ebook img

Comparative Biochemistry of Parasitic Helminths PDF

182 Pages·1989·13.021 MB·English
Save to my drive
Quick download
Download
Most books are stored in the elastic cloud where traffic is expensive. For this reason, we have a limit on daily download.

Preview Comparative Biochemistry of Parasitic Helminths

Comparative Biochemistry of Parasitic Helminths Comparative Biochemistry of Parasitic Helminths Edited by EVA -MARIA BENNET Laboratory Co-ordinator at the Australian National University CAROLYN BEHM Lecturer in Biochemistry at the Australian National University CHRISTOPHER BRYANT Professor of Zoology and Dean of the Faculty of Science at the Australian National University London New York CHAPMAN AND HALL First published in 1989 by Chapman and Hall Ltd 11 New Fetter Lane, London EC4P 4EE Published in the USA by Chapman and Hall 29 West 35th Street, New York NY 10001 © 1989 Chapman and Hall Softcover reprint of the hardcover \ 5t edition \989 St Edmundsbury Press Ltd, Bury St Edmunds, Suffolk ISBN 978-94-010-686\-\ e-ISBN-\3: 978-94-009-0833-8 DO\: 10.\ 007/978-94-009-0833-8 ISB N 978-94-0 \ 0-686\-\ All rights reserved. No part of this book may be reprinted or reproduced, or utilized in any form or by any electronic, mechanical or other means, now known or hereafter invented, including photocopying and recording, or in any information storage and retrieval system, without permission in writing from the publisher. British Library Cataloguing in Publication Data Comparative biochemistry or parasitic helminths. 1. Helminthic diseases I. Bennet, Eva II. Behm, Carol III. Bryant, Christopher, 1936- 616.9'62 ISBN 978-94-0\0-686\-\ Contents Preface 1 Ascaris suum: a useful model for anaerobic mitochondrial metabolism and the transition in aerobic-anaerobic devel'oping parasitic helminths 1 R. Komuniecki and P. R. Komuniecki 2 The role of 5-hydroxytryptamine (5-HT: serotonin) in glucose transport, intermediary carbohydrate metabolism and helminth neurobiology 13 D. F. Mettrick 3 What are the functions of the catecholamines and 5-hydroxytryptamine in parasitic nematodes? 25 D. Smart 4 The physiological significance of Complex II (succinate- ubiquinone reductase) in respiratory adaptation 35 H. Oya and K. Kita 5 Oxygen and the lower Metazoa 55 C. Bryant 6 How do parasitic helminths use and survive oxygen and oxygen metabolites? 67 R. K. Prichard 7 Carbohydrate and energy metabolism in adult schistosomes: a reappraisal 79 D. P. McManus 8 Using carbon-I3 Nuclear Magnetic Resonance spectroscopy to study helminth metabolism 95 c.A. Behm 9 Detoxification reactions in parasitic helminths 109 1. Barrett 10 Parasite transport and inactivation functions involved in antiparasitic efficacy 115 R.S. Rew 11 The molecular biology of drug resistance in parasitic helminths 125 G.c. Coles 12 Comparative biochemistry of parasites and its role in drug resistance - an investigation of species differences in tubulin 145 E. Lacey 13 Systemic effects of helminth infections as revealed by serum LDH isozymes and kinetic parameters of transport (V max and Kt) of the host tissue 169 P. Venkateswara Rao Helminth index 179 Preface When Professor John Sprent first suggested, in 1982, that the Australian Society for Parasitology should bid for the opportunity to mount the Sixth International Congress of Parasitology, the immediate reaction was one of disbelief. However, in the two years or so before ICOPA 5, in Toronto, he used his considerable powers to the utmost and spent himself unstintingly in persuading Australian parasitologists to put together a bid. The Society inevitably agreed, for it is difficult to prevent such a determined and eminent man from getting his own way! A case for an Australian venue was prepared and, as President, I was charged with the task of convincing the delegates in Toronto that Australia was worth going all the way to see. The events of that meeting are now far in the past; suffice to say that, in the end, Australia won by the narrowest of margins, largely due to the energy of my inventive colleagues who put the case for Australia at every possible and improbable moment. I do not remember a great deal about the scientific aspects of ICOPA 5. I was far too preoccupied with an awful spectre, that of telling John Sprent that I had failed, to pay attention to much other than lobbying for votes. I do remember, however, telling myself how much I would enjoy the next ICOPA without the terrible responsibility of capturing ICOPA 7. I was completely naive; participating in the organization of an ICOPA is much more demanding! And it was during the run-up to ICOPA 6 that we increased our collective burdens with the decision to run a satellite conference. But at least we'd get some parasitology! The idea came to us because, for the first time ever, there would be on Australian soil most of the parasite biochemists in the world. Having got them here, why should we not continue to enjoy their wisdom and company beyond ICOPA? And how could we show our appreciation that they had come? It occurred to us that our biochemical colleagues would be delighted to see something - even a small bit -of Australia and that they might enjoy a more rural setting for the business of a small but friendly conference. The chosen venue was the Australian National University's field station at Kioloa. You probably will not fmd it on your map, but it is on the east coast, about three hundred kilometres south of Sydney. Its flavour is rural and its accommodation rude but it is equipped with a good lecture room and laboratory. It is backed by rain forest, frequented by lyre-birds, and its small river runs down to sandy beaches with marine rock platforms and nearby archaeological sites. It has barbecue areas and refrigerators -the latter is a necessity of life in the outback -and cattle to provide a certain element of surprise. It is just the place for hard thinking about adaptive biochemistry and then going out to see the effects of adaptive biochemistry in action. The Australian National University was approached for fmandal support. It generously gave us a grant that was sufficient to allow us to charter a bus to take us from Brisbane to Kioloa, a distance of about sixteen hundred kilometres. It also enabled us to provide healthy food and basic comforts for participants, which was how we justified Kioloa not being a five star hotel! We chose the bus because -well, it was cheap and it allowed our guests to see something of the country in a leisurely way. But it also got the conference off to a flying start, providing two days in which to catch up with old friends, grapple with old problems and get ourselves thoroughly up to date. It also gave participants a sense of the sheer size of Australia. I remember one of our Japanese friends, after two days on the road, coming to me with a large map of Australia, about a metre sqQare, to ask if I could indicate the route. I did. We had travelled about eight centimetres. His jaw dropped and he said "So little! So long! I think Australia must be paradise!" . The theme of the conference was the comparative biochemistry of parasites, but we had charged each of the participants to provide a personal view, to tell us about their ideas, however outlandish, and to be speculative and challenging. How well each of them -and we -have succeeded you can judge for yourself. C. Bryant Canberra 1988 Chapter 1 Ascaris suum: A Useful Model for Anaerobic Mitochondrial Metabolism and the Aerobic anaerobic Transition in Developing Parasitic Helminths R. Kornuniecki and P.R. Komuniecki Department of Biology, University of Toledo Toledo, Ohio 43606 USA Abstract. The developmental cycle of Ascaris suum involves a transition from free-living stages, that use aerobic energy generating pathways, to adult worms, where pathways are maximally adapted to anaerobic energy generation. Mitochondria from A. suum provide an excellent model for studies of anaerobic metabolism and mitochondrial biogenesis. Adult worm body wall muscle has been used as a single tissue source for large scale isolation of anaerobic mitochondria for studies on regulation of some of the key soluble enzymes and comparison with counterparts in aerobic tissues. The basic catalytic mechanism of the ascarid pyruvate dehydrogenase complex is, for example, similar to its aerobic counterpart, its regulation however exhibits a number of unique features many of which can be directly related to its anaerobic environment. Another example is provided by the pathways of branched chain fatty acid synthesis in Ascaris, which characteristically involve the reversal of (3-oxidation operative in mammalian mitochondria. Electron transfer is NADH dependent and the enzyme methyl branched-chain acyl CoA dehydrogenase differs in its regulatory properties in accord with its physiological function as a reductase. Key regulatory proteins of adult mitochondria have been purified to homogeneity and recent advances include the preparation of polyclonal antibodies. These can provide sensitive assays for the molecular events governing mitochondrial biogenesis during transition from aerobic to anaerobic energy generation during the moult from L3 to IA. This ascarid system is ideally suited to investigate a number of important questions about the aerobic anaerobic transition present in many different helminths. 2 MEfABOUC REGULATION IN ASCARID DEVELOPMENT Introduction Mitochondria from adult Ascaris suum body wall muscle exhibit a predominantly anaerobic energy metabolism, even in the presence of oxygen, and accumulate succinate and the reduced volatile acids, acetate, propionate, 2- methylbutyrate and 2-methylvalerate as end products of carbohydrate metabolism (Saz, 1981; Kohler, 1985). These organelles provide an excellent model system for studies of anaerobic mitochondrial metabolism and mitochondrial biogenesis. First, during culture they undergo a transition from aerobic to anaerobic energy generation during the moult from L3 to L4. Second, the soluble mitochondrial enzymes involved in the anaerobic energy generating pathway, outlined in Figure 1, make up over 50% of the total matrix protein. This situation contrasts sharply with classical aerobic mitochondria, where the enzymes of the tricarboxylic acid cycle, while catalysing one of the major metabolic activities associated with the matrix; constitute only a minor portion of the matrix protein (Srere, 1985). In fact, over 65 different enzymatic activities have been identified in matrix fractions from aerobic mitochondria and over 140 different peptides have been identified by two-dimensional gel electrophoresis (Altman and Katz, 1976; Henslee and Srere, 1979). Third, A. suum body wall muscle is one of the few helminth tissues available for the large scale isolation of mitochondria for regulatory studies or, more importantly, for enzyme purification. During the past 15 years, most of the soluble enzymes involved in A. suum's anaerobic mitochondrial pathways have been purified to homogeneity and partially characterized (Figure 1). In addition, the NADH-cytochrome c reductase (complex I-III) and succinate-coenzyme Q reductase (complex II) from A. suum inner mitochondrial membranes also have recently been isolated and characterized (Takarniya, Furushlma and Oya, 1986a, 1986b). Many of these enzymes superficially resemble their counterparts in aerobic tissues and it is only recently that many of their more subtle and fascinating regulatory adaptations have been uncovered. The purpose of this limited review is to outline the regulation of some of the key soluble enzymes of the ascarid mitochondrion and, now that pure enzymes are available, suggest directions for future research into the regulation of ascarid mitochondrial metabolism and biogenesis. Pyruvate dehydrogenase complex (PDC) The PDC isolated from adult A. suum body wall muscle is similar to enzyme complexes isolated from many mammalian tissues in that it contains three major components involved with the catalytic mechanism: pyruvate dehydrogenase (El), dihydrolipoyl transacetylase (E2) and lipoamide METABOliC REGULATION IN ASCARID DEVELOPMENT 3 malate ~fumarate ~ succinate pyruvate succinyl CoA acetyl CoA methYb:nalonyl CoA co.-Jf 2 propionyl CoA r ,.-, )- EN:lYME apparent subunit Mr (x IO-~ I _ malic enzyme 64 2. fumarase 49 2-methylacetoacetyl 3. pyruvate dehydrogenase CoA complex: lipoamide dehydrogenase 55 pyruvate dehydrogenase 41,39 transacetylase 68 2-methylhydroxy ")C" 45 butyryl CoA t 4. CoA transferase 50 5. methylmalonyl CoA 75 mutase 2-methylcrotonyl 6. propionyl CoA carboxylase CoA (partially purified) ~ 7. "condensing" enzyme (partially purified) 2-methylbutyryJ 8. 2-methylacetoacetyl CoA 30 CoA reductase + 9. 2-methyl branch-chain 43 acyl CoA dehydrogenase 2-methylbutyrate 10. electrontransfer flavoprotein 36,31 Figure 1. Enzymes involved in the pathway of malate-dependent 2-methylbutyrate formation in A. suum mitochondria References. Enzyme: 1. Fodge, Gracy and Harris, 1972; 2. Payne, Powley and Harris, 1979; 3. Komuniecki, Komuniecki and Saz, 1979; Thissen, DeSai, McCartney and Komuniecki, 1986; Komuniecki and Saz, 1979; 4. McLaughlin, Saz and deBruyn, 1986; S. Han, Bratt and Hogenkamp, 1984; 6.Saz and Pietrzak, 1980; 7. Suarez de Mata, Saz and Pasto, 1977; 8. Suarez de Mata, Zarranz. Lizardo and Saz, 1983; 9.,10. Komuniecki, Fekete and Thissen-Parra, 1985.

See more

The list of books you might like

Most books are stored in the elastic cloud where traffic is expensive. For this reason, we have a limit on daily download.