Enzymes of the Cholinesterase Family

524 Pages·1995·15.99 MB·English

by  Hermona Soreq

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