Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors

268 Pages·1990·10.04 MB·English

by  Moseley Waite (auth.)

BIOCHEMISTRY~
MOLECULAR
BIOLOGY~
AND PHYSIOLOGY OF
PHOSPHOLIPASE A2
AND ITS
REGULATORY FACTORS
ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY
Editorial Board:
NATHAN BACK, State University of New York at Buffalo
IRUN R. COHEN, The Weizmann Institute of Science
DAVID KRITCHEVSKY, Wistar Institute
ABEL LAJTHA, N.S. Kline Institute for Psychiatric Research
RODOLFO PAOLETTI, University of Milan
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BIOCHEMISTRY,
MOLECULAR BIOLOGY,
AND PHYSIOLOGY OF
PHOSPHOLIPASE A2
AND ITS
REGULATORY FACTORS
Edited by
Anil B. Mukherjee
National Institute of Child Health and Human Development/
National Institutes of Health
Bethesda, Maryland
PLENUM PRESS • NEW YORK AND LONDON
Library of Congress Cataloging in Publication Data
Biochemistry, molecular biology, and physiology of phospholipase A2 and its
regulatory factors / edited by Ani! B. Mukherjee.
p. cm. - (Advances in experimental medicine and biology; v. 279)
Proceedings of a symposium held Sept. 19-20, 1989, in Bethesda, Md.
Includes bibliographical references.
Includes index.
ISBN-13: 978-1-4612-7910-5 e-ISBN-13: 978-1-4613-0651-1
DOl: 10.1007/978-1-4613-0651-1
I. Phospholipase A2 - Congresses. 2. Phospholipase A2 - Mechanism of action
Congresses. 3. Phospholipase A2 - Inhibitors-Congresses. I. Mukherjee, Ani! B.
[DNLM: I. Phospholipases-antagonists & inhibitors-congresses. 2. Phospho
lipases-physiology-congresses. WI AD559 v. 279 I QU 136 B6143 1989]
QP609.P553B56 1990
612'.01513-dc20
DNLM/DLC 90-14266
for Library of Congress CIP
Proceedings of a symposium on Biochemistry, Molecular Biology,
and Physiology of Phospholipase A2 and Its Regulatory Factors,
held September 19-20, 1989, in Bethesda, Maryland
© 1990 Plenum Press, New York
Softcover reprint of the hardcover 1s t edition 1990
A Division of Plenum Publishing Corporation
233 Spring Street, New York, N.Y. 10013
All rights reserved
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
During the past decade there has been a dramatic expansion of our knowledge on
phospholipases in general, and phospholipase A2 (PLA2) in particular. Progress in this
field has been evident on many fronts, with novel information rapidly accumulating in the
literature regarding the chemistry and molecular biology of this enzyme and its role in
many important physiological processes. These include cellular signal transduction via the
G-protein cycle, and in the generation of many cellular mediators, such as the platelet
activating factor (PAF) and the eicosanoids that participate in the initiation and
propagation of inflammation, to mention a few. This symposium was organized to obtain
an overview of current investigations on this enzyme from the standpoint of its
chemistry, molecular biology and physiology. Another important focus of this symposium
concerns the regulation of PLA2, including endogenous and synthetic inhibitors and
activators of this enzyme. To review these important areas in PLA2 research we invited
scientists who made significant contributions in this field.
The papers in this volume are organized to emphasize the recent advances in
several areas of investigation, including: (I) the structure and mechanism of action of
PLA2, (2) mechanism of activation of PLA2, (3) molecular biology, physiology and
endogenous inhibitors of this enzyme and finally, (4) clinical investigations emphasizing
the pathophysiological role of this enzyme in human diseases. The first article in this
volume is by Dr. Moseley Waite who very kindly agreed to review the research in the
generalized field of phospholipases and provide a comprehensive overview of past, present
and future directions in this broad field of research. The next article is by Drs. Ward
and Pattabiraman who provided a detailed analysis of structural features of PLA2 from
different species. In the next three articles Dr. Heinrikson and his associates discuss the
structure-function relationship of PLA2 while the mechanism(s) of action of this enzyme
is discussed by Dr. Dennis and his associates and Dr. Verheij and his colleagues.
The second group of articles focuses on the activation of PLA2. Drs. Biltonen,
Heimberg, Lathrop and Bell discuss the molecular aspects of PLA2 activation and Dr.
Cordelia-Miele and colleagues describe a novel posttranslational modification of PtA2 by
transglutaminase that leads to its activation. The article by Dr. Hoffman nd his
colleagues describes the mechanism of activation of PLA2 in human monocytes. These
articles are followed by those of Drs. Miele and Baglioni and their associates who discuss
the inhibitory properties of uteroglobin and antiflammin peptides. The work on the
molecular biology of human placental PLA2 is presented by Dr. Crowl and his colleagues.
The physiological aspects of PLA2 including the regulation of this enzyme via the G
protein cycle is discussed by Dr. Burch. Dr. Russo-Marie presents evidence that
lipocortins inhibit cellular PLA2 activity, whereas Drs. A. Hirata and F. Hirata discuss
the biology of PLA2 inhibitory proteins. Dr. Franson and his associates present data
which suggest that PLA2 activity may be inhibited by endogenous fatty acids and
oligomers of prostaglandin BI.
The last two articles are devoted to the clinical correlation of PLA2 activation with
pathophysiology of human diseases. Drs. Bomalaski and Clark discuss the activation of
PLA2 in rheumatoid arthritis and possible involvement of a novel protein called PLA2
activating protein (PLAP) in this process. Drs. Pruzanski and Vadas present evidence for
v
the role of soluble PLA2s in human pathology. These articles provide an excellent
overview of PLA2 as a mediator of human inflammatory diseases such as rheumatoid
arthritis.
I would like to express my deep appreciation to the scientists who have contributed
to this symposium volume. Undoubtedly, great progress has been made in this field and
much more remains to be done. I would like to emphasize that many outstanding
scientists who have contributed in the field of PLA2 research unfortunately could not be
included in this symposium due to the constraints of time and money. I hope that our
next symposium will be able to accommodate many more scientists in this field.
I would also like to thank Drs. Duane Alexander and Arthur Levine, Director and
Scientific Director, respectively, of the National Institute of Child Health and Human
Development, National Institutes of Health, for their support and appropriation of
resources for organizing this minisymposium on PLA2. Finally, I would like to thank the
editors of Plenum Press for their enthusiastic support in publishing this volume.
Anil B. Mukherjee, M.D., Ph.D.
Section on Developmental Genetics
Human Genetics Branch
National Institute of Child Health
and Human Development
Bldg. 10, Room 9S242
Bethesda, Maryland 20892
vi
CONTENTS
Phospholipases, Enzymes That Share a Substrate Class.
M. Waite
Comparative Anatomy of Phospholipase A2 Structures. 23
K.B. Ward and N. Pattabiraman
A Novel Bifunctional Mechanism of Surface Recognition Phospholipase A2. 37
R.L. Heinrikson and F.J. Kezdy
Activation, Aggregation, Inhibition and the Mechanism of
Phospholipase A2 . . . . . . . . . . . . . . . . . 49
T.L. Hazlett, R.A. Deems, and E.A. Dennis
Probing the Mechanism of Pancreatic Phospholipase A2 With the Aid of
Recombinant DNA Techniques . . . . . . . . . . . . . . . . . 65
O.P. Kuipers, c.J. van den Bergh, H.M. Verheij, and G.H. de Haas
Molecular Aspects of Phospholipase A2 Activation . . . . . . 85
R.L. Biltonen, T.R. Heimberg, B.K. Lathrop, and J.D. Bell
Stimulation of Phospholipases A2 by Transglutaminases . . . . 105
E. Cordelia-Miele, L. Miele, S. Beninati, and A.B. Mukherjee
Functional Consequences of Phospholipase A2 Activation in
Human Monocytes. . . . . . . . . . . . . . . . . . 125
T. Hoffman, C. Brando, E.F. Lizzio, C. Lee, M. Hanson,
K. Ting, Y.J. Kim, T. Abrahmsen, J. Puri, and E. Bonvini
Inhibition of Phospholipase A2 by Uteroglobin and
Antiflammin Peptides . . . . . . . . . . . . . . . . . . . 137
L. Miele, E. Cordelia-Miele, A. Facchiano, and A.B. Mukherjee
Antiflammins Inhibit Synthesis of Platelet-Activating Factor
and Intradermal Inflammatory Reactions . . . . . . . 161
G. Camussi, C. Tetta, and C. Baglioni
Isolation and Characterization of cDNA Clones from Human Placenta
Coding for Phospholipase A2 ........... . 173
R. Crowl, C. Stoner, T. Stoller, Y.-C. Pan, and R. Conroy
G-Protein Regulation of Phospholipase A2: Partial Reconstitution
of the System in Cells . . . . . . . . . . . . . . . . . . 185
R.M. Burch
vii
Lipocortins as Antiphospholipase A2 and Antiinflammatory Proteins. 197
F. Russo-Marie
Biology of Phospholipase Inhibitory Proteins 211
F. Hirata and A. Hirata
Inhibition of Human Phospholipase A2 by Cis-Unsaturated Fatty Acids
and Oligomers of Prostaglandin B 1 . . . . . . . . . . . 219
R. Franson, R. Raghupathi, M. Fry, l. Saal, B. Vishwanath,
S.S. Ghosh, and M.D. Rosenthal
Activation of Phospholipase A2 in Rheumatoid Arthritis 231
l.S. Bomalaski and M.A. Clark
Soluble Phospholipase A2 in Human Pathology: Clinical Laboratory
Interface ........................ . 239
W. Pruzanski and P. Vadas
List of Contributors 253
Index ...... . 257
viii
PHOSPHOLIPASES, ENZYMES THAT SHARE A SUBSTRATE CLASS
Moseley Waite
Department of Biochemistry
Bowman Gray School of Medicine of Wake Forest University
300 South Hawthorne Road
Winston-Salem, North Carolina 27103
INTRODUCTION
The title of this chapter was chosen to emphasize a point, namely,
that PLs are classified as a group solely on the basis that they hydrolyze
phospholipids. Beyond this commonality, this is a diverse group of
enzymes, both in structure and in function. l One or more of these enzymes
have been described in almost every, if not all organisms analyzed for
their presence. The sites of hydrolysis and nomenclature for the PLs are
given in Fig. 1.
Two general types of PLs exist, the acyl hydrolases (PLAl , PLA2,
PLB),~' and the phosphodiesterases (PLC, PLD). The functions of these
enzymes vary considerably and more is being learned daily about their key
role in cellular function. In general, three areas of function can be
considered: 1) digestive, 2) membrane repair and remodeling, and
3) regulatory.
All types have been identified as digestive enzymes in a broad
definition of digestive. For example, the best known examples of PLA s
2
are derived from a multitude of venoms and from the mammalian pancreas
whereas PLA (lipases) are known to "digest" the phospholipids in
l
circulating lipoproteins. Also, the beef pancreas contains a PLA that is
l
thought to be involved in digestion. 2 Both PLCs and PLDs have been
identified in media of actively-growing bacteria. These were postulated
to degrade extracellular materials for absorption, although a number are
toxins. l
Membrane remodeling will not be considered here because of space
constraints. Suffice it to mention that this essential role needs not
~'Abbreviations used are: C18:0, stearic acid; C20:4, arachidonic acid;
DG, diacylglycerol; f-MPL, formyl-methionyl-leucyl-phenylalanine; GPI,
glycerophosphorylinositol; MDCK, Madin-Darby canine kidney; PA, phosphatidic
acid; PL, phospholipase; PC, phosphatidylcholine; PE, phosphatidyl
ethanolamine; PEt, phosphatidylethanol;PG, phosphatidylglycerol; PI,
phosphatidylinositol; PIP, phosphatidylinositol 4-monophosphate; PIP2,
phosphatidylinositol 4,S-bisphosphate; PKC, phospholipid-sensitive Ca2+
dependent protein kinase C; PS, phosphatidylserine; LPI, lysophosphatidyl
inositol; LPL, lysophospholipase; TPA, tetradecanoyl-phorbol-acetate.
Biochemistry, Molecular Biology, and Physiology of Phospholipase A, and Its Regulatory Factors
Edited by A. B. Mukherjee, Plenum Press, New York, 1990