Enzymes of the Cholinesterase Family PDF
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Enzymes of the Cholinesterase Family Enzymes of the Cholinesterase Family Edited by Daniel M. Quinn University of Iowa Iowa City, Iowa A. S. Balasubramanian Christian Medical College and Hospital Vellore, Tamil Nadu, India Bhupendra P. Doctor Walter Reed Army Institute of Research Washington, D.C. and Palmer Taylor University of California at San Diego La Jolla, California Springer Science+Business Media, LLC Library of Congress Cataloglng-ln-PublIcatIon Data Enzymes of the Cholinesterase family / edited by Daniel M. Quinn ... [et al.]. p. cm. "Proceedings of the Fifth International Meeting on Choiinesterases, held September 24-28, 1994, in Madras, India"—T.p. verso. Includes bibliographical references and index. ISBN 978-1-4899-1053-0 1. Choiinesterases—Congresses. I. Quinn, Daniel M. II. International Meeting on Choiinesterases (5th : 1994 : Madras, India) [DNLM: 1. Acetylcholinesterase—metabolism—congresses. 2. ButyrylcholInesterase—metabolism—congresses. QU 136E611 1995] QP609.C4E56 1995 574. 19'253~dc20 DNLM/DLC for Library of Congress 95-39179 CIP Front cover: A model of the complex between the snake venom toxin fasciculin (light color) and acetylcholinesterase (dark color), constructed by H.K.L. van den Born et ai [(1995) Protein Science 4, 703—715]. Photography by Z. Radie of the University of California at San Diego. Proceedings of the Fifth International Meeting on Cholinesterases, held September 24-28, 1994, in Madras, India ISBN 978-1-4899-1053-0 ISBN 978-1-4899-1051-6 (eBook) DOI 10.1007/978-1-4899-1051-6 © Springer Science+Business Media New York 1995 Originally published by Plenum Press, New York in 1995 Softcover reprint of the hardcover 1st edition 1995 All rights reserved 1098765432 1 No part of this book may be reproduced, stored in a retrieval system, or transmitted in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher PREFACE The Fifth International Meeting on Cholinesterases convened in Madras, India, in September of 1994. The long and rich history and culture of India provided an excellent setting for the meeting. More than 120 delegates from Asia, Australia, Europe and North America heard 54 oral presentations and viewed 54 posters on current research on enzymes of the cholinesterase family. The aim of this book is to compile the presentations of the Fifth International Meeting on Cholinesterases into a volume that describes recent investigations on the structure and catalytic function of acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) and related enzymes, as well as studies on the molecular and cellular biology of these enzymes and the genes which encode them. Cholinesterases enjoy a long and storied history in diverse areas. In basic biochemical research, AChE is one of the best studied, though yet enigmatic, of enzymes. The efficient catalytic function of this enzyme presents the biochemist with a fundamental challenge in understanding the relationship between structure and function. AChE and BuChE belong to a family of proteins, the alB hydrolase fold family, whose constituents evolutionarily diverged from a common ancestor. Proteins in this family have a wide range of physiological functions. In commerce, AChE is a prime target for agricultural insect control, and for the development of therapeutic agents for Alzheimer's disease. On the national security front, AChE is the target of chemical warfare agents, "nerve gases," which pose a threat on the battlefield of nations at war and in the city centers of nations at peace. Recent events, chronicled in the international news media, provide a stark reminder of this fact. The broad reach of cholinesterase function and research affects the biological scientist and nonscientist alike. From biotechnology to the military, one is hard pressed to find a family of enzymes whose effect on the human condition is more pervasive. Various presentations at the meeting described structure-activity relationships for the interaction of cholinesterases with toxic organophosphorus agents. Novel efforts at antidotal therapy were described that aim to use cholinesterases in the presence of nucleophilic oximes to detoxify organophosphorus inhibitors. Strategies for effective inhibition of acetylcholinesterase in the central nervous system, as an approach to the treatment of the cognitive dis functions associated with Alzheimer's disease, were described, as were the structure-activity relation ships of new anti-Alzheimer's agents. The cell and molecular biology of cholinesterases is advancing rapidly. The relation ships between AChE gene structure and the various molecular forms of the enzyme were described at the meeting, as were the mechanisms of gene expression, cellular biosynthesis, and assembly of the cholinesterases. Various noncatalytic roles for cholinesterases were described, which include involvement in nervous system development and in neurotrans mission involving dopamine-containing nerve terminals. v vi Preface Reports of structure-function relationships not only described the fine detail that is emerging on the structural basis of the rapid catalytic mechanisms effected by choli nesterases, but also provided the bases for several controversies. X-ray crystallography of catalytically relevant ligand complexes with AChE provided visual verification of the roles, suggested by site-directed mutagenesis and other studies, for loci in the active site that are responsible for acyl group specificity, quaternary ammonium recognition, oxyanion recog nition and acid-base catalysis. The crystal structure of AChE provided the template for theoretical evaluation ofthe role of the electrical field of the enzyme in ligand binding. Good spirited controversies arose on whether the electrical field of the enzyme plays a significant role in the rapidity of AChE catalysis, and whether an anthropomorphic "back door" mechanism is required for release of cationic products. This Preface outlines just a fraction of the wide range of topics discussed at the Fifth International Meeting on Cholinesterases in Madras, India. The chapters that follow provide a clear view of the breadth and vigor of research on enzymes of the cholinesterase family. The meeting in Madras was a once in a lifetime opportunity for an international delegation to discuss and debate such research in a congenial atmosphere. Our Indian hosts are to be commended for the graciousness and organizational effort that were key to the success of the meeting. Daniel M. Quinn A. s. Balasubramanian Bhupendra P. Doctor Palmer Taylor CONTENTS Part I. GENE STRUCTURE AND EXPRESSION OF CHOLINESTERASES A. Presentations Antisense Oligonucleotides Suppressing Expression of Cholinesterase Genes Modulate Hematopoiesis in Vivo and ex Vivo ....................... . Hermona Soreq, Efrat Lev-Lehman, Deborah Patinkin, Mirta Grifman, Gal Ehrlich, Dalia Ginzberg, Fritz Eckstein, and Haim Zakut Properties of Class A Acetylcholinesterase, the Enzyme Encoded by ACE-I in Caenorhabditis elegans . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7 Martine Arpagaus, Nathalie Schirru, Emmanuel Culetto, Vincenzo Talesa, Xavier Cousin, Arnaud Chatonnet, Yann Fedon, Jean-Baptiste Berge, Didier Fournier, and Jean-Pierre Toutant Ligand Specificity and Gene Expression in the Cholinergic Synapse: A Comparison between Acetylcholinesterase and the Nicotinic Acetylcholine Receptor.. 15 Palmer Taylor, Zoran Radic, Hans-JUrgen Kreienkamp, Zhigang Luo, Natilie A. Pickering, and Shelley Camp Butyrylcholinesterase Transcription Start Site and Promoter ..................... 23 Omar Jbilo, Jean-Pierre Toutant, Arnaud Chatonnet, and Oksana Lockridge The C-Terminal Alternative Regions of Acetylcholinesterase. . . . . . . . . . . . . . . . . . . .. 29 Jean Massoulie, Alain Anselmet, Suzanne Bon, Fran<,:oise Coussen, Eric Krejci, and Claire Legay Developmental Expression of Acetylcholinesterase in Skeletal Muscle. . . . . . . . . . . .. 37 Zoran Grubic and Armand F. Miranda vii viii Contents B. Posters Alternative Exon 6 Directs Synaptic Localization of Recombinant Human Acetylcholinesterase in Neuromuscular Junctions of Xenopus laevis Embryos ..................................................... 45 Meira Sternfeld, Shlomo Seidman, Revital Ben Aziz-Aloya, Michael Shapira, Rina Timberg, Daniela Kaufer, and Hermona Soreq Developmental Regulation of Acetylcholinesterase mRNA in the Mouse Diaphragm: Alternative Splicing and Focalization ............................. 47 Claire Legay, Monique Huchet, Jean Massoulit\ and Jean-Pierre Changeux Acetylcholinesterase and Butyrylcholinesterase Expression in Adult Rabbit Tissues and during Development . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 49 Omar Jbilo, Yann L'Hermite, Vincenzo Talesa, Jean-Pierre Toutant, and Arnaud Chatonnet Mutations in the Catalytic Subunit of Acetylcholinesterase Do Not Appear Responsible for Congenital Myasthenic Syndrome Associated with End-Plate Acetylcholinesterase Deficiency ......................... 51 S. Camp, A. G. Engel, D. K. Getman, S. Bon, J. Massoulie, and P. Taylor Regulation of Acetylcholinesterase (AChE) mRNA by Ryanodine-Sensitive and L-Type Calcium Channels during Myogenesis in Vitro and Muscle Development in Vivo ........................................... 53 Zhigang Luo, Martine Pincon-Raymond, and Palmer Taylor Regulation of AChE Gene Expression in Neuronally Induced Mouse P19 Cells. . . . .. 55 B. A. Coleman and P. Taylor Regulation of Human Acetylcholinesterase Gene Expression. . . . . . . . . . . . . . . . . . . .. 56 D. Getman, K. Inoue, and P. Taylor Promoter Elements of the Mouse Acetylcholinesterase Gene: Regulation during Muscle Differentiation ......................................... 57 Annick Mutero and Palmer Taylor Part II. POLYMORPHISM AND STRUCTURE OF CHOLINESTERASES A. Presentations Structures of Complexes of Acetylcholinesterase with Covalently and Non-Covalently Bound Inhibitors ................................ 59 J. L. Sussman, M. Harel, M. Raves, D. M. Quinn, H. K. Nair, and I. Silman Electrostatic Properties of Human Acetylcholinesterase. . . . . . . . . . . . . . . . . . . . . . . .. 67 Daniel R. Ripoll, Carlos H. Faerman, Richard Gillilan, Israel Silman, and Joel L. Sussman Contents ix Substrate Binding Site and the Role of the FLAP Loop in Candida rugosa Lipase, a Close Relative of Acetylcholinesterase. . . . . . . . . . . . . . . . . . . . . . . . . . . .. 71 Miroslaw Cygler, Pawel Grochulski, and Joseph D. Schrag Studies on Partially Unfolded States of Torpedo californica Acetylcholinesterase 77 Israel Silman, David I. Kreimer, Irina Shin, Elena A. Dolginova, Ester Roth, Daniella Goldfarb, Reuven Szosenfogel, Mia Raves, Joel L. Sussman, Nina Borochov, and Lev Weiner FTIR-Spectroscopic Investigations of the Structure and Temperature Stability of the Acetylcholinesterase from Torpedo californica .. . . . . . . . . . . . . . . . . . . .. 83 Ferdinand Hucho, Dieter Naumann, and Ute Gome-Tschelnokow Residues in the C-Terminus of Torpedo californica Acetylcholinesterase Important for Modification into a Glycophospholipid Anchored Form . . . . . . . . . . .. 89 Goran Bucht, Lena Lindgren, and Karin Hjalmarsson Computer Modeling of Acetylcholinesterase and Acetylcholinesterase-Ligand Complexes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 97 S. T. Wlodek, J. Antosiewicz, M. K. Gilson, 1. A. McCammon, T. W. Clark, and L.R. Scott Structural Analysis of the Asparagine-Linked Oligosaccharides ofCholinesterases: N-Linked Carbohydrates of Cholinesterases ........................ 105 Ashima Saxena and B. P. Doctor Pressure Effects on Structure and Activity of Cholinesterase ..................... 113 P. Masson and C. Clery B. Posters Hydrophobicity on Esterase Activity of Human Serum Cholinesterase ............. 123 L. Jaganathan, K. Padmalatha, G. Revathi, and R. Boopathy Alterations in the Topography of Acetylcholinesterase Active Site Gorge after Binding of Peripheral Anionic Site Ligands ......................... 125 Anton Stalc, Zoran Grubic, Marjeta Sentjurc, Slavko Pecar , Mary K. Gentry, and Bhupendra P. Doctor Acetylcholinesterase from Octopus vulgaris (Cephalopoda): Evidence for a Specific High Salt-Soluble and Heparin-Soluble Fraction of Globular Forms ..... 127 Vincenzo Talesa, Marta Grauso, Elvio Giovannini, Gabriella Rosi, and Jean-Pierre Toutant Molecular Polymorphism of Acetylcholinesterase in Hirudo medicinalis ........... 128 Vincenzo Talesa, Marta Grauso, Elvio Giovannini, Gabriella Rosi, and Jean-Pierre Toutant Subunit Association and Stabilization of Butyrylcholinesterase (BChE) ............ 129 R. M. Blong, P. Masson, and O. Lockridge x Contents Denaturation of Recombinant Human Acetylcholinesterase ...................... 131 M. Lebleu, C. Clery, P. Masson, S. Reuveny, D. Marcus, B. Velan, and A. Shafferman Part III. MECHANISM OF CATALYSIS OF CHOLINESTERASES A. Presentations Amino Acid Residues that Control Mono-and Bisquatemary Oxime-Induced Reactivation of O-Ethyl Methylphosphonylated Cholinesterases ........ 133 Y. Ashani, Z. Radic, I. Tsigelny, D. C. Vellom, N. A Pickering, D. M. Quinn, B. P. Doctor, and P. Taylor Modulation of Catalysis and Inhibition of Fetal Bovine Serum Acetylcholinesterase by Monoclonal Antibodies ...................................... 141 B. P. Doctor, Mary K. Gentry, Ashima Saxena, and Yacov Ashani Insect Acetylcholinesterase and Resistance to Insecticides ....................... 149 Didier Fournier, Marie Maturano, Laurent Gagnoux, Philippe Ziliani, Cyril Pertuy, Madeleine Pralavorio, Jean-Marc Bride, Leila Elmarbouh, Alain Klaebe, and Patrick Masson Phosphonate Ester Active Site Probes of Acetylcholinesterase, Trypsin and Chymotrypsin ................................................ 155 Akos Bencsura, Istvan Enyedy, Carol Viragh, Rinat Akhmetshin, and Ildiko M. Kovach Irreversible Site-Directed Labeling Studies on Cholinesterases ................... 163 L. Ehret-Sabatier, I. Schalk, C. Loeb, F. Nachon, and M. Goeldner Mutation of Human Butyrylcholinesterase Glycine 117 to Histidine Preserves Activity but Confers Resistance to Organophosphorus Inhibitors ....... 169 C. A Broomfield, C. B. Millard, o. Lockridge, and T. L. Caviston Reaction of Acetylcholinesterase with Organophosphonates: Molecular Fate at the Rim of a Gorge ............................................... 177 Harvey Alan Berman Amino Acid Residues in Acetylcholinesterase which Influence Fasciculin Inhibition .. 183 Zoran Radic, Daniel M. Quinn, Daniel C. Vellom, Shelley Camp, and Palmer Taylor Molecular Aspects of Catalysis and of Allosteric Regulation of Aceytlcholinesterases 189 A. Shaffe rman, AOrdentlich, D. Barak, C. Kronman, N. Ariel, M. Leitner, Y. Segall, A. Bromberg, S. Reuveny, D. Marcus, T. Bino, A. Lazar, S. Cohen, and B.Velan
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