Biochemistry of Signal Transduction in Myocardium

262 Pages·1996·9.8 MB·English

by  Han A. A. van Heugten, Yvonne E. G. Eskildsen-Helmond, Jos M. J. Lamers

BIOCHEMISTRY OF SIGNAL TRANSDUCTION IN MYOCARDIUM
Developments in Molecular and Cellular Biochemistry
Series Editor: Naranjan S. Dhalla, Ph.D., FACC
1. V.A. Najjar (ed.): Biological Effects o/Glutamic Acid and Its Derivatives. 1981 ISBN 90-6193-841-4
2. V.A. Najjar (ed.): Immunologically Active Peptides. 1981 ISBN 90-6193-842-2
3. V.A. Najjar (ed.): Enzyme Induction and Modulation. 1983 ISBN 0-89838-583-0
4. V.A. Najjar and L. Lorand (eds.): Transglutaminase. 1984 ISBN 0-89838-593-8
5. GJ. van der Vusse (ed.): Lipid Metabolism in Normoxic and Ischemic Heart. 1989 ISBN 0-7923-0479-9
6. IF.C. Glatz and GJ. van der Vusse (eds.): Cellular Fatty Acid-Binding Proteins. 1990
ISBN 0-7923-0896-4
7. H.E. Morgan (ed.): Molecular Mechanisms o/Cellular Growth. 1991 ISBN 0-7923-1183-3
8. GJ. van der Vusse and H. Stam (eds.): Lipid Metabolism in the Healthy and Diseased Heart. 1992
ISBN 0-7923-1850-1
9. Y. Yazaki and S. Mochizuki (eds.): Cellular Function and Metabolism. 1993 ISBN 0-7923-2158-8
10. I.F.C. Glatz and G.I. van der Vusse (eds.): Cellular Fatty-Acid-Binding Proteins, II. 1993
ISBN 0-7923-2395-5
11. R.L. Khandelwal and I.H. Wang (eds.): Reversible Protein Phosphorylation in Cell Regulation. 1993
ISBN 0-7923-2637-7
12. l Moss and P. Zahradka (eds.): ADP-Ribosylation: Metabolic Effects and RegUlatory Functions. 1994
ISBN 0-7923-2951-1
13. V.A. Saks and R. Ventura-Clapier (eds.): Cellular Bioenergetics: Role o/Coupled Creatine Kinases. 1994
ISBN 0-7923-2952-X
14. I. Slezak and A. ZiegelhOffer (eds.): Cellular Interactions in Cardiac Pathophysiology. 1995
ISBN 0-7923-3573-2
15. I.A. Barnes, H.G. Coore, A.H. Mohammed and R.K. Sharma (eds.): Signal Transduction Mechanisms.
1995 ISBN 0-7923-3663-1
16. A.K. Srivastava and I.-L. Chiasson (eds.): Vanadium Compounds: Biochemical and Therapeutic Applica-
tions. 1995 ISBN 0-7923-3763-8
17. lMJ. Lamers and P.D. Verdouw (eds.): Biochemistry 0/ Signal Transduction in Myocardium. 1996
ISBN 0-7923-4067-1
KLUWER ACADEMIC PUBLISHERS - DORDRECHT / BOSTON / LONDON
Biochemistry of
Signal Transduction
in Myocardium
Edited by
JOS MJ. LAMERS
Department of Biochemistry,
Cardiovascular Research Institute COEUR,
Faculty of Medicine of Health Science,
Erasmus University Rotterdam,
P.O. Box 1738,
3300 DR Rotterdam,
The Netherlands
and
PIETER D. VERDOUW
Department of Cardiology,
Cardiovascular Research Institute COEUR,
Erasmus University Rotterdam,
P.O. Box 1738,
3300 DR Rotterdam,
The Netherlands
Kluwer Academic Publishers
Dordrecht / Boston / London
A C.LP. Catalogue record for this book is available from the Library of Congress.
ISBN- 13: 978-1-4612-8544-1 e-ISBN-13: 978-1-4613-1275-8
DOl: 10.1007/978-1-4613-1275-8
Published by Kluwer Academic Publishers,
P.O. Box 17,3300 AA Dordrecht, The Netherlands.
Kluwer Academic Publishers incorporates
the publishing programmes of
D. Reidel, Martinus Nijhoff, Dr W. Junk and MTP Press.
Sold and distributed in the U.S.A. and Canada
by Kluwer Academic Publishers,
101 Philip Drive, Norwell, MA 02061, U.S.A.
In all other countries, sold and distributed
by Kluwer Academic Publishers Group,
P.O. Box 322, 3300 AH Dordrecht, The Netherlands.
Printed on acid-free paper
All Rights Reserved
© 1996 Kluwer Academic Publishers
Softcover reprint of the hardcover 1 ste dition 1996
No part of the material protected by this copyright notice may be reproduced or
utilized in any form or by any means, electronic or mechanical,
including photocopying, recording or by any information storage and
retrieval system, without written permission from the copyright owner.
Molecular and Cellular Biochemistry:
An International Journal for Chemical Biology in Health and Disease
CONTENTS VOLUME 157, Nos. 1-2, 1996
BIOCHEMISTRY OF SIGNAL TRANSDUCTION IN MYOCARDIUM
lM.I. Lamers and P.D. Verdouw, guest editors
Preface 1
Part I: Basic mechanisms
H.A.A. van Heugten, Y.E.G. Eskildsen-Helmond, H.W. de Jonge, K. Bezstarosti and J.M.I. Lamers: Phos-
phoinositide-generated messengers in cardiac signal transduction 5-14
D.E. Dostal, G.W. Booz and K.M. Baker: Angiotensin II signalling pathways in cardiac fibroblasts: Conventional
versus novel mechanisms in mediating cardiac growth and function 15-21
A.B. Vaandrager and H.R de Jonge: Signalling by cGMP-dependent protein kinases 23-30
J. T.A. Meij: Regulation of G protein function: Implications for heart disease 31-38
Y.E.G. Eskildsen-Helmond, H.A.A. Van Heugten and J.M.I. Lamers: Regulation and functional significance of
phospholipase D in myocardium 19-48
C. Page and A.F. Doubell: Mitogen-activated protein kinase (MAPK) in cardiac tissues 49-57
L. Piacentini and F. Niroomand: Phosphotransfer reactions as a means of G protein activation 59-63
M. Puc~at and G. Vassort: Signalling by protein kinase C isoforms in the heart 65-72
Part II: (patho)physiological responses in myocardium
N. Maulik, D.T. Engelman, M. Watanabe, RM. Engelman and D.K. Das: Nitric oxide - a retrograde messenger
for carbon monoxide signaling in ischemic heart 75-86
G.L. Engelmann, R.A. Worrell, R.A. Duff, P.S. Grutkoski, K.R. Chien and R.P. Harvey: Expression of cardiac
muscle markers in rat myocyte cell lines 87-91
B.R. Kwak and H.I. Jongsma: Regulation of cardiac gap junction channel permeability and conductance by
several phosphorylating conditions 93-99
C.H. Yu, S.Y. Liu and V. Panagia: The transphosphatidylation activity of phospholipase D 101-105
E. Vincan, C.B. Neylon, A.N. Jacobsen and E.A. Woodcock: Reduction in Gh protein expression is associated
with cytodifferentation of vascular smooth muscle cells 107-110
H.S. Sharma, N. Maulik, B.C.G. Gho, D.K. Das and P.D. Verdouw: Coordinated expression of heme oxygen-
ase-I and ubiquitin in the porcine heart subjected to ischemia and reperfusion 111-116
M.P. Gupta, M. Gupta, E. Dizon and R Zak: Sympathetic control of cardiac myosin heavy chain gene expression 117-124
W.H. Dillmann: Regulation of expression of cardiac sarcoplasmic reticulum proteins under pathophysiological
conditions 125-128
B.C. Tilly, K. Bezstarosti, W.E.M. Boomaars, C.R Marino, J.MJ. Lamers and H.R de Jonge: Expression and
regulation of chloride channels in neonatal rat cardiomyocytes 129-135
I. Fleming, J. Bauersachs and R. Busse: Paracrine functions of the coronary vascular endothelium 137-145
Part III: Normal and failing myocardium
EJ. Kelso, R.F. Geraghty, B.I. McDermott, E.R. Trimble, D.P. Nicholls and B. Silke: Mechanical effects ofET-1
in cardiomyocytes isolated from normal and heart-failed rabbits 149-155
T.-H. Cheng, F.-Y. Lee, J. Wei and C.-I. Lin: Comparison of calcium-current in isolated atrial myocytes from
failing and nonfailing human hearts 157-162
M.B. Anand-Srivastava: G-proteins and adenylyl cyclase signalling in hypertension 163-170
S. Bartel, B. Stein, T. Eschenhagen, U. Mende, J. Neumann, W. Schmitz, E.-G. Krause, P. Karczewski and H.
Scholz: Protein phosphorylation in isolated trabeculae from nonfailing and failing human hearts 171-179
XJ. Martin, D.G. Wynne, P.E. Glennon, AF.M. Moorman and K.R Boheler: Regulation of expression of
contractile proteins with cardiac hypertrophy and failure 181-189
D. Kaura, N. Takeda, R. Sethi, X. Wang, M. Nagano and N.S. Dhalla: /3-Adrenoceptor mediated signal transduc-
tion in congestive heart failure in cardiomyopathic (UM-X7.l) hamsters 191-196
Part IV: Cardiovascular therapeutics
H.W. de Jonge, D.H.W. Dekkers and J.MJ. Lamers: Polyunsaturated fatty acids and signalling via phospholipase
C-/3 and A2 in myocardium 199-210
AHJ. Danser: Local renin-angiotensin systems 211-216
A. Bordoni, J.A Lopez-Jimenez, C. Spano, P.L. Biagi, D.F. Horrobin and S. Hrelia: Metabolism of linoleic and
a-linolenic acids in cultured cardiomyocytes: Effect of different N-6 and N-3 fatty acid supplementation 217-222
C. Guarnieri, E. Giordano, C. Muscari, L. Grossi and C.M. Caldarera: Alpha-tocopherol pretreatment improves
endothelium-dependent vasodilation in aortic strips of young and aging rats exposed to oxidative stress 223-228
B. Huisamen and A. Lochner: Inositolpolyphosphates and their binding proteins - a short review 229-232
W. Sluiter, W.J.A de Vree, A Pietersma and J.F. Koster: Prevention of late lumen loss after coronary an-
gioplasty by photodynamic therapy: Role of activated neutrophils 233-238
H.A.J. Struijker-Boudier, M.WJ. Messing and H. van Essen: Alpha-adrenergic reactivity of the microcirculation
in conscious spontaneously hypertensive rats 239-244
U. Ravens, H.M. Himmel, M. Fliiss, K. Davia and S.E. Harding: Phosphodiesterase inhibition and Ca2+ sensitiza-
tion 245-249
W. Schmitz, P. Boknik, B. Linck, F.U. Miiller: Adrenergic and muscarinic receptor regulation and therapeutic
implications in heart failure 251-258
G. Noll, RR Wenzel and T.F. Liischer: Endothelin and endothelin antagonists: Potential role in cardiovascular
and renal disease 259-267
Index to Volume 157 269-272
Molecular and Cellular Biochemistry 157: I, 1996.
© 1996 Kluwer Academic Publishers.
Preface
The papers in this volume are the Proceedings of the Satel- proteins, transcription and mitotic factors) for the many pro-
lite Symposium of the XVth World Congress of the Interna- tein kinases, to elucidate the biological significance of the cell
tional Society for Heart Research on 'Signal Transduction in type-specific expression and heterogeneity of signalling pro-
Normal and Diseased Myocardium', which was held in Rot- teins (e.g. membrane receptors, isoenzymes of protein kinase
terdam at the Faculty of Medicine and Health Sciences ofthe C, G-proteins) and to unravel the cross-talk interaction be-
Erasmus University, June 30 and July 1, 1995. The Satellite tween the signalling systems (e.g. phospholipase C with ade-
Symposium was organized by the Cardiovascular Research nylate cyclase and phospholipase C with phospholipase D).
Institute COEUR, which is a collaborative research division The multiplicity of receptor types, G-proteins, effector pro-
formed by the departments of Biochemistry 1, Cardiology, teins, second messengers and protein kinases, their substrate
Internal Medicine I and III and Pharmacology. proteins and the 'cross-talk' interactions in the myocardium
This special collection of reviews and research papers raises fundamental questions about the mechanisms that as-
covers many of the areas under intensive and rapid develop- sure the precision and timing of the myocardial responses to
ment such as agonist-receptor and receptor G-protein effec- hormonal and pharmacological stimuli.
tor coupling, generation of second messengers, cross-talk The Symposium was made possible by the financial sup-
between various signalling pathways, regulation of hyper- port of the Vereniging Trustfonds Erasmus Universiteit Rot-
trophic and hyperplastic cell growth. The last section provides terdam, Royal Netherlands Academy of Arts and Sciences,
an update on cardiovascular therapy based upon interference Netherlands Heart Foundation, Dutch Union for Biochem-
with intra- and extracellular signalling in the cardiovascular istry and Molecular Biology, Foundation Gerrit Jan Mulder,
system. We hope that this special issue of Molecular and Foundation Heart Metabolism and I.R.I.S. Servier. The edi-
Cellular Biochemistry provides an up-to-date source of in- tors would like to express their gratitude to the Editor-in-
formation for all scientists and clinicians interested in the Chief Naranjan S. Dhalla (Past-President of the ISHR) for
mechanisms by which external signals are transmitted to the publishing this Focussed Issue on 'Biochemistry of Signal
interior of cells and regulation of a variety of physiological, Transduction in Myocardium'.
pathological and pharmacological responses.
Diverse and distinct auto-, para- and endocrine stimuli 10S M.J. LAMERS
arriving at the surface of endothelium, smooth muscle cells, AND PIETER D. VERDOUW
cardiomyocytes and fibroblasts within the myocardium en- Department of Cardiology
gage cell type - specific receptors which leads to transmis- and Department of Biochemistry
sion of signals across the cell plasma membrane and results Cardiovascular Research Institute COEUR
in the production and activation of second messengers. The Faculty of Medicine and Health Sciences
most common mechanism by which these second messengers Erasmus University Rotterdam
function is via direct or indirect activation of specific protein P.O. Box 1738
kinases. The current challenge for scientists is to identify the 3000 DR Rotterdam
specific substrates (e.g. metabolic enzymes, Ca2+ -regulating The Netherlands
PART I
BASIC MECHANISMS
Molecular and Cellular Biochemistry 157: 5~14, 1996.
© 1996 Kluwer Academic Publishers.
Phosphoinositide-generated messengers in cardiac
signal transduction
Han A.A. van Heugten, Yvonne E.G. Eskildsen-Helmond, Henriette W.
de Jonge, Karel Bezstarosti and Jos MJ. Lamers
Department ofB iochemistry, Cardiovascular Research Institute COEUR, Faculty ofM edicine & Health Sciences, Erasmus
University Rotterdam, P.O. Box 1738, 3000 DR, Rotterdam, The Netherlands
Abstract
A multitude of agonists like e.g. endothelin-l, angiotensin-II, serotonin, thrombin, histamine and vasopressin as well as u 1-
adrenergic and muscarinic stimulation lead to stimulation of the phosphoinositide cycle in the heart. Besides this seven mem-
brane spanning-domain receptor-coupled stimulation of the key enzyme of the phosphoinositide cycle, phospholipase C-~,
another class of hormones, growth factors, also couple to the phosphoinositide cycle, now through receptors with intrinsic tyrosine
kinase activity that can phosphorylate and stimulate the phospholipase C-y isozyme. In this review we summarize the multi-
tude of receptor (sub )types, G-protein-subunit- and phospholipase C-isozymes that are present in the heart. Furthermore, gen-
eration of second messengers and cellular responses are described together with the (patho )physiological implications for the
heart of phospho in os iti de cycle activation and second messenger accumulation. (Mol Cell Biochem 157: 5-14, 1996)
Key words: Phosphatidylinositol cycle, cardiomyocytes, receptors, G-proteins, phospholipase C, (patho)physiological implications
Introduction in the light of possible (patho )physiological implications for
the heart.
By binding to cell surface receptors, many agonists are able
to activate the phosphoinositide (PtdIns) cycle through stimu-
lation of phospholipase C (PLC) giving rise to the second Transmembrane signal transduction
messengers inositol 1 ,4,5-trisphosphate (Ins (l ,4,5)P) and
1 ,2-diacylglycerol (1,2-DAG) from hydrolysis of pho s pha - Receptors
tidyl inosito14,5-bisphosphate (Ptdlns(4,5)P2). As two ma-
jor isozymes ofPLC are involved in hydrolysis of phospho- Receptors that are coupled to GTP-binding proteins (G-pro-
inositides, it is not surprising to see that two classes of teins) show a high degree of homology and can mediate ac-
receptors can be distinguished that mediate activation ofPLC. tivation of the phosphatidylinositol pathway or of other
One class of receptors is comprised of proteins with seven pathways through interaction with specific GTP-binding
transmembrane-spanning domains that are coupled to hetero- protein isozymes. The G-protein-PLC coupled receptors are
trimeric GTP-binding proteins that on their tum mediate sig- good representatives of this type of proteins that contain
nal transduction to PLC-p. The other class of PtdIns cycle- seven transmembrane-spanning regions with an intracellu-
stimulating receptors harbour receptor-tyrosine kinase activ- lar COOH-terminus and an extracellular NH2-terminus. The
ity that is activated upon receptor occupation and that results protein contains multiple potential N-glycosylation sites in
in stimulation ofPLC-y upon phosphorylation ofthe enzyme. the extracellular NH2 -terminal domain together with cysteine
The first section describes the components mentioned above, residues in the four extracellular domains that are thought to
with emphasis on the presence in the heart while the second be sites for disulfide bridge formation. Many of the recep-
section illustrates activation of the PtdIns cycle in the heart tors are susceptible to desensitization upon receptor occupa-
Address/or o./JjJrints: J.M.J. Lamers, Department of Biochemistry, Cardiovascular Research Institute COEUR, Faculty of Medicine and Health Sciences,
Erasmus University Rotterdam, P.O. Box 1738, 3000 DR, Rotterdam, The Netherlands
6
tion. Intracellular putative phosphorylation sites for serine/ embryonic or neonatal cardiomyocytes, ATIB is expressed as
threonine protein kinases are present in these proteins and well [12] suggesting developmental regulation of expression.
might playa role in this regulation. Several isoforms exist In contrast to rodents, humans only contain one AT I receptor
for some agonist-specific receptors, all encoded by different that is strongly homologous to both rat ATI genes but from
genes. Many important receptors have been identified up till sequence comparison it is not possible to subclassify the hu-
now, as e.g. the aI-adrenergic, angiotensin-II (AngIl), man AT I receptor. The function of the AT 2 receptor is not yet
endothelin-l (ET- 1), muscarinic, serotonin (5-HT), hista- known, but it was suggested that it mediates an anti-prolif-
minic and a-thrombin receptors. However, it is not unlikely erative effect, as discussed in ref [10]. In rat heart, the ATI
that new receptors of this type will be identified in the future. as well as AT2 receptor subtype are expressed [13]. Studies
Through screening at low stringency with sequences that are with cultured rat ventricular myocytes indicated that AngII
known to be highly conserved among known receptors, i.e. not only activates the PtdIns cycle, but also activates phos-
the transmembrane-spanning domains, several genes were pholipase D, phospholipase A2 and increases cAMP content
identified that were termed' orphan receptors'. Although the in these cells [14, 15]. All signal-transduction pathways that
physiological ligands of these receptors have not been iden- are activated by AngIl were reported to require the ATI
tified, many have been shown to have pharmacological rel- receptor, but no ATI subtype-specificity has been reported yet
evance [1]. An example of such a receptor that is also [14]. Moreover, it was also suggested that PLC and phos-
expressed in the heart was recently described but the ligand pholipase A2 are activated by distinctly different AngIl
has yet to be identified [2, 3]. As the mRNA level was down- receptor subtypes [15].
regulated by the cAMP pathway, reminiscent of the ~­ Endothelin comprises a family of three peptides (ET- 1, -2
adrenoceptor, this receptor is likely to be coupled to the and -3) and was first discovered in 1988 to be synthesized
cAMP pathway. and excreted by vascular endothelial cells, but endothelin
aI-Adrenergic receptors belong to a family of closely re- production was later confirmed to occur in a multitude of
lated isoforms that mediate regulation of myocardial func- nonvascular tissues, such as e.g. epithelial tissue in the lung
tion by the sympathetic nervous system through diverse (for reviews on endothelin and its receptor see refs [16-19])
signalling pathways (reviewed in ref [4]). Initial pharmaco- and cardiomyocytes as well [20]. Endothelin is a potent va-
logical evidence suggested that two different isoforms, alA soconstrictor, but also stimulates endothelium-derived relax-
and alB' existed. Subsequently, three different genes for the ing factor (NO) release. Three SUbtypes of endothelin
al-adrenoceptor were identified, ala/d' alb and alc in human receptors have been identified pharmacologically up to date;
as well as in rat [5]. All three receptors coupled to the PtdIns ET A' that has a high affinity for ET- 1 but a lower affinity for
cycle in transfection studies in rat fibroblasts, where the a le- ET-2 and still lower affinity for ET-3, ETB that has equipo-
adrenoceptor has the highest norepinephrine efficacy, and ala/d tent affinity for all three endothelin isotypes and ETc that
the lowest [5]. The three receptor genes show distinct tissue- preferentially interacts with ET -3. The ETA as well as ETB
specific expression in rat, but all three genes are expressed receptors, cloned and expressed in recipient cells, are able to
in heart (6]. In cultured cardiomyocytes all three genes are activate the PtdIns cycle. However, activation of this signal
expressed again, in sharp contrast to cultured heart fibroblasts transduction pathway seems to be coupled to vasoconstric-
that contain no al-adrenoceptor mRNA [7]. In cultured tion through the ETA receptor in smooth muscle cells and to
neonatal rat cardiomyocytes the alA -adrenoceptor class me- NO release in endothelial cells through the ETB receptor. In
diates activation of the PtdIns cycle [8] while in freshly iso- rat heart, ETA and ET B receptor subtypes are present where
lated adult rat ventricular myocytes both the a lA- and the ETA receptor was suggested to mediate inotropy while the
alB -adrenoceptor class were shown to couple to the PtdIns ET B receptor was more linked to chronotropy, as discussed
pathway [9] partly confirming the results from the above in ref [21]. However, as ET- 1 was a much more potent acti-
mentioned transfection experiments. vator of the PtdIns cycle than ET- 3 in neonatal atrial cells
AngII is formed from angiotensinogen that is released into [21], it is likely that only the ETA receptor is coupled to PLC
the circulation by the liver or is locally produced by e.g. the in the heart. We have to be aware of the fact that the ETA
heart. Blocking AngII function by antagonists has e.g. anti- receptor in adult rat or human cardiomyocytes not only cou-
hypertensive and renal protective effects and blocks cardiac ples to phospholipase C but also inhibits adenylate cyclase
hypertrophy, showing that this peptide exerts its function all in these cells [22, 23], resulting in a negative chronotropic
throughout the body. AngII receptors can be subdivided into component of the response of the heart to ET- 1 [24] on top
two major classes, ATI and AT2 (reviewed in ref [IO]). In ro- of the positive chronotropic effect caused by PLC stimula-
dents, two ATI receptor subtypes (ATIA and ATIB) exist that tion. Furthermore, the fact that the ETA receptor shows a
are encoded by different genes and the mRNAs are expressed lower molecular weight and relatively low affinity for ET-l
tissue-selectively [11] as well as cell-specific showing ex- in the neonatal ventricle when compared to cultured neonatal
pression of only AT IA in adult heart. However, in cultured myocytes ([25] and references therein), suggests that results