins)
    22 VOJENSKÉ ZDRAVOTNICKÉ LISTY - SUPLEMENTUM VOLUME LXVII, 1998, no. 2 NATURAL NEUROTOXINS WITH TARGETING T0 CHOLINERGIC NERVOUS SYSTEM (CHOLINOTOXINS) Jiří PATOČKA Department of Toxicology, Purkyně Military Medical Academy, Hradec Králové Summary Cholinergic nervous system plays an important røle in many physiological and behavioral functions in all animals. The activity of central and peripheral nervous system depends on the production and fate of acetylcholine and all compounds influenced its biosynthesis, storage, release, hydrolysis, and interactions with different subtypes of acetylcholine both muscarinic and nicotinic receptors. Many natural neurotoxins also interact with different parts of cholinergic nervous system and these compounds are the aim of this review. KEY WORDS: Cholinergic nervous system; Alkaloids; Animal venoms; Neurotoxins. 1. Introduction purposes by native civilizations in all continents. Toxins of venomous animals as for instance snakes, Natural toxins are chemical agents of biological scorpions, spiders, bees etc., have fascinated origin, present in the bodies of some organisms or mankind because of their dramatic toxic effect on in the special glands which product venom. Toxins other animals. These poisons are used by the have evolved in microorganisms, fungi, plants and animals for protection against predators or for animals over many thousands of years to have capturing prey and very often affect their nervous specific and unique effects. Venoms from different system (neurotoxins). Many venoms have multiple toxic plants are known and used for different components or toxins that lead toa complicated VOLUME LXVII, 1998, no. 2 VOJENSKE ZDRAVOTNICKÉ LISTY - SUPLEMENTUM › 23 clinical picture. The toxicity of many toxins is very Arecoline high, very often comparable with chemical warfare agents, and they may be dangerous for humans.
    [Show full text]
  • Lawrence Berkeley National Laboratory Recent Work
    Lawrence Berkeley National Laboratory Recent Work Title EFFECTS OF CHANGES IN AROUSAL ON AMNESIA INDUCED BY INHIBITION OF BRAIN PROTEIN SYNTHESIS Permalink https://escholarship.org/uc/item/44p749mf Author Flood, James F. Publication Date 1976-06-01 eScholarship.org Powered by the California Digital Library University of California 0 \) J ,-J 0 J v '1 J Submitted to Physiology and Behavior LBL-5302 Preprint C. \ EFFECTS OF CHANGES IN AROUSAL ON AMNESIA INDUCED BY INHIBITION OF BRAIN PROTEIN SYNTHESIS James F. Flood, Murray E. Jarvik, Edward L. Bennett, Ann E. Orme, and Mark R. Rosenzweig June 7, 1976 Prepared for the U. S. Energy Research and Development Administration under Contract W -7405-ENG-48 for Reference Not to be taken from this room t"" b:l t"" I \.)1 w I"} 0 -. N DISCLAIMER This document was prepared as an account of work sponsored by the United States Government. While this document is believed to contain coiTect information, neither the United States Government nor any agency thereof, nor the Regents of the University of California, nor any of their employees, makes any waiTanty, express or implied, or assumes any legal responsibility for the accuracy, completeness, or usefulness of any information, apparatus, product, or process disclosed, or represents that its use would not infringe privately owned rights. Reference herein to any specific commercial product, process, or service by its trade name, trademark, manufacturer, or otherwise, does not necessarily constitute or imply its endorsement, recommendation, or favoring by the United States Government or any agency thereof, or the Regents of the University of California.
    [Show full text]
  • Interaction of the Neurotoxic and Nontoxic Secretory Phospholipases A2 with the Crotoxin Inhibitor from Crotalus Serum
    Eur. J. Biochem. 267, 4799±4808 (2000) q FEBS 2000 Interaction of the neurotoxic and nontoxic secretory phospholipases A2 with the crotoxin inhibitor from Crotalus serum Grazyna Faure1, Christina Villela2, Jonas Perales2 and Cassian Bon1 1Unite des Venins, Institut Pasteur, Paris, France;2Departamento de Fisiologia e FarmacodinaÃmica, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brasil Crotalus durissus terrificus snakes possess a protein in their blood, named crotoxin inhibitor from Crotalus serum (CICS), which protects them against crotoxin, the main toxin of their venom. CICS neutralizes the lethal potency of crotoxin and inhibits its phospholipase A2 (PLA2) activity. The aim of the present study is to investigate the specificity of CICS towards snake venom neurotoxic PLA2s(b-neurotoxins) and nontoxic mammalian PLA2s. This investigation shows that CICS does not affect the enzymatic activity of pancreatic and nonpancreatic PLA2s, bee venom PLA2 and Elapidae b-neurotoxins but strongly inhibits the PLA2 activity of Viperidae b-neurotoxins. Surface plasmon resonance and PAGE studies further demonstrated that CICS makes complexes with monomeric and multimeric Viperidae b-neurotoxins but does not interact with nontoxic PLA2s. In the case of dimeric b-neurotoxins from Viperidae venoms (crotoxin, Mojave toxin and CbICbII), which are made by the noncovalent association of a PLA2 with a nonenzymatic subunit, CICS does not react with the noncatalytic subunit, instead it binds tightly to the PLA2 subunit and induces the dissociation of the heterocomplex. In vitro assays performed with Torpedo synaptosomes showed a protective action of CICS against Viperidae b-neurotoxins but not against other PLA2 neurotoxins, on primary and evoked liberation of acetylcholine.
    [Show full text]
  • Chapter 18 TOXINS from VENOMS and POISONS
    Toxins From Venoms and Poisons Chapter 18 TOXINS FROM VENOMS AND POISONS SCOTT A. WEINSTEIN, PhD, MD,* and JULIAN WHITE, MD† INTRODUCTION SOME DEFINITIONS: VENOMS, TOXINS, AND POISONS NONWARFARE EPIDEMIOLOGY OF VENOM-INDUCED DISEASES AND RELATED TOXINS Venomous Bites and Stings Venomous Snakes Scorpions, Spiders, and Other Arachnids Insects Marine Envenoming: Sea Snakes, Cnidarians, and Venomous Fish Poisoning by Animals, Plants, and Mushrooms Relevance to Biological Warfare MAJOR TOXIN CLASSES AND THEIR CLINICAL EFFECTS Paralytic Neurotoxins Excitatory Neurotoxins Myotoxins Hemostasis-Active Toxins Hemorrhagic and Hemolytic Toxins Cardiotoxins Nephrotoxins Nectrotoxins Other Toxins CONCLUSIONS AND DIRECTIONS FOR RESEARCH *Physician, Toxinologist, Toxinology Division, Women’s & Children’s Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia †Head of Toxinology, Toxinology Division, Women’s & Children’s Hospital, 72 King William Road, North Adelaide, South Australia 5006, Australia 415 Bio Ch 18 - mark EEI - pp415-460.indd 415 6/21/18 1:02 PM Medical Aspects of Biological Warfare INTRODUCTION This chapter considers toxins that might be ex- venom-derived toxins have not generally been con- ploited as offensive biological weapons, or that may sidered suitable for use as a mass offensive weapon; have medical relevance to deployed military per- however, primarily fungal- or plant-derived toxins sonnel. The major characteristics of important toxin certainly have been weaponized (eg, ricin; see chapter classes are summarized, and their medical effects are 16). Using venoms as a weapon is also obviously dis- covered. Venom toxins are emphasized because little tinct from the weaponization of toxins from bacteria. information is available about venomous animals in However, many toxins found in animals, plants, relation to military medicine.
    [Show full text]
  • Toxicon 60 (2012) 95–248
    Toxicon 60 (2012) 95–248 Contents lists available at SciVerse ScienceDirect Toxicon journal homepage: www.elsevier.com/locate/toxicon 17th World Congress of the International Society on Toxinology & Venom Week 2012 Honolulu, Hawaii, USA, July 8–13, 2012 Abstract Editors: Steven A. Seifert, MD and Carl-Wilhelm Vogel, MD, PhD 0041-0101/$ – see front matter 10.1016/j.toxicon.2012.04.354 96 Abstracts Toxins 2012 / Toxicon 60 (2012) 95–248 Abstracts Toxins 2012 Contents A. Biotoxins as Bioweapons. ...............................................................................97 B. Drug Discovery & Development..........................................................................100 C. Evolution of Toxins & Venom Glands . .....................................................................119 D. Hemostasis. ......................................................................................128 E. History of Toxinology . ..............................................................................137 F. Insects . ...........................................................................................141 G. Marine . ...........................................................................................144 H. Microbial Toxins. ..................................................................................157 I. Miscellaneous . ......................................................................................164 J. Pharmacology . ......................................................................................165 K. Physiology
    [Show full text]
  • UNIVERSITY of CALIFORNIA, SAN DIEGO Cell
    UNIVERSITY OF CALIFORNIA, SAN DIEGO Cell Membrane-Cloaked Nanoparticles for Targeted Therapeutics A dissertation submitted in partial satisfaction of the requirements for the degree Doctor of Philosophy in Bioengineering by Brian Tsengchi Luk Committee in charge: Professor Liangfang Zhang, Chair Professor Shu Chien, Co-Chair Professor Michael J. Heller Professor Andrew C. Kummel Professor Dong-Er Zhang 2016 © Brian Luk, 2016 All rights reserved The Dissertation of Brian Tsengchi Luk is approved, and it is acceptable in quality and form for publication on microfilm and electronically: Co-Chair Chair University of California, San Diego 2016 iii DEDICATION This dissertation is dedicated to all those who have helped me reach this point in my life—from teachers to coaches to friends and colleagues; all have been a mentor to me in some shape or form. Without them, reaching this point would have been an impossibility, and I am eternally grateful for the support and guidance each person has provided. A special thanks goes to my loving family, who have supported me in all my endeavors and never cease to push me to be the person they know I can be. iv EPIGRAPH Nature composes some of her loveliest poems for the microscope and the telescope. Theodore Roszak v TABLE OF CONTENTS Signature Page ............................................................................................................... iii Dedication ...................................................................................................................... iv Epigraph
    [Show full text]
  • Potential Military Chemical/ Biological Agents and Compounds
    Army Field Manual No 3-9 Navy Publication No P-467 Air Force Manual No 355-7 Potential Military Chemical/ Biological Agents and Compounds Headquarters Department of the Army Department of the Navy Department of the Air Force Washington, DC, 12 December 1990 PCN 320 008457 00 FM 3-9 Preface This field manual provides commanders and The proponent of this publication is Head- staffs with general information and technical quarters, TRADOC. Submit recommended data concerning chemical and biological changes for improving this publication on DA agents and other compounds of military inter- Form 2028 (Recommended Changes to Publi- est. It discusses the use; the classification; and cations and Blank Forms) and forward it to the physical, chemical, and physiological Commandant, US Army Chemical School, properties of these agents and compounds. It ATTN: ATZN-CM-NF, Fort McClellan, AL also discusses protection and decontamination 36205-5020. Send applicable Air Force com- of these agents. In addition, it discusses their ments by letter to HQ, USAF/XOOTM, symptoms and the treatment of those Washington, DC 20330-5054. symptoms. 2 *FM 3-9 • NAVFAC P-467 • AFR 355-7 1 FM 3-9 2 United States Policy Biological Agents – No Use 1. The United States will not use biological agents, including toxins and all other methods of biological warfare, under any circumstances. 2. The United States will strictly limit biological research to defensive measures. Chemical Agents – No First Use 1. US armed forces will not use lethal or incapacitating chemical agents first. 2. The United States will strictly reserve the right to retaliate, using lethal or incapacitating chemical agents, against an enemy force that has used them on US forces.
    [Show full text]
  • Secreted Phospholipases A2 of Snake Venoms
    Toxins 2013, 5, 2533-2571; doi:10.3390/toxins5122533 OPEN ACCESS toxins ISSN 2072-6651 www.mdpi.com/journal/toxins Review Secreted Phospholipases A2 of Snake Venoms: Effects on the Peripheral Neuromuscular System with Comments on the Role of Phospholipases A2 in Disorders of the CNS and Their Uses in Industry John B. Harris 1,†,* and Tracey Scott-Davey 2 1 Medical Toxicology Centre and Institute of Neurosciences, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK 2 Experimental Scientific Officer, Electron Microscopy Unit, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK; E-Mail: [email protected] † Emeritus professor of experimental neurology. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +44-191-222-6442 or +44-191-285-4913. Received: 8 October 2013; in revised form: 2 December 2013 / Accepted: 10 December 2013 / Published: 17 December 2013 Abstract: Neuro- and myotoxicological signs and symptoms are significant clinical features of envenoming snakebites in many parts of the world. The toxins primarily responsible for the neuro and myotoxicity fall into one of two categories—those that bind to and block the post-synaptic acetylcholine receptors (AChR) at the neuromuscular junction and neurotoxic phospholipases A2 (PLAs) that bind to and hydrolyse membrane phospholipids of the motor nerve terminal (and, in most cases, the plasma membrane of skeletal muscle) to cause degeneration of the nerve terminal and skeletal muscle. This review provides an introduction to the biochemical properties of secreted sPLA2s in the venoms of many dangerous snakes and a detailed discussion of their role in the initiation of the neurologically important consequences of snakebite.
    [Show full text]
  • Chemical Hygiene Plan 2015 (Revision 9)
    Chemical Hygiene Plan 2015 (Revision 9) Dartmouth College Environmental Health and Safety Arts and Sciences Geisel School of Medicine Thayer School of Engineering This document must be readily available in all Dartmouth teaching and research laboratories using hazardous chemicals Policy Chemical Hygiene Plan Page: 1 Written by: Michael D. Cimis Revision date: 11/17/15 Dartmouth College Chemical Hygiene Plan Table of Contents INTRODUCTION: 4 SELECTED DEFINITIONS 5 1) FLAMMABLE AND COMBUSTIBLE LIQUIDS 5 2) CORROSIVES 6 3) REACTIVES 6 4) TOXIC MATERIALS 6 REGULATORY BACKGROUND: 8 SCOPE: 8 RESPONSIBILITIES: 8 MINORS AND VOLUNTEERS WORKING IN LABORATORIES: 9 REGISTRATION OF HAZARDOUS CHEMICAL WORK WITH EHS 9 MINIMUM REQUIREMENTS IN DARTMOUTH COLLEGE LABORATORIES: 10 ADMINISTRATIVE CONTROLS: 10 “DESIGNATED AREA” AND FACILITY CONTROLS: 10 PERSONNEL CONTROLS 11 INFORMATION AND TRAINING: 12 SAFETY DATA SHEETS: 12 LABELING CONTAINERS IN THE LABORATORY 12 PERSONAL PROTECTIVE EQUIPMENT: 13 SAFE STORAGE AND DISPOSAL OF HAZARDOUS CHEMICALS: 14 EMERGENCY PROCEDURES: 14 CHEMICAL SPILLS: 14 REPORTING A CHEMICAL SPILL: 15 FIRST AID FOR CHEMICAL CONTAMINATION: 15 PROCEDURES FOR POWER OUTAGES OR SERVICE INTERRUPTIONS: 16 AIR MONITORING & EXPOSURES TO HAZARDOUS CHEMICALS: 16 SPECIAL NOTE ON PREGNANCY: 16 Policy Chemical Hygiene Plan Page: 2 Written by: Michael D. Cimis Revision date: 11/17/15 MEDICAL CONSULTATION: 17 SERVICES PROVIDED BY EHS: 17 SERVICES PROVIDED BY FACILITIES: 17 WORKING WITH PARTICULARLY HAZARDOUS SUBSTANCES: 17 REGULATED CARCINOGENS 18
    [Show full text]