The olympic textbook of science in sport part 1

9781405156387_1_pre.qxd 9/11/08 13:08 Page i OLYMPIC TEXTBOOK OF SCIENCE IN SPORT Olympic Textbook of Science in Sport Edited by Ronald J Maughan © 2009 International Olympic Committee ISBN: 978-1-405-15638-7 9781405156387_1_pre.qxd 9/11/08 13:08 Page iii O LY M P I C T E X T B O O K O F S C I E N C E I N S P O RT VOLUME XV OF THE ENCYCLOPAEDIA OF SPORTS MEDICINE AN IOC MEDICAL COMMISSION PUBLICATION EDITED BY RONALD J MAUGHAN, PhD A John Wiley & Sons, Ltd., Publication 9781405156387_1_pre.qxd 9/11/08 13:08 Page iv This edition first published 2009, © 2009 International Olympic Committee Published by Blackwell Publishing Ltd Blackwell Publishing was acquired by John Wiley & Sons in February 2007 Blackwell’s publishing program has been merged with Wiley’s global Scientific, Technical and Medical business to form Wiley-Blackwell Registered office: John Wiley & Sons Ltd, The Atrium, Southern Gate, Chichester, West Sussex, PO19 8SQ, UK Editorial offices: 9600 Garsington Road, Oxford, OX4 2DQ, UK The Atrium, Southern Gate, Chichester, West Sussex, PO19 8SQ, UK 111 River Street, Hoboken, NJ 07030-5774, USA For details of our global editorial offices, for customer services and for information about how to apply for permission to reuse the copyright material in this book please see our website at www.wiley.com/wileyblackwell The right of the author to be identified as the author of this work has been asserted in accordance with the Copyright, Designs and Patents Act 1988 All rights reserved No part of this publication may be reproduced, stored in a retrieval system, or transmitted, in any form or by any means, electronic, mechanical, photocopying, recording or otherwise, except as permitted by the UK Copyright, Designs and Patents Act 1988, without the prior permission of the publisher Wiley also publishes its books in a variety of electronic formats Some content that appears in print may not be available in electronic books Designations used by companies to distinguish their products are often claimed as trademarks All brand names and product names used in this book are trade names, service marks, trademarks or registered trademarks of their respective owners The publisher is not associated with any product or vendor mentioned in this book This publication is designed to provide accurate and authoritative information in regard to the subject matter covered It is sold on the understanding that the publisher is not engaged in rendering professional services If professional advice or other expert assistance is required, the services of a competent professional should be sought The contents of this work are intended to further general scientific research, understanding, and discussion only and are not intended and should not be relied upon as recommending or promoting a specific method, diagnosis, or treatment by physicians for any particular patient The publisher and the author make no representations or warranties with respect to the accuracy or 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Internet Websites listed in this work may have changed or disappeared between when this work was written and when it is read No warranty may be created or extended by any promotional statements for this work Neither the publisher nor the author shall be liable for any damages arising herefrom Library of Congress Cataloging-in-Publication Data The Olympic textbook of science in sport / edited by Ron J Maughan p ; cm – (Encyclopaedia of sports medicine ; v 15) “An IOC Medical Commission publication.” Includes bibliographical references and index ISBN 978-1-4051-5638-7 Sports–Physiological aspects Physical fitness–Physiological aspects Human mechanics I Maughan, Ron J., 1951- II IOC Medical Commission III Series [DNLM: Sports–physiology Athletic Performance Biomechanics Exercise Nutrition Physiology Sports Medicine–methods QT 13 E527 1988 v.15] RC1235.O59 2008 613.7′11–dc22 2008024090 ISBNs: 978-1-4051-5638-7 978-1-4051-9257-6 (leather bound) A catalogue record for this book is available from the British Library Set in 9/12 pt Palatino by Graphicraft Limited, Hong Kong Printed and bound in Malaysia by Vivar Printing Sdn Bhd 2009 9781405156387_1_pre.qxd 9/11/08 13:08 Page v Contents List of Contributors, vii Foreword, ix Preface, x Introduction: Sport, Science and Sports Science, ronald j maughan Part 1: Physiology and Biochemistry Muscle: Producing Force and Movement, paavo v komi and masaki ishikawa Physiological Demands of Sprinting and Multiple-Sprint Sports, 25 clyde williams Physiological Demands of Endurance Exercise, 43 andrew m jones and david c poole Physiological Adaptations to Training, 56 martin j gibala and mark rakobowchuk Skeletal Muscle Metabolic Adaptations to Training, 70 graham p holloway and lawrence l spriet Part 2: Nutrition Nutrition Needs of Athletes, 87 ronald j maughan Dietary Goals and Eating Strategies, 101 louise m burke Hydration, 116 susan m shirreffs Part 3: Anthropometry Body Composition and Sports Performance, 131 timothy olds Part 4: Immunology 10 Exercise Immunology, 149 michael gleeson 11 Exercise, Inflammation, and Metabolism, 163 ben te k peders en Part 5: Cell Biology 12 Genetic Determinants of Physical Performance, 181 claude bouchard and tuomo rankinen 13 Molecular Mechanisms of Adaptations to Training, 202 frank w booth and p darrell neufer 9781405156387_1_pre.qxd vi 9/11/08 13:08 Page vi contents Part 6: Biomechanics, Engineering, and Ergonomics 14 15 Biomechanics of Human Movement and Muscle-Tendon Function, 215 vasilios baltzopoulos and constantinos n maganaris Part 9: Limitations to Performance 19 Cardiorespiratory Limitations to Performance, 307 niels h secher 20 Metabolic Limitations to Performance, 324 francis b stephens and paul l greenhaff 21 The Brain and Fatigue, 340 timothy d noakes, helen crewe and ross tucker Sports Ergonomics, 230 thomas reilly and adrian lees Part 7: Psychology 16 17 Exercise and Psychological Well-being, 251 panteleimon ekkekakis and susan h backhouse Psychological Characteristics of Athletes and their Responses to Sport-Related Stressors, 272 john s raglin and gregory wilson Part 10: Special Populations 22 The Young Athlete, 365 lyle j micheli and margo mountjoy 23 The Female Athlete, 382 myra a nimmo Part 8: Pharmacology Part 11: Exercise and Health 18 24 Performance-Enhancing Drugs, 285 mario thevis and wilhelm schänzer Health Benefits of Exercise and Physical Fitness, 401 michael j lamonte, karl f kozlowski and frank cerny Index, 417 9781405156387_1_pre.qxd 9/11/08 13:08 Page vii List of Contributors SUSAN H BACKHOUSE PhD, Carnegie Research Institute, Leeds Metropolitan University, Leeds, UK MICHAEL GLEESON PhD, School of Sport and Exercise Sciences, Loughborough University, Loughborough, UK VASILIOS BALTZOPOULOS PhD, Institute for Biomedical Research into Human Movement and Health, Manchester Metropolitan University, Manchester, UK FRANK W BOOTH PhD, Department of Biomedical Sciences, Medical Pharmacology, and Physiology, University of Missouri, Columbia, MO, USA PAUL L GREENHAFF PhD, Centre for Integrated Systems Biology and Medicine, School of Biomedical Sciences, University of Nottingham Medical School, Queen’s Medical Centre, Nottingham, UK GRAHAM P HOLLOWAY PhD, Department of Human Health and Nutritional Sciences, University of Guelph, Guelph, Ontario, Canada CLAUDE BOUCHARD PhD, Pennington Biomedical Research Center, Baton Rouge, LA, USA LOUISE M BURKE PhD, APD, Department of Sports Nutrition, Australian Institute of Sport, Bruce, ACT, Australia, and Deakin University, Melbourne, Victoria, Australia FRANK CERNY PhD, Department of Exercise and Nutrition Science, School of Public Health and Health Professions, State University of New York at Buffalo, Buffalo, NY, USA MASAKI ISHIKAWA PhD, Department of Health and Sport Management, Osaka University of Health and Sport Sciences, Osaka, Japan ANDREW M JONES PhD, School of Sport and Health Sciences, University of Exeter, Exeter, UK PAAVO V KOMI PhD, Department of the Biology of Physical Activity, University of Jyväskylä, Jyväskylä, Finland KARL F KOZLOWSKI EdM, Department of HELEN CREWE BSc (Hons), UCT/MRC Research Unit for Exercise Science and Sports Medicine, Department of Human Biology, University of Cape Town, Newlands, South Africa Exercise and Nutrition Science, School of Public Health and Health Professions, State University of New York at Buffalo, Buffalo, NY, USA MICHAEL J LAMONTE PhD, Department of PANTELEIMON EKKEKAKIS PhD, Department of Kinesiology, Iowa State University, Ames, IA, USA Social and Preventive Medicine, School of Public Health and Health Professions, State University of New York at Buffalo, Buffalo, NY, USA MARTIN J GIBALA PhD, Exercise Metabolism ADRIAN LEES PhD, Research Institute for Sport and Research Group, Department of Kinesiology, McMaster University, Hamilton, Ontario, Canada Exercise Sciences, Liverpool John Moores University, Henry Cotton Campus, Liverpool, UK 9781405156387_1_pre.qxd viii 9/11/08 13:08 Page viii list of contributors CONSTANTINOS N MAGANARIS PhD, Institute for Biomedical Research into Human Movement and Health, Manchester Metropolitan University, Manchester, UK MARK RAKOBOWCHUK MSc, Exercise Metabolism Research Group, Department of Kinesiology, McMaster University, Hamilton, Ontario, Canada TUOMO RANKINEN PhD, Pennington RONALD J MAUGHAN PhD, School of Biomedical Research Center, Baton Rouge, LA, USA Sport and Exercise Sciences, Loughborough University, Loughborough, UK THOMAS REILLY DSc, Research Institute for Sport LYLE J MICHELI MD, Harvard Medical School, and Exercise Sciences, Liverpool John Moores University, Henry Cotton Campus, Liverpool, UK and Division of Sports Medicine, Children’s Hospital Boston, Boston, MA, USA MARGO MOUNTJOY MD, Health & WILHELM SCHÄNZER PhD, Center for Preventive Doping Research, Institute of Biochemistry, German Sport University, Cologne, Germany Performance Centre, University of Guelph, Guelph, Ontario, Canada NIELS H SECHER MD, DMSc, Department of P DARRELL NEUFER PhD, Department Anaesthesia, Rigshospitalet, University of Copenhagen, Copenhagen, Denmark of Exercise and Sports Sciences, and Department of Physiology, East Carolina University, Greenville, NC, USA SUSAN M SHIRREFFS PhD, School of Sport and Exercise Sciences, Loughborough University, Loughborough, UK MYRA A NIMMO PhD, School of Sport and Exercise Sciences, Loughborough University, Loughborough, UK LAWRENCE L SPRIET PhD, Department of Human Health and Nutritional Sciences, University of Guelph, Guelph, Ontario, Canada TIMOTHY D NOAKES MBChB, MD, DSc, UCT/MRC Research Unit for Exercise Science and Sports Medicine, Department of Human Biology, University of Cape Town, Newlands, South Africa TIMOTHY OLDS PhD, Nutritional Physiology Research Centre, University of South Australia, Adelaide, Australia BENTE K PEDERSEN MD, DMSc, Centre of Inflammation and Metabolism, Rigshospitalet 7641, Copenhagen, Denmark FRANCIS B STEPHENS PhD, Centre for Integrated Systems Biology and Medicine, School of Biomedical Sciences, University of Nottingham Medical School, Queen’s Medical Centre, Nottingham, UK MARIO THEVIS PhD, Center for Preventive Doping Research, Institute of Biochemistry, German Sport University, Cologne, Germany ROSS TUCKER PhD, UCT/MRC Research Unit for Exercise Science and Sports Medicine, Department of Human Biology, University of Cape Town, Newlands, South Africa DAVID C POOLE PhD, DSc, School of Sport and Health Sciences, University of Exeter, Exeter, UK, and Departments of Kinesiology, Anatomy and Physiology, Kansas State University, Manhattan, KS, USA CLYDE WILLIAMS PhD, School of Sport and Exercise Sciences, Loughborough University, Loughborough, UK GREGORY WILSON PED, Department of JOHN S RAGLIN PhD, Department of Kinesiology, Indiana University, Bloomington, IN, USA Exercise and Sport Science, University of Evansville, Evansville, IN, USA 9781405156387_1_pre.qxd 9/11/08 13:08 Page ix Foreword The general aim of all volumes in the series, Encyclopaedia of Sports Medicine, is the enhancement of the health and welfare of athletes at all levels of competition in all parts of the world The most respected scientific investigators and clinicians have collaborated to produce each volume of the collection which contains reference texts that are both comprehensive for the topics and representative of the leading edge of knowledge Volume XV, The Olympic Textbook of Science in Sport, reexamines the biochemical, physiological, and biomechanical issues that were included in the original Volume I in 1988 and synthesizes the new research information that has been published during the last 20 years I wish to congratulate Professor Ronald Maughan and all of the Contributing Authors on the excellent quality of their efforts and welcome this volume to the Encyclopaedia series Dr Jacques Rogge President of the International Olympic Committee 9781405156387_1_pre.qxd 9/11/08 13:08 Page x Preface As the standards of sporting excellence continue to rise to ever higher levels, so the scientific study of sport also continues to evolve The Medical Commission of the International Olympic Committee has recognised that science is not parochial or nationalistic, but rather that scientific knowledge should be available to all athletes As part of its mission to support athletes and those sports scientists from many different disciplines who, in turn, support them, the IOC Medical Commission decided to commission a Textbook of Science in Sport The concept was of an encyclopaedia of sports science An encyclopaedia should be a book or set of books giving information on many subjects or on many aspects of one subject: it should be both comprehensive and authoritative The aim of this encyclopaedia therefore is to provide reviews of the many disciplines that comprise the sports sciences To so, a cast of leading experts from many countries was recruited as authors These authors have given generously of their time and expertise and to them the credit is due for this volume I would like to extend special thanks to Howard “Skip” Knuttgen for his unfailing support in driving this project to its conclusion His vast experience as Coordinator of Scientific Publications for the IOC Medical Commission has been an enormous asset at every stage of the process I am also deeply grateful to Victoria Pittman and Cathryn Gates, Development Editors at WileyBlackwell in Oxford, and to Alice Nelson who was production manager All did an excellent job and ensured that the project remained on track Ronald J Maughan, PhD 9781405156387_4_012.qxd 198 9/11/08 c h a p ter 13:13 Page 198 12 References Altshuler, D., Brooks, L.D., Chakravarti, A., Collins, F.S., Daly, M.J & Donnelly, P (2005) A haplotype map of the human genome Nature 437, 1299 –1320 Alvarez, R., Terrados, N., Ortolano, R., et al (2000) Genetic variation in the renin–angiotensin system and athletic performance European Journal of Applied Physiology 82, 117–120 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splice junction mutation in a new myopathic variant of phosphoglycerate kinase deficiency (PGK North Carolina) Annals of Neurology 35, 349–353 Verhaaren, H.A., Schieken, R.M., Mosteller, M., Hewitt, J.K., Eaves, L.J & Nance, W.E (1991) Bivariate genetic analysis of left ventricular mass and weight in pubertal twins (the Medical College of Virginia twin study) American Journal of Cardiolology 68, 661–668 Vickers, M.H., Breier, B.H., McCarthy, D & Gluckman, P.D (2003) Sedentary behavior during postnatal life is determined by the prenatal environment and exacerbated by postnatal hypercaloric nutrition American Journal of Physiology Regulatory, Integrative and Comparative Physiology 285, R271–R273 Vorgerd, M., Karitzky, J., Ristow, M., et al (1996) Muscle phosphofructokinase deficiency in two generations Journal of Neurological Science 141, 95–99 Wang, Y.X., Zhang, C.L., Yu, R.T., et al (2004) Regulation of muscle fiber type and running endurance by PPARdelta PLoS Biology 2, e294 9781405156387_4_012.qxd 9/11/08 13:13 Page 201 genetic determinants of physical performance Wehner, M., Clemens, P.R., Engel, A.G & Kilimann, M.W (1994) Human muscle glycogenosis due to phosphorylase kinase deficiency associated with a nonsense mutation in the muscle isoform of the alpha subunit Human Molecular Genetics 3, 1983–1987 Williams, A.G., Day, S.H., Folland, J.P., Gohlke, P., Dhamrait, S & Montgomery, H.E (2005) Circulating angiotensin converting enzyme activity is correlated with muscle strength Medicine and Science in Sports and Exercise 37, 944 – 948 Williams, A.G., Rayson, M.P., Jubb, M., et al (2000) The ACE gene and muscle performance Nature 403, 614 Wilmore, J.H., Stanforth, P.R., Gagnon, J., et al (2001a) Cardiac output and stroke volume changes with endurance training: the HERITAGE Family Study Medicine and Science in Sports and Exercise 33, 99–106 Wilmore, J.H., Stanforth, P.R., Gagnon, J., et al (2001b) Heart rate and blood pressure changes with endurance training: the HERITAGE Family Study Medicine and Science in Sports and Exercise 33, 107–116 Woods, D., Hickman, M., Jamshidi, Y., et al (2001) Elite swimmers and the D allele of the ACE I/D polymorphism Human Genetics 108, 230–232 201 Woods, D.R., World, M., Rayson, M.P., et al (2002) Endurance enhancement related to the human angiotensin I-converting enzyme I-D polymorphism is not due to differences in the cardiorespiratory response to training European Journal of Applied Physiology 86, 240–244 Yang, N., MacArthur, D.G., Gulbin, J.P., et al (2003) ACTN3 genotype is associated with human elite athletic performance American Journal of Human Genetics 73, 627–631 Zhao, B., Moochhala, S.M., Tham, S., et al (2003) Relationship between angiotensin-converting enzyme ID polymorphism and Vo2max of Chinese males Life Science 73, 2625–2630 9781405156387_4_013.qxd 9/11/08 13:13 Page 202 Chapter 13 Molecular Mechanisms of Adaptations to Training FRANK W BOOTH AND P DARRELL NEUFER Knowledge about changes in molecules as a result of physical training is increasing rapidly and will have an impact on training methods The decision was made to limit this chapter to the interactions between nutrition and exercise as this topic is most relevant to optimal sports performance, which will likely be the interest of most readers of this chapter The timing and type of nutrition in relationship to an exercise bout has an impact on the resultant extent of the adaptation to training In addition, the type of exercise (resistance or endurance) affects which genes interact with nutrition to produce the nature and magnitude of the training adaptation Athletes are interested in superior physical performance so they wish to obtain every legal “edge.” Only cellular and molecular studies of exercise and nutrition can provide the basic science which can then be applied to generate an “edge” in improved performance by means of the timing and quality of nutrition As every athlete knows, the ability to perform improves with training and declines when training ceases The body senses exercise and signals changes to improve performance; likewise it senses abstinence from training There are three major strategies the body uses to send messages (signals) after an exercise bout: Whole body messengers: exercise releases hormones into the blood that signal all cells For example, high Olympic Textbook of Science in Sport Edited by Ronald J Maughan © 2009 International Olympic Committee ISBN: 978-1-405-15638-7 202 intensity exercise increases “stress hormones” such as catecholamines that enhance glycogen breakdown in contracting muscles Signals released by the active muscle: e.g., intenseresistance exercise increases the production of insulinlike growth factor (IGF-1) in skeletal muscle cells IGF-1 is released from the muscle cell and interacts with a receptor on the outer membrane of the same muscle cell The binding of IGF-1 to its receptor (analogous to fitting a key [IGF-1] into a lock [IGF-1 receptor]) initiates a cascade of events leading to an increased size of the muscle cell (hypertrophy) Signals acting within active muscle cell: the muscle cell can signal itself internally Adenosine monophosphate kinase (AMPK) inside the muscle cell senses when the energy status of the muscle cell begins to drop during exercise and signals the same muscle cell to begin to oxidize greater amounts of fatty acids Transition from endurance to strength adaptations Adaptations in skeletal muscle from endurance and strength training differ; endurance adaptations consist of minimal or no hypertrophy and large increases in mitochondrial density, while strength adaptations have hypertrophy with minimal or no increases in mitochondria Recently, some of the cellular bases for these differential changes have been reported AMPK senses cellular energy status Increases in the AMP : ATP ratio during endurance and resistance types of muscle contraction activate AMPK, whose activation in skeletal muscle represses 9781405156387_4_013.qxd 9/11/08 13:13 Page 203 molecular mechanisms of adaptations to training Resistance exercise Endurance exercise IGF-I AMPk TSC2–mTOR-P p70s6k-P 203 Scientific basis for the timing of nutrition to enhance adaptations to resistance training Increased mitochondria and GLUT Response of protein synthesis and degradation to mechanically induced hypertrophy Improved aerobic endurance general principles S6-P Hypertrophy and greater strength Fig 13.1 An abbreviated view is shown for the differential signaling by two different exercise types that produce two different outcomes in physical performance AMPK, adenosine monophosphate kinase; IGF-1, insulin-like growth factor 1; mTOR, mammalian target of rapamycin the growth-promoting mammalian target of rapamycin (mTOR) signaling pathway A very simplified explanation is that endurance-type exercise may signal adaptations through the AMPK–PGC-1α pathway while hypertrophy-producing exercise may be signaling through the Akt (PKB)–TSC2–mTOR pathway (Fig 13.1) Forcing an increase in PGC-1α protein by genetic manipulation within non-exercising muscle causes increased mitochondrial density, which mimics an adaptation of endurance-type training However, IGF-1, released locally within skeletal muscle as a result of mechanical overload, interacts with the IGF-1 receptor on the muscle’s outer membrane and initiates signaling through Akt to increase the translation of mRNAs to make nascent proteins Forcing an increase in Akt protein by genetic manipulation causes non-exercising muscles to hypertrophy, which mimics an adaptation of resistance-type training A more in depth consideration of the two signaling pathways in response to endurance and strength exercises can be obtained from recent papers (Bolster et al 2002; Atherton et al 2005; Coffey et al 2006) The nutritional basis for resistance training is related more to the types and timing of amino acid availability, while for endurance training the timing of carbohydrate intake is more important Nutrients (amino acids as the building blocks of new protein as well as glucose and fatty acids as a source of ATP to fuel the assembly of amino acids into protein) are necessary to permit muscle growth in response to resistance exercise The timing of nutrition in close relationship to the performance of the resistance exercise bout is necessary to enhance the potential for muscle growth protein synthesis increases more than protein degradation if muscles hypertrophy in response to resistance training In order to understand the concepts of timing and type of nutrition, the principles of the size of skeletal muscle mass need to be first presented An increase in the mass of skeletal muscle can be caused by any of the following combinations: • Protein synthesis increases while protein degradation decreases; • Protein synthesis increases with no change in protein degradation; • Protein synthesis is unchanged, but protein degradation falls; • Percentage fall in protein degradation exceeds the percentage decline in protein synthesis; • Percentage increase in protein synthesis greatly exceeds to the percentage increase in protein degradation The last of these seems to be what happens biologically, as first shown in living animals by Millward’s laboratory with the model of stretch-induced hypertrophy of skeletal muscle in 1978 (Laurent, Sparrow & Millward 1978) Wong and Booth (1990a) extended the stretch model of hypertrophy to actual resistance exercise by animals, and observed an increase in protein 9781405156387_4_013.qxd 204 9/11/08 c h a p ter 13:13 Page 204 13 synthesis rates with resistance training Because the percentage increase in protein synthesis greatly exceeded the percentage increase in muscle hypertrophy, they inferred that protein degradation must also have increased to eliminate the excess protein made Similar observations were next made in human skeletal muscle by Chesley et al (1992) Biolo et al (1995) extended the findings by their direct determinations of muscle protein turnover; they found that an acceleration of both protein synthesis and degradation during recovery after resistance exercise Biolo et al (1995) employed stable isotopic tracers of amino acids, arteriovenous catheterization of the femoral vessels, and biopsy of the vastus lateralis muscle in human subjects Effect of nutrition timing in relation to resistance exercise time on protein synthesis Studies have since refined these earlier observations by the important findings that the timing and type of nutrition affect the percentage increases in protein synthesis after resistance training protein meal Biolo et al (1997) found that infusing a balanced amino acid mixture immediately after resistance exercise in overnight fasted humans increased muscle protein synthesis to a greater extent than at rest, but did not affect protein degradation An animal study extended the investigation of nutritional timing to resistance training When a meal was ingested by animals in the hour immediately after resistance exercise during a 10-week training period, hind limb muscle weight was 6% higher than in a matched group eating in the fifth hour after the resistance exercise Weights of abdominal fats were 24% lower in the animals fed immediately after exercise These findings could be interpreted to suggest that the partitioning of calories between muscle and fat is dependent upon the timing of eating after resistance exercise If muscles are primed by calories in the immediate period after resistance exercise, muscle protein synthesis can increase These studies established that an edge in strength performance can be gained if food is ingested imme- diately after resistance exercise In conclusion, there is a small time window for nutrition to enhance protein synthesis when resistance exercise is performed; nutrition must be taken immediately before or after resistance exercise increase in protein translation by mechanically induced hypertrophy To understand the scientific basis of how nutrition affects the magnitude of skeletal muscle hypertrophy it is necessary to present brief information on signaling to the translational regulation of protein synthesis Protein translation is the amount of protein made from mRNA per unit of time A guess that protein translation was increased by mechanical overload of muscle was already available in 1978 (Laurent, Sparrow & Millward 1978) Millward inferred that the increase in protein synthesis found in muscles undergoing stretch hypertrophy in the wings of chickens was mediated initially (after day) by an increase in translation without any increase in RNA concentration A few days of continued mechanical overload later, the increase in muscle protein synthesis reflected the higher RNA content Wong and Booth (1990b) reported that as little as duration of total daily resistance-type exercise by animals increased gastrocnemius protein synthesis rates by nearly 50%, with minor effects on skeletal α-actin mRNA level, suggesting that translational and posttranslational mechanisms in the model of stimulated concentric resistance exercise likely were occurring Later it was found that specific mRNAs are increased in muscle during recovery from resistance exercise branched-chain amino acids enhance protein synthesis when resistance exercise occurs In the 1970s, various investigators had already found that branched-chain amino acids (leucine, isoleucine, and valine), or leucine alone, stimulated protein synthesis rates in isolated or perfused skeletal muscles of animals Almost two decades passed until similar experiments were performed in humans Tipton et al (1999) reported that comparable percentage enhancements in protein synthesis rates of skeletal 9781405156387_4_013.qxd 9/11/08 13:13 Page 205 molecular mechanisms of adaptations to training muscle were obtained by oral solutions of either mixed (all) amino acids or of only essential amino acids (which include the branched-chain amino acids) after a bout of resistance exercise in men and women compared to an oral placebo solution There was no significant difference between the treatments for the rate of protein breakdown The amino acid effect on net muscle anabolism was also found not to be simply a caloric effect branched-chain amino acids are best consumed immediately prior to resistance exercise The response of net muscle protein synthesis to consumption of an oral essential amino acid– carbohydrate supplement solution immediately before resistance exercise is greater than that when the solution is consumed after exercise in 30-yearold men and women Tipton et al (2001) suggest that this is primarily because of an increase in muscle protein synthesis as a result of increased delivery of amino acids to the legs during the exercise recent reviews There are numerous outstanding review articles with more detailed information on the effects of resistance exercise on muscle protein synthesis; the reader is encouraged to pursue them (Bolster et al 2003a; Zambon et al 2003; Phillips 2004; Norton & Layman 2006; Rennie et al 2006; Wolfe 2006) alterations by mechanically induced hypertrophy to molecules signaling to increase protein translation One of the molecules activated downstream of Akt when Akt is activated by insulin or IGF-1 is mTOR Bodine et al (2001) showed that hypertrophy of skeletal muscle in adult animals seems to be crucially regulated by the activation of the Akt–mTOR pathway and its downstream targets, where mTOR phosphorylates the proteins p70S6K and 4E-BP1 When p70S6K and 4E-BP1 become phosphorylated, the translation of new proteins is increased The post-exercise times of increases for the molecules 205 that increase protein translation in animal skeletal muscle in response to an acute bout of resistance exercise were first published by Bolster et al (2003b) They are given in parenthesis after the molecule: Akt phosphorylation (5 and 10 min); mTOR (no change); 4E-BP1 phosphorylation (10, 15, and 30 min); eIF4E association to eIF4G (5 and 10 min); p70S6K1 phosphorylation (no change); ribosomal protein S6 phosphorylation (10, 15, and 30 min); eIF2B activity (no change); and eIF2α phosphorylation (no change) Bolster et al (2003a) interpreted their results as collectively providing strong evidence that events downstream of mTOR-mediating signaling are briefly upregulated during the first 30 following an acute bout of resistance exercise and that this response may constitute the most proximal growth response of the muscle cell to resistance exercise Phosphorylation of S6K1 is also increased 2- to 2.5-fold in human skeletal muscle during recovery from resistance exercise (Koopman et al 2006) Because mTOR is a hub that integrates nutritional and mechanical signals, an implication is that the immediacy of the timing of nutrition to mechanical signals is related to the short window of time that Akt–mTOR pathway is increased by a mechanical signal These observations have been extended to human skeletal muscle branched-chain amino acids ingested during and after resistance exercise may mediate signal transduction through p 70 S K in human skeletal muscle Activation of mTOR signals activation of p70S6K by phosphorylation Resistance exercise leads to increased p70S6K phosphorylation at Ser424 and/or Thr421, which continues for and h after exercise in 25-year-old male subjects (Karlsson et al 2004) further observed that ingestion of branched-chain amino acids by the same subjects further increased p70S6K phosphorylation by 3.5-fold during recovery p70S6K phosphorylation at Thr389 was unaltered directly after resistance exercise when subjects ingested only a placebo without branched-chain amino acids However, the presence of branchedchain amino acids during recovery greatly enhanced Thr389 phosphorylation The ribosomal protein S6 is 9781405156387_4_013.qxd 206 9/11/08 c h a p ter 13:13 Page 206 13 activated by p70S6K phosphorylation Phosphorylation of the ribosomal protein S6 was increased in the recovery period only when subjects ingested branched-chain amino acids (Karlsson et al 2004) muscle glycogen concentration prior to resistance exercise affects some signaling responses While carbohydrate ingestion alone has a stimulatory effect on net muscle protein balance following resistance exercise, its effect is much less than the stimulation produced by amino acids (Miller et al 2003) However, the concentration of glycogen within the muscle prior to the resistance exercise does affect the molecules that signal translational increases In overnight fasted, well-trained cyclists performing resistance exercise, Akt phosphorylation was elevated 3.4-fold 10 after resistance exercise when the muscle glycogen content was high, but was unaffected after exercise when the low muscle glycogen was low prior to exercise (Creer et al 2005) p90 ribosomal S6 kinase phosphorylation was increased 10 after exercise, regardless of muscle glycogen availability (Creer et al 2005); however, mTOR protein concentration and phosphorylation were not significantly altered by the resistance exercise response of genes during mechanically loaded hypertrophy of skeletal muscle While great recent progress has occurred in understanding the translational mechanisms by which resistance exercise contributes to muscle growth, less emphasis has been placed upon the pretranslational responses of transcription, slicing, and mRNA stability Carson et al (1995) identified serum response factor (SRE) as a hypertrophy response element on the skeletal α-actin promoter during stretch hypertrophy The hypertrophying muscles also had increases in ribosomal RNA per gram of muscle While the concentration of skeletal α-actin mRNA per gram of muscle did not change, because the muscle hypertrophied, the amount of skeletal αactin mRNA per whole muscle was greater The levels of hundreds of mRNAs in human skeletal muscle are altered by acute changes in nutrition and exercise Insulin (a surrogate for nutrition) changes 800 mRNAs (Rome et al 2003); h of an exhaustive bout of high intensity cycling altered 126 mRNAs (Mahoney et al 2005); and 18 h after a bout of one-leg resistance exercise 704 and 1479 mRNAs, respectively, were different from those in the non-exercised leg (Zambon et al 2003); and 600–1100 mRNAs changed 4–8 h after 300 eccentric contractions (Chen et al 2003) Little is known about the interaction between the timing of food intake and a bout of resistance exercise on the timescale of changes in mRNA Scientific basis for the timing of nutrition to enhance adaptations to endurance training In contrast to resistance exercise, the adaptive responses to endurance exercise in skeletal muscle center, not on contractile proteins, but on those proteins involved in the uptake and utilization of energy The turnover rate of ATP in myofibers may increase by as much as 20-fold during endurance exercise, and these high rates of ATP synthesis and use must be sustained for prolonged periods In order to meet this increased energy demand, the cell must undergo a corresponding increase the oxidation rate of substrates, the byproducts of which are used to drive the resynthesis of ATP The rate at which those processes responsible for the provision and catabolism of substrates can operate ultimately sets the limit to the system (i.e., the intensity and/or duration at which an exercise bout can be sustained) From the muscle fiber’s perspective, the objective is to meet the metabolic demand as efficiently as possible in an effort to minimize the disruption to overall cellular homeostasis Once the activity is over, the priority shifts to replenishing metabolic reserves that have been depleted during exercise At first, one might think that because the myofiber has no idea if another exercise bout will ever be performed again, there is no incentive to activate an adaptive response However, as any endurance athlete will attest, skeletal muscle undergoes a remarkable adaptive response to endurance training, ultimately leading to increases in the efficiency of substrate utilization and, thus, the intensity and/or 9781405156387_4_013.qxd 9/11/08 13:13 Page 207 molecular mechanisms of adaptations to training duration at which an exercise bout can be performed The potential influence of nutrition during exercise recovery on the adaptive responses associated with endurance training is the topic of the following section 207 the protein inactive fail to synthesize glycogen and develop nearly 10-fold greater percentage of type myofibers, suggesting low glycogen content, serves as an intracellular signal to activate the expression of genes required to support oxidative-based metabolism Muscle glycogen resynthesis During recovery from prolonged strenuous exercise, the resynthesis of muscle glycogen becomes the metabolic priority for skeletal muscle Even in the absence of insulin, glucose uptake is elevated over basal levels In addition, the sensitivity of muscle to insulin is increased to facilitate glucose uptake into muscle once carbohydrate is ingested Glycogen synthase, the rate-limiting enzyme that catalyzes the deposition of glucosyl units on the glycogen molecule, is also activated in direct proportion to the level of muscle glycogen depletion The activity of glycogen synthase is controlled primarily by phosphorylation at multiple regulatory sites within the enzyme Dephosphorylation activates the enzyme, a process that is catalyzed by protein phosphatase 1G (PP1G), a glycogen-bound form of protein phosphatase that consists of a catalytic subunit targeted to the glycogen molecule via its interaction with a specific glycogen targeting protein Interestingly, a number of enzymes (GSK3, PP1c) that interact with the glycogen targeting protein also bind to different types of targeting proteins that localize activity of the enzyme to other parts of the cell such as the sarcoplasmic reticulum, myofibrils, and the nucleus It is thus tempting to speculate that specific enzymes normally associated with the glycogen granule under resting conditions are released and targeted to other parts of the cell as glycogen content declines during exercise These enzymes could then coordinate, for example, the transcriptional activation of specific genes related to metabolism As glycogen content is restored, these enzymes would renew their interaction with glycogen targeting proteins and gradually become resequestered within the glycogen structure Such a mechanism would serve to coordinate gene regulation with the intracellular energy status In support of this hypothesis, transgenic mice harboring a genetically engineered defect in the glycogen synthase enzyme that renders Molecular basis for the adaptive responses to endurance exercise training Any discussion of the mechanisms contributing to exercise training adaptations must take into account and be consistent with the principles of protein turnover kinetics This is particularly challenging in the context of exercise because the stimulus experienced by the muscle is intermittent rather than continuous In other words, the adaptive response to a single acute exercise bout, presumably in response to the disturbance to metabolic homeostasis, will be counterbalanced by the “de-exercise” response as the cell returns to and remains in the resting state until the next exercise bout occurs In response to a single endurance exercise bout, a series of events take place that appear to lead ultimately to adaptations associated with exercise training Using techniques to isolate nuclei in combination with reverse transcription polymerase chain reaction (RT-PCR) based nuclear run-on analysis, it has been demonstrated that the transcription of a number of genes is activated by exercise This initial adaptive response of the muscle has a number of important features: Although transcription is activated by some genes during the exercise bout, many genes are primarily not “turned on” until after exercise (Seip et al 1997; Kraniou et al 2000; Pilegaard et al 2000, 2003; Hildebrandt et al 2003) The transcriptional activation of specific genes is transient, remaining elevated for a period of time during recovery before gradually returning to baseline (Pilegaard et al 2000, 2003 Hildebrandt et al 2003) The magnitude and duration of increase in transcription varies tremendously between different genes The activation of transcription generates a corresponding increase in the mRNA for that gene and, although not as well studied, presumably an increase in the corresponding protein 9781405156387_4_013.qxd 208 9/11/08 c h a p ter 13:13 Page 208 13 All mRNAs and proteins also undergo degradation at a certain rate (i.e., change in protein concentration and/or change in time) (O’Doherty et al 1994; Seip et al 1997; Kuo et al 1999, 2004; Jones et al 2003) Like the transcriptional activation of genes, the turnover rate of both mRNAs and proteins varies considerably between different genes Thus, it should be apparent that the slower the turnover rate, the longer an adaptive increase in expression will persist during recovery from exercise Only those mRNAs or proteins with a slow enough turnover rate will still be elevated by the time the next exercise bout is performed and, by extension, accumulate over the course of an exercise training program A more detailed discussion of the kinetic principles of the adaptive response to exercise training is available (Booth & Neufer 2006) Effect of timing and composition of meals on the adaptive responses to endurance exercise in skeletal muscle The above discussion raises the question as to whether the control of exercise-responsive genes may be sensitive and/or associated with the metabolic state of the myofibers during recovery from exercise To test this hypothesis, Pilegaard et al (2002) had subjects perform one-legged cycling exercise to lower muscle glycogen content in one leg and, following a carbohydrate-restricted diet, the following day complete 2.5 h of two-legged cycling exercise Although exercise induced a two- to threefold increase in transcription of the pyruvate dehydrogenase kinase (PDK4) and uncoupling protein (UCP3) genes in the reduced-glycogen leg only, interpretation of the results was somewhat complicated by the fact that the low-glycogen protocol increased the basal mRNA content for PDK4 and UCP3 as well as hexokinase II and lipoprotein lipase In a separate study, subjects completed two 3-h, two-legged knee-extensor trials (separated by weeks) in which both muscle and liver glycogen content was either lowered or returned to control levels by an exercise and/or diet regimen the preceding day Again, the induction of both PDK4 and UCP3 mRNA was significantly greater during the low glycogen trial PDK4 encodes for a kinase that phosphorylates and inactivates pyruvate dehydrogenase, preventing entry of glycolytic products into the mitochondria for oxidation and thus, in theory, preserving glucose for muscle glycogen resynthesis (Pilegaard & Neufer 2004) UCP3 appears to be induced during recovery from exercise as a mechanism to protect against elevated mitochondrial reactive oxygen species (ROS) production (Anderson, Yamazaki & Neufer 2007) The potential impact of glycogen content on genes that encode for mitochondrial enzymes has been more difficult to discern, presumably because of the generally low level of induction of these genes in response to exercise (Pilegaard et al 2000, 2003, 2005; Hildebrandt et al 2003) Clearly, more comprehensive research will be required to assess fully the impact of glycogen content on the regulation of metabolic gene expression in skeletal muscle Perhaps the exercise-responsive gene most sensitive to glycogen content identified to date is the cytokine interleukin (IL-6), the transcriptional activation and mRNA for which increase during exercise is far more dramatic when pre-exercise muscle glycogen content is low (Keller et al 2001; Steensberg et al 2001) Although it has been suggested that release of IL-6 from muscle may serve an interorgan signaling molecule to the liver to accelerate gluconeogenesis (Steensberg et al 2000; Keller et al 2001), direct evidence to support this hypothesis has been elusive, suggesting that IL-6 may have other biologic roles (Pedersen et al 2004) An alternative approach to test the potential influence of metabolic state on the regulation of exerciseinduced gene expression is to manipulate the type of diet consumed during the recovery period after exercise Indeed, restricting carbohydrate for as long as 66 h after exercise has been shown to elicit a sustained increase in muscle insulin sensitivity that appears to be mediated, at least in part, by a sustained increase in muscle GLUT4 transporter protein expression (Garcia-Roves et al 2003) Muscle glycogen resynthesis after exercise is minimal in rats when carbohydrate intake is restricted (Richter et al 2001) In addition, transitioning to a high-carbohydrate diet quickly reverses the exercise-induced increase in GLUT4 mRNA and protein (Garcia-Roves et al 9781405156387_4_013.qxd 9/11/08 13:13 Page 209 molecular mechanisms of adaptations to training 2003), again consistent with the notion that the adaptive response to exercise may be tied to the replenishment of glycogen reserves To test this hypothesis further in humans, Pilegaard et al (2005) had subjects complete 75 of cycling, consuming either a high- or low-carbohydrate diet during the ensuing 24 hours of recovery Ingestion of carbohydrate reversed the exercise-induced transcriptional activation of several exercise-responsive genes (PDK4, UCP3, LPL, and carnitine palmitoyl transferase 1) within – h after exercise, whereas restricting carbohydrate intake resulted in a sustained activation of these genes through 8–24 h of recovery It is important to note that many of the genes that respond to exercise and remain elevated under low carbohydrate intake are also upregulated in muscle by fasting and high-fat feeding (Tunstall et al 2002; Cameron-Smith et al 2003), raising the possibility that the increased reliance of skeletal muscle on lipid metabolism both during and after exercise, particularly when carbohydrate intake is restricted, may serve as the signaling mechanism to regulate exercise-responsive genes Regardless of the exact molecular mechanisms leading to the transcriptional activation of genes in response to exercise, it is clear that substrate availability and/or cellular metabolic recovery (glycogen resynthesis) influence the magnitude and duration of metabolic gene activation The extent to which the metabolic state of myofibers may affect the cumulative adaptive 209 responses during exercise training requires further research Conclusions While it has long been known that physical performance is limited by genes inherited from ancestors, it is now known that the level of expression by these genes can be modulated by environmental conditions In 1967, Holloszy showed that the mitochondrial protein, cytochrome c, is increased by endurance training in rats, demonstrating that the protein level is not fixed In the last decade it has now been demonstrated that nutrition interacts with both resistance and endurance types of exercise to adjust the degree of skeletal muscle’s adaptation to exercise The future will continue to explain, at the molecular level, how plastic and adaptable humans are to their level of physical activity Such information on the molecular response of the body to exercise is not only of importance for those wishing maximal physical performance in sports, but also to the non-athlete who wishes to obtain maximal health benefits of a physically active lifestyle Acknowledgments The authors thank Kevin Tipton for suggestions on the manuscript, which was written while supported by NIH grant AG18780 References Anderson, 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