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Protein Oxidation and Aging [Other digital carrier]

  • Formaat: Other digital carrier, 516 pages, kõrgus x laius x paksus: 250x150x15 mm, kaal: 725 g
  • Ilmumisaeg: 20-Nov-2012
  • Kirjastus: John Wiley & Sons Inc
  • ISBN-10: 1118493036
  • ISBN-13: 9781118493038
Teised raamatud teemal:
  • Formaat: Other digital carrier, 516 pages, kõrgus x laius x paksus: 250x150x15 mm, kaal: 725 g
  • Ilmumisaeg: 20-Nov-2012
  • Kirjastus: John Wiley & Sons Inc
  • ISBN-10: 1118493036
  • ISBN-13: 9781118493038
Teised raamatud teemal:

Reviews our current understanding of the role of protein oxidation in aging and age-related diseases

Protein oxidation is at the core of the aging process. Setting forth a variety of new methods and approaches, this book helps researchers conveniently by exploring the aging process and developing more effective therapies to prevent or treat age-related diseases. There have been many studies dedicated to the relationship between protein oxidation and age-related pathology; now it is possible for researchers and readers to learn new techniques as utilizing protein oxidation products as biomarkers for aging.

Protein Oxidation and Aging begins with a description of the tremendous variety of protein oxidation products. Furthermore, it covers:

  • Major aspects of the protein oxidation process
  • Cellular mechanisms for managing oxidized proteins
  • Role of protein oxidation in aging
  • Influence of genetic and environmental factors on protein oxidation
  • Measuring protein oxidation in the aging process
  • Protein oxidation in age-related diseases

References at the end of each chapter serve as a gateway to the growing body of original research studies and reviews in the field.

Introduction to the Wiley Series on Protein and Peptide Science xi
Preface xiii 1 Oxidative Stress and Protein Oxidation 1 1.1 The Large
Variety of Protein Oxidation Products, 7 1.1.1 Primary Protein Oxidation
Products, 7 1.1.1.1 Carbon-Centered Radicals, 9 1.1.1.2 Thiyl Radicals, 13
1.1.1.3 Aromatic Ring-Derived Radicals, 13 1.1.1.4 Transfer between Sites,
16 1.1.2 Reactive Compounds Mediating in Protein Oxidation, 18 1.1.2.1
Hydroxyl Radical, 20 1.1.2.2 Superoxide Radicals, 21 1.1.2.3 Hydrogen
Peroxide, 24 1.1.2.4 Lipid Peroxyl Radicals, 24 1.1.2.5 Alkoxyl Radicals,
24 1.1.2.6 *NO and Peroxynitrite, 25 1.1.2.7 Hypochlorous Acid, 30 1.1.3
Enzymatic Systems Playing a Role in Protein Oxidation, 31 1.1.3.1 NADPH
Oxidase, 32 1.1.3.2 Lipoxygenases, 35 1.1.3.3 Protein Kinases, 35 1.1.3.4
Mixed-Function Oxidases, 36 1.1.3.5 Nitric Oxide Synthetase (NOS), 38
1.1.3.6 Myeloperoxidase, 41 1.1.3.7 Cyclooxygenase, 42 1.1.4 Protein
Oxidation in Cells and Cellular Structures, 43 1.1.4.1 Protein Oxidation in
Blood and Blood Cells, 43 1.1.4.2 Protein Oxidation of Glycolytic Enzymes
and Mitochondria, 46 1.1.4.2.1 Glycolytic Enzymes, 48 1.1.4.2.2 Aconitase,
49 1.1.4.2.3 Carnitine Palmitoyltransferase-1, 49 1.1.4.3 Cytochrome P450
Enzymes, 49 1.1.4.4 Protein Oxidation in the Nucleus and Chromatin, 50
1.1.4.4.1 Histone Modifi cation, 50 1.1.4.5 Protein Oxidation in the
Endoplasmic Reticulum, 52 1.1.4.6 Protein Oxidation in Peroxisomes, 54 1.2
Reversible Oxidative Modifi cations, 55 1.2.1 Methionine Sulfoxides and
Methionine Modifi cations, 55 1.2.2 Cysteine Modifi cations and Disulfi de
Bond Formation, 61 1.2.3 Surface Hydrophobicity Modifi cations, 64 1.3
Irreversible Oxidation Products, 64 1.3.1 Protein Oxidation and Enzymatic
Posttranslational Modifications, 65 1.3.2 Deamidation and Transamination, 66
1.3.3 Protein Glycation and AGEs, 67 1.3.3.1 Receptor for Advanced
Glycation End Products (RAGE), 75 1.3.3.2 Nepsilon-Carboxymethyllysine and
Nepsilon-Carboxyethyllysine, 76 1.3.3.3 Pentosidine, 76 1.3.4 Racemization,
77 1.3.5 Nitrosylation, 77 1.3.6 Tyrosyl Radicals and Nitrotyrosines, 78
1.3.6.1 Dityrosines, 79 1.3.7 Protein Carbonyls, 80 1.3.8 Aldehyde--Protein
Reactions, 81 1.3.8.1 MDA-Protein Adducts, 82 1.3.8.2
4-Hydroxy-2,3-Nonenal-Protein Adducts, 82 1.3.9 Cross-Linking of Proteins,
82 1.4 The Oxidation of Extracellular Matrix, Membrane and Cytoskeletal
Proteins, 83 1.4.1 Collagen, 84 1.4.2 Elastin, 95 1.4.3 The Oxidation of
Membrane Proteins, 97 1.4.4 Band 3, 97 1.4.5 Actin, 99 1.5 Mechanism and
Factors Influencing the Formation of Protein Oxidation Products, 100 1.5.1
Redox Status, 101 1.5.2 Protein Turnover, 106 1.5.3 Metal-Catalyzed
Oxidation (MCO), 107 1.5.4 Heat Shock Proteins, 109 1.6 Protein Aggregates:
Formation and Specific Metabolic Effects, 111 1.6.1 Accumulation of Oxidized
Proteins, 113 1.6.2 Lipofuscin and Ceroid, 115 1.7 Methods to Measure
Protein Oxidation Products in Research Laboratories, 119 1.7.1 Determination
of Methionine Sulfoxide Reduction and Methionine Oxidation, 120 1.7.2
Determination of Protein Glycation and Adducts, 121 1.7.3 Analysis of
Isoaspartate Formation, 122 1.7.4 Measurement of Fragmentation, 122 1.7.5
Measurement of Tyrosine Oxidation, 123 1.7.6 Protein Carbonyl Measurement,
124 1.7.7 Radioactive Labeling Protocols for Proteolysis and Aggregation
Measurements, 128 1.7.8 Standard Chromatographic Methods for the Measurement
of Protein Modifi cations, 132 1.7.9 Liquid Chromatography Techniques
Supported by Mass Spectrometry, 133 1.7.10 GC/MS, 134 1.7.11 Analysis of
Protein-Bound 3-Nitrotyrosine by a Competitive ELISA Method, 134 1.7.12
Protein Oxidation Products as Biomarkers in Clinical Science, 135
References, 139 2 Removal of Oxidized Proteins 215 2.1 The Limited Repair
of Some Oxidized Proteins, 216 2.1.1 Thiol Repair, 216 2.1.2 Methionine
Sulfoxide Reductases, 219 2.2 Proteolysis, 221 2.2.1 The Proteasomal System
and Its Role in the Degradation of Oxidized Proteins, 222 2.2.1.1 The
Ubiquitin--Proteasome System (UPS), 222 2.2.1.2 The Components of the UPS,
222 2.2.1.2.1 The 20S Proteasome, 222 2.2.1.2.2 The Inducible Forms of the
Proteasome and Their Function, 227 2.2.1.2.3 The 11S Regulator, 231
2.2.1.2.4 The 19S Regulator and the UPS, 233 2.2.1.2.5 The PA200 Regulator
Protein, 238 2.2.1.2.6 Cellular Proteasome Inhibitors, 239 2.2.1.3
Low-Molecular-Weight Proteasome Inhibitors, 239 2.2.1.4 Cellular Function of
the UPS, 241 2.2.1.5 The Degradation of Oxidized Proteins: A Function of the
20S Proteasome, 243 2.2.1.5.1 Early Studies on the Turnover of Oxidized
Proteins, 244 2.2.1.5.2 In Vitro Studies and the Recognition of Oxidized
Proteins by the Proteasome, 244 2.2.1.5.3 Cellular and In Vivo Studies of
the Degradation of Oxidized Proteins, 248 2.2.1.5.4 The Inhibition of the
Proteasome by Cross-Linked Oxidized Proteins and Proteasomal Regulation
during Oxidative Stress, 251 2.3 The Role of Other Proteases in the Fate of
Oxidized Proteins, 254 2.3.1 Lysosomal Degradation of Oxidized Proteins and
the Role of Autophagy, 254 2.3.2 Mitochondrial Degradation of Oxidized
Proteins and the Lon Protease, 256 2.3.3 The Uptake of Extracellular
Oxidized Proteins and the Role of the Proteasome in Their Degradation, 258
2.3.4 Calpains and the Degradation of Oxidized Proteins, 259 2.4 Role of
Heat Shock Proteins in Protein Degradation, 260 2.5 Conclusion, 262
References, 262 3 Protein Oxidation and Aging: Different Model Systems and
Affecting Factors 295 3.1 Protein Oxidation during Aging: Lower Organisms
and Cellular Model Systems, 297 3.1.1 Yeast, 297 3.1.1.1 Saccharomyces
cerevisiae, 297 3.1.1.2 Schizosaccharomyces pombe, 301 3.1.2 Podospora
anserina, 301 3.1.3 Bacteria, 302 3.1.3.1 Escherichia coli, 302 3.1.4 Cell
Cultures, 304 3.2 Nonmammalian Model Systems and the Accumulation of
Oxidized Proteins during Aging, 308 3.2.1 Caenorhabditis elegans, 308 3.2.2
Drosophila melanogaster, 310 3.2.3 Aquatic Systems, 313 3.2.4 Plants, 315
3.2.5 Amphibians, 317 3.3 Age-Related Protein Oxidation in Humans and
Mammals, 317 3.3.1 Humans, 317 3.3.2 Animals, 319 3.3.2.1 Rabbits, 323
3.3.2.2 Mice, 324 3.3.2.3 Rats, 327 3.3.2.4 Gerbils, 329 3.3.2.5 Primates,
330 3.4 Inherited Factors Influencing Protein Oxidation during Aging, 331
3.4.1 Genetic Instability, Mutations, and Polymorphism, 331 3.4.2 Gender,
333 3.4.3 Vitagenes, 334 3.4.4 Signal Transduction and Transcription
Factors, 335 3.4.5 Ion Channels, 340 3.5 Age-Related Protein Aggregate
Formation in Model Systems, 341 3.6 Environmental Factors Affecting Healthy
Aging, 342 3.6.1 UV-Induced Skin Photoaging and Skin Aging, 344 3.6.2
Pesticides, 348 3.6.3 Exercise, 349 3.6.4 Dietary Factors and Prevention
Strategies, 351 3.6.4.1 Melatonin, 353 3.6.4.2 Growth Hormone, 354 3.6.4.3
Biotrace Metal Elements: Zinc, 356 3.6.4.4 Ascorbic Acid, 357 3.6.4.5
Vitamin E, 360 3.6.4.6 Carnitine and Acetyl-L-Carnitine, 361 3.6.4.7
Homocysteine, 362 3.6.4.8 Ubiquinone, Coenzyme Q10, 363 3.6.4.9 Carnosine,
363 3.6.4.10 Lipoic Acid, 364 3.6.4.11 N-Acetyl-L-Cysteine, 365 3.6.5
Pharmacological Response and Biotransformation in Aging, 365 3.6.5.1 Plant
Extracts, 366 3.6.5.2 Polyphenols and Flavonoids, 366 3.6.5.3 Resveratrol,
367 3.6.5.4 AGE and ALE Inhibitors, 368 3.6.6 Caloric Restriction, 369 3.7
Repair and Degradation of Oxidized Proteins during Aging, 370 References,
372 4 Protein Oxidation in Some Age-Related Diseases 417 4.1 Protein
Oxidation during Neurodegeneration and Neurological Diseases, 417 4.1.1
Brain Aging, 418 4.1.2 Alzheimer's Disease, 420 4.1.3 Parkinson's Disease,
424 4.1.4 Huntington's Disease, 425 4.1.5 Stroke, 427 4.1.6 Amyotrophic
Lateral Sclerosis, 427 4.2 Protein Oxidation in Cardiac Diseases, 429 4.2.1
Ischemia--Reperfusion, 429 4.2.2 Atherosclerosis, 430 4.3 Protein Oxidation
in Diabetes, 431 4.4 Protein Oxidation in Degenerative Arthritis, 434 4.5
Protein Oxidation in Muscle Wasting and Sarcopenia, 435 4.6 Protein
Oxidation in Destructive Eye Diseases, 437 4.6.1 Age-Related Macular
Degeneration, 437 4.6.2 Cataract, 438 4.7 Protein Oxidation in
Osteoporosis, 440 4.8 Protein Oxidation in Cancer, 441 4.8.1 Proteasome
Inhibitors in Cancer Therapy, 444 4.9 Other Diseases, 446 4.9.1 Premature
Aging Diseases Progeria and Werner's Syndrome, 446 4.9.2 Renal Failure and
Hemodialysis in Elderly People, 447 4.9.3 Obesity, 447 4.9.4 Idiopathic
Pulmonary Fibrosis, 448 4.9.5 Presbycusis (Age-Related Hear Loss), 448
References, 448 List of Abbreviations 479 Index 493