Miwa / Beckman / Muller Oxidative Stress in Aging

From Model Systems to Human Diseases
1. Auflage 2008
ISBN: 978-1-59745-420-9
Verlag: Humana Press
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 320 Seiten

Reihe: Aging Medicine

Human aging is a complex phenomenon. This state-of-the-art book discusses the role of free radicals in aging in different animal models, as well as the relevance of free radicals on age-related diseases and pathological conditions in humans (following an introduction section of the basics and theory of free radicals). In addition, the major interventions trials of antioxidant supplements in age-related disease, cancer and so forth are reviewed and discussed.

Autoren/Hrsg.

Miwa, Satomi

Beckman, Kenneth Bruce

Muller, Florian

Inhaltsverzeichnis

1;Preface;6
2;Table of Contents;8
3;Contributors;12
4;Section I: Introduction;16
4.1;Chapter 1;17
4.1.1;Introduction;17
4.1.1.1;1 Living in the Presence of Oxygen;17
4.1.1.1.1;1.1 History of Free Radical Theory from Lavoisier to Harman;18
4.1.1.1.2;1.2 Development and Derivatives of Free Radical Theory;19
4.1.1.1.2.1;1.2.1 Aging;20
4.1.1.2;2 Oxidative Stress in Aging: Format of the Book;20
4.1.1.2.1;Section I. Introduction;21
4.1.1.2.2;Section II. Role of Oxidative Stress in Aging;22
4.1.1.2.2.1;Part II-A Different Model Systems;22
4.1.1.2.2.2;Part II-B Comparative Approach;22
4.1.1.2.3;Section III. Oxidative Stress in Human Aging and Diseases;22
4.1.1.2.4;Section IV. Future;23
4.1.1.3;References;23
4.2;Chapter 2;25
4.2.1;The Basics of Oxidative Biochemistry;25
4.2.1.1;1 Chemistry of Reactive Oxygen Species;25
4.2.1.1.1;1.1 Superoxide;25
4.2.1.1.2;1.2 Hydrogen Peroxide;27
4.2.1.1.3;1.3 Hydroxyl Radical;27
4.2.1.2;2 Antioxidant System;27
4.2.1.2.1;2.1 SOD Accelerates Dismutation of Superoxide Radical;28
4.2.1.2.2;2.2 Peroxiredoxins are Major Scavengers of Endogenously Produced H2O2;29
4.2.1.2.3;2.3 How Many Unknown Antioxidant Genes are out There?;30
4.2.1.2.3.1;2.3.1 Biliverdin/Bilirubin and Biliverdin Reductase;31
4.2.1.2.3.2;2.3.2 Apolipoprotein D (ApoD);31
4.2.1.2.3.3;2.3.3 Sulfiredoxin and Sestrin;31
4.2.1.2.4;2.4 ROS Sources;32
4.2.1.2.5;2.5 Measuring Oxidative Damage;34
4.2.1.2.5.1;2.5.1 Lipid Peroxidation;35
4.2.1.2.5.2;2.5.2 DNA Oxidative Damage;36
4.2.1.2.5.3;2.5.3 Protein Oxidation;37
4.2.1.2.6;2.6 How Does Oxidative Damage Kill or Compromise the Function of the Cell?;38
4.2.1.2.6.1;2.6.1 Lipid Peroxidation;38
4.2.1.2.6.2;2.6.2 DNA Oxidative Damage;39
4.2.1.2.6.3;2.6.3 Oxidative Damage to Proteins;40
4.2.1.3;3 Conclusions;40
4.2.1.4;References;40
5;Section II: The Role of Oxidative Stress in Aging;51
5.1;Part II-A: Different Model Systems;51
5.1.1;Chapter 3;53
5.1.1.1;Retrograde Response, Oxidative Stress, and Cellular Senescence;53
5.1.1.1.1;1 Introduction;53
5.1.1.1.2;2 Role of Mitochondrial ROS in Telomere-Dependent Senescence;54
5.1.1.1.3;3 Is Retrograde Signaling Part of a Senescence Signature? Does It Have a Causal Role?;56
5.1.1.1.4;4 Conclusions;63
5.1.1.1.5;References;64
5.1.2;Chapter 4;67
5.1.2.1;Reactive Oxygen Species in Molecular Pathways Controlling Aging in the Filamentous Fungus Podospora anserina;67
5.1.2.1.1;1 Introduction: Senescence in Podospora anserina;67
5.1.2.1.2;2 Mitochondrial DNA Instabilities;70
5.1.2.1.3;3 Oxidative Stress;71
5.1.2.1.3.1;3.1 ROS Generation;71
5.1.2.1.3.2;3.2 ROS Scavenging;73
5.1.2.1.3.3;Untitled;68
5.1.2.1.4;4 Retrograde Response;73
5.1.2.1.5;5 Mitochondrial Dynamics;74
5.1.2.1.6;6 Age-Related Changes in Cytoplasmic Copper Levels;75
5.1.2.1.7;7 ROS-Induced Apoptosis;75
5.1.2.1.8;8 Conclusions and Outlook;75
5.1.2.1.9;References;77
5.1.3;Chapter 5;81
5.1.3.1;Oxidative Stress and Aging in the Budding Yeast Saccharomyces cerevisiae;81
5.1.3.1.1;1 The Model System;81
5.1.3.1.2;2 ROS and Aging: A Lesson from Knockouts;83
5.1.3.1.3;3 More Than Just Damage;87
5.1.3.1.4;4 Age-Dependent Oxidative Damage Is Regulated;89
5.1.3.1.5;5 Conclusions;90
5.1.3.1.6;References;91
5.1.4;Chapter 6;95
5.1.4.1;Oxidative Stress and Aging in the Nematode Caenorhabditis elegans;95
5.1.4.1.1;1 Introduction;95
5.1.4.1.2;2 Why Test Theories of Aging in C. elegans?;97
5.1.4.1.2.1;2.1 C. elegans as a Model for Studies of Aging;97
5.1.4.1.2.2;2.2 Approaches to Testing Oxidation-Related Theories of Aging;98
5.1.4.1.3;3 Is Aging in C. elegans Caused by Molecular Damage?;99
5.1.4.1.3.1;3.1 Age Increases in Damage to Protein, DNA, and Lipid;99
5.1.4.1.3.2;3.2 Age Increases in Blue Fluorescence;99
5.1.4.1.3.3;3.3 Molecular Damage in Mutants with Altered Life Span;101
5.1.4.1.3.4;3.4 Conclusions;101
5.1.4.1.4;4 Do Reactive Oxygen Species Cause Aging in C. elegans?;101
5.1.4.1.4.1;4.1 Alterations of Prooxidant Levels;101
5.1.4.1.4.2;4.2 Does Elevated ROS Accelerate Age Changes in Molecular Damage?;103
5.1.4.1.4.3;4.3 Antioxidant Defense and Aging;103
5.1.4.1.4.4;4.4 SOD and Catalase;104
5.1.4.1.4.5;4.5 Other Antioxidant Defenses;106
5.1.4.1.4.6;4.6 Noncatalytic Antioxidants;108
5.1.4.1.4.7;4.7 Conclusions;109
5.1.4.1.5;5 Do Mitochondria Play a Role in C. elegans Aging?;109
5.1.4.1.5.1;5.1 Does Superoxide Production by Mitochondria Contribute to Aging?;109
5.1.4.1.5.2;5.2 Mitochondria, Superoxide, and Aging in C. elegans;110
5.1.4.1.5.3;5.3 Mitochondrial ETC Defects Can Increase or Reduce Life Span;110
5.1.4.1.5.4;5.4 Is Superoxide Production Important for Mitochondrial Effects on Aging?;113
5.1.4.1.5.5;5.5 Uncoupling Proteins and Aging in C. elegans;114
5.1.4.1.5.6;5.6 Conclusions;114
5.1.4.1.6;6 Is Metabolic Rate a Determinant of Aging in C. elegans?;115
5.1.4.1.6.1;6.1 Metabolic Rate and Superoxide Production;115
5.1.4.1.6.2;6.2 Effects of Temperature on Life Span;115
5.1.4.1.6.3;6.3 Metabolic Rate in Long-Lived Nematodes;115
5.1.4.1.6.4;6.4 Differences in Energy Metabolism between C. elegans and Vertebrates;116
5.1.4.1.6.5;6.5 Conclusions;117
5.1.4.1.7;7 Overall Conclusions;117
5.1.4.1.8;References;118
5.1.5;Chapter 7;125
5.1.5.1;Roles of Oxidative Stress in the Aging Process of Drosophila melanogaster;125
5.1.5.1.1;1 Introduction;125
5.1.5.1.1.1;1.1 The Free Radical/Oxidative Stress Hypothesis of Aging;125
5.1.5.1.1.2;1.2 Interpretation of Experimental Tests of the Oxidative Stress Hypothesis;126
5.1.5.1.2;2 Physiological Adaptation;128
5.1.5.1.2.1;2.1 The Rate-of-Living Hypothesis;129
5.1.5.1.2.2;2.2 Departures from the Rate-of-Living Model;129
5.1.5.1.2.3;2.3 Ramifications for Longevity Studies in Poikilotherms;130
5.1.5.1.2.4;2.4 Ramifications for the Oxidative Stress Hypothesis;131
5.1.5.1.3;3 Experimental Manipulations of Oxidant Production;132
5.1.5.1.3.1;3.1 Mitochondrial Catalase;132
5.1.5.1.3.2;3.2 Uncoupling Proteins (UCPs);133
5.1.5.1.3.3;3.3 Iron Metabolism;134
5.1.5.1.3.4;3.4 Cytochrome c Oxidase (COX);134
5.1.5.1.4;4 Overexpression of Antioxidants;135
5.1.5.1.4.1;4.1 Nonenzymatic Antioxidants;135
5.1.5.1.4.2;4.2 Enzymatic Antioxidants;135
5.1.5.1.5;5 Repair;136
5.1.5.1.5.1;5.1 Methionine Sulfoxide Reductase;137
5.1.5.1.5.2;5.2 Protein Carboxyl Methyltransferase (PCMT);137
5.1.5.1.5.3;5.3 Small Heat Shock Proteins (Hsp22);137
5.1.5.1.6;6 Conclusions (Perspective);138
5.1.5.1.7;References;139
5.1.6;Chapter 8;143
5.1.6.1;Does Oxidative Stress Limit Mouse Life Span?;143
5.1.6.1.1;1 Introduction;144
5.1.6.1.2;2 The Model: Mus musculus “laboratorienscis”;145
5.1.6.1.3;3 Life Span of Antioxidant and Oxidative Damage Repair Knockout Mice;146
5.1.6.1.3.1;3.1 Sod1-/- or CuZnSOD Knockout;146
5.1.6.1.3.2;3.2 MnSOD Knockout;147
5.1.6.1.3.3;3.3 Sod3-/-/EC-SOD Knockout;149
5.1.6.1.3.4;3.4 Glutathione Peroxidase-1 Knockout;149
5.1.6.1.3.5;3.5 Peroxiredoxin Knockout;150
5.1.6.1.3.6;3.6 MsrA Knockout;151
5.1.6.1.3.7;3.7 Knockouts of the Ogg1/Myh 8-oxo-dG Control System;151
5.1.6.1.3.8;3.8 Combinations of Antioxidant Knockouts;152
5.1.6.1.3.9;3.9 Gene Expression Changes in Antioxidant Knockout Mice: An Independent Measure of In Vivo Oxidative Stress and Compensatory Antioxidant Up-Regulation;152
5.1.6.1.4;4 Conclusions;153
5.1.6.1.5;References;154
5.2;Part II-B: The Comparative Approach;162
5.2.1;Chapter 9;163
5.2.1.1;Mitochondrial Free Radical Production and Caloric Restriction: Implications in Vertebrate Longevity and Aging;163
5.2.1.1.1;1 Introduction;163
5.2.1.1.2;2 Mitochondrial ROS Generation Rate: Comparative Studies;164
5.2.1.1.3;3 Mitochondrial DNA Oxidative Damage: Comparative Studies;167
5.2.1.1.4;4 Caloric Restriction, Mitochondrial ROS Production, DNA Oxidative Damage, and Longevity;168
5.2.1.1.5;5 Protein Restriction, Methionine Restriction and Longevity;170
5.2.1.1.6;6 Protein Restriction, Methionine Restriction, mtROS Production, and Oxidative Damage;170
5.2.1.1.7;References;172
6;Section III: Oxidative Stress in Human Aging and Diseases;177
6.1;Chapter 10;179
6.1.1;Deregulation of Mitochondrial Function: A Potential Common Theme for Cardiovascular Disease Development;179
6.1.1.1;1 Introduction;179
6.1.1.2;2 Atherogenesis;180
6.1.1.2.1;2.1 Changing Concepts of Atherogenesis;182
6.1.1.2.2;2.2 Mechanisms of CVD;182
6.1.1.3;3 Mitochondrial Paradigm for CVD Development;183
6.1.1.3.1;3.1 Mitochondria and Their DNA;183
6.1.1.3.2;3.2 Mitochondrial Oxidative Phosphorylation;184
6.1.1.3.3;3.3 Mitochondrial Oxidant Production and Regulation;186
6.1.1.3.4;3.4 Mitochondrial Damage and Function;187
6.1.1.4;4 CVD Risk Factors and Mitochondrial Damage;189
6.1.1.5;5 Mitochondrial Function and Genetics May Influence Disease Susceptibility;191
6.1.1.6;6 Conclusions;194
6.1.1.7;References;194
6.2;Chapter 11;205
6.2.1;Oxidative Stress in Type 2 Diabetes Mellitus;205
6.2.1.1;1 Introduction;205
6.2.1.2;2 Normal Glucose Tolerance;206
6.2.1.3;3 Pathophysiology of T2DM;206
6.2.1.3.1;3.1 Insulin Resistance;207
6.2.1.4;4 The Insulin Receptor;208
6.2.1.5;5 Insulin Receptor Signal Transduction;208
6.2.1.6;6 Molecular Mechanism of Insulin Resistance;209
6.2.1.7;7 Reactive Oxygen Species (ROS) and Insulin Action;210
6.2.1.7.1;7.1 Possible Role of Oxidative Stress in Pathogenesis of Insulin Resistance;210
6.2.1.7.2;7.2 Molecular Mechanism of Oxidative Stress-Induced Insulin Resistance;211
6.2.1.7.3;7.3 beta Cell Failure;212
6.2.1.7.4;7.4 Cellular Mechanisms of b Cell Failure and Role of ROS;214
6.2.1.7.5;7.5 Molecular Etiology of Type 2 Diabetic Complications;216
6.2.1.8;8 Summary and Conclusions;219
6.2.1.9;References;219
6.3;Chapter 12;227
6.3.1;DNA Oxidative Damage and Cancer;227
6.3.1.1;1 Introduction;227
6.3.1.2;2 Oxygen, Reactive Oxygen, and Cancer;228
6.3.1.3;3 ROS-Mediated DNA Damage;230
6.3.1.4;4 8-OxodG and Cancer;230
6.3.1.5;5 DNA Base Excision Repair and Cancer;233
6.3.1.6;6 Mitochondria, ROS, and Cancer;235
6.3.1.7;7 Conclusions;238
6.3.1.8;References;238
6.4;Chapter 13;243
6.4.1;Oxidative Stress in Hypertension;243
6.4.1.1;1 Introduction;243
6.4.1.2;2 Linking Oxidative Stress with Hypertension;244
6.4.1.3;3 NAD(P)H Oxidase: A Major Prooxidant Enzyme;247
6.4.1.3.1;3.1 Nox Isoforms;247
6.4.1.3.1.1;3.1.1 Nox1;247
6.4.1.3.1.2;3.1.2 Nox2;248
6.4.1.3.1.3;3.1.3 Nox4;249
6.4.1.3.2;3.2 p22phox;249
6.4.1.3.3;3.3 p47phox;250
6.4.1.3.4;3.4 p67phox;250
6.4.1.3.5;3.5 Rac1;251
6.4.1.4;4 Superoxide Dismutases, Glutathione Peroxidases, and Catalase: Predominant Antioxidant Defense Systems;251
6.4.1.4.1;4.1 Superoxide Dismutases;251
6.4.1.4.1.1;4.1.1 CuZnSOD;252
6.4.1.4.1.2;4.1.2 MnSOD;253
6.4.1.4.1.3;4.1.3 EC-SOD;254
6.4.1.4.2;4.2 Glutathione Peroxidases;255
6.4.1.4.3;4.3 Catalase;255
6.4.1.5;5 Summary;256
6.4.1.6;References;257
6.5;Chapter 14;267
6.5.1;Aging and Cardiac Ischemia-Mitochondria and Free Radical Considerations;267
6.5.1.1;1 Cardiac Mitochondria and Metabolism;267
6.5.1.2;2 Cardiac Mitochondrial Generation of Reactive Oxygen Species (ROS);268
6.5.1.3;3 Pathologic Mechanisms in Ischemia-Reperfusion (IR) Injury;270
6.5.1.4;4 Changes in Risk Factors and Underlying Causes of IR Injury during Aging;272
6.5.1.5;5 Changes in Cardiac Mitochondria during Aging;273
6.5.1.5.1;5.1 Aging and Complex III;273
6.5.1.5.2;5.2 Aging and Complex IV;274
6.5.1.6;6 Response of Cardiac Mitochondria to IR Injury: Changes during Aging;275
6.5.1.7;7 Efficacy of Cardioprotection in Aging;276
6.5.1.8;8 Concluding Remarks;277
6.5.1.9;References;277
6.6;Chapter 15;283
6.6.1;Role of the Antioxidant Network in the Prevention of Age-Related Diseases;283
6.6.1.1;1 Introduction;283
6.6.1.2;2 Galenic Antioxidant Supplementations and Disease Prevention;285
6.6.1.2.1;2.1 Cardiovascular Diseases;285
6.6.1.2.2;2.2 Cancer;286
6.6.1.2.3;2.3 Evidence from Meta-Analysis;287
6.6.1.3;3 Nonenzymatic Antioxidant Network;288
6.6.1.4;4 Measurement of Total Antioxidant Capacity In Vivo;289
6.6.1.4.1;4.1 Single Electron Transfer Assays;290
6.6.1.4.1.1;4.1.1 FRAP Assay;290
6.6.1.4.1.2;4.1.2 TEAC Assay;290
6.6.1.4.2;4.2 Hydrogen Atom Transfer Assays;290
6.6.1.4.2.1;4.2.1 TRAP Assay;290
6.6.1.4.2.2;4.2.2 Fluo-Lip Assay;291
6.6.1.4.2.3;4.2.3 ORAC Assay;291
6.6.1.5;5 Dietary Modulation of the Antioxidant Network;292
6.6.1.6;6 Imbalance of Nonenzymatic Antioxidant Network and Degenerative Diseases;295
6.6.1.7;7 Conclusions;298
6.6.1.8;References;299
7;Section IV: Future;305
7.1;Chapter 16;307
7.1.1;Reactive Oxygen Species as Signaling Molecules;307
7.1.1.1;1 Reactive Oxygen Species (ROS) in Growth Factor Signaling;307
7.1.1.2;2 NADPH Oxidases;309
7.1.1.3;3 Protein Tyrosine Phosphatases;311
7.1.1.4;4 Mitochondrial ROS;313
7.1.1.5;5 ROS in Cellular Senescence;315
7.1.1.6;6 ROS and Stem Cells;318
7.1.1.7;7 Summary;319
7.1.1.8;References;319
7.2;Chapter 17;323
7.2.1;Summary and Outlook;323
7.2.1.1;1 Does Oxidative Stress Limit Life Span?;323
7.2.1.2;2 Role of Oxidative Stress in Pathology;325
7.2.1.3;3 Epilogue;326
8;Index;327