Protein Carbonylation

Name: Protein Carbonylation | Principles, Analysis, and Biological Implications
Brand: Wiley
Price: 153.99 EUR
Availability: OnlineOnly

Principles, Analysis, and Biological Implications

Joaquim Ros(Herausgeber*in)

Wiley (Verlag)

Erschienen am 5. Mai 2017

416 Seiten

E-Book

PDF mit Adobe-DRM

Systemvoraussetzungen

978-1-119-37496-1 (ISBN)

153,99 €inkl. 7% MwSt.

Systemvoraussetzungen

für PDF mit Adobe-DRM

E-Book Einzellizenz

Als Download verfügbar

Beschreibung

Weitere Details

Weitere Ausgaben

Person

Inhalt

1 - Title Page [Seite 5]
2 - Copyright Page [Seite 6]
3 - Contents [Seite 7]
4 - List of Contributors [Seite 14]
5 - Preface [Seite 18]
6 - Chapter 1 Reactive Oxygen Species Signaling from the Perspective of the Stem Cell [Seite 19]
6.1 - 1.1 Introduction [Seite 19]
6.2 - 1.2 ROS Regulation [Seite 20]
6.3 - 1.3 ROS Signaling [Seite 21]
6.4 - 1.4 ROS and Stem Cells [Seite 23]
6.4.1 - 1.4.1 Adult Stem Cells [Seite 23]
6.4.2 - 1.4.2 Embryonic Stem Cells [Seite 25]
6.5 - 1.5 ROS, Metabolism, and Epigenetic Influence [Seite 27]
6.6 - 1.6 Stem Cells and Mitochondria [Seite 27]
6.7 - 1.7 ROS and Stem Cell Aging [Seite 30]
6.8 - 1.8 Concluding Remarks [Seite 31]
6.9 - References [Seite 31]
7 - Chapter 2 Analysis of Protein Carbonylation [Seite 42]
7.1 - 2.1 Introduction [Seite 42]
7.2 - 2.2 In Vivo Carbonylation Reactions [Seite 45]
7.2.1 - 2.2.1 Polypeptide Backbone Cleavage [Seite 46]
7.2.2 - 2.2.2 Carbonylation via Amino Acid Side Chain Oxidation [Seite 48]
7.2.3 - 2.2.3 Michael Addition of Carbonyl-Containing Group [Seite 49]
7.2.4 - 2.2.4 Oxidation of Glycated Proteins [Seite 50]
7.3 - 2.3 Analytical Derivatization of Carbonylated Groups [Seite 52]
7.4 - 2.4 Selective Purification and/or Detection of Carbonylated Proteins and Peptides [Seite 54]
7.4.1 - 2.4.1 Affinity Selection of 4-HNE Adducts as a Means of Purification [Seite 54]
7.4.2 - 2.4.2 Antibody-Based Detection of 2,4-DNP-Derivatized Proteins [Seite 54]
7.4.3 - 2.4.3 Biotinylated Protein Selection [Seite 55]
7.4.4 - 2.4.4 Fluorescence Detection [Seite 55]
7.5 - 2.5 Oxidative Stress-Based PTMS Not Involving Carbonylation [Seite 56]
7.6 - 2.6 Conclusion [Seite 56]
7.7 - References [Seite 58]
8 - Chapter 3 Diversity of Protein Carbonylation Pathways: Direct Oxidation, Glycoxidation, and Modifications by Lipid Peroxidation Products [Seite 66]
8.1 - 3.1 Introduction [Seite 66]
8.2 - 3.2 Pathways of Protein Carbonylation [Seite 67]
8.2.1 - 3.2.1 Direct Oxidation of Lys, Arg, Pro, and Thr Amino Acid Residues Side Chains [Seite 67]
8.2.2 - 3.2.2 Tryptophan Oxidation [Seite 70]
8.2.3 - 3.2.3 Protein Carbonylation via Backbone Cleavage [Seite 71]
8.2.4 - 3.2.4 Protein Carbonylation via Michael Addition of Reactive Lipid Peroxidation Products [Seite 71]
8.2.5 - 3.2.5 Protein Carbonylation via Glycoxidation and Reactions with Carbohydrate Autoxidation Products [Seite 73]
8.3 - 3.3 Analytical Methods for Detection of Total and Specific Protein Carbonylation [Seite 75]
8.3.1 - 3.3.1 Detection of Total Protein Carbonylation Using Carbonyl-Specific Derivatization [Seite 76]
8.3.2 - 3.3.2 Mass Spectrometry-Based Identification of Carbonylated Proteins, Types, and Sites of Modifications [Seite 79]
8.4 - 3.4 Protein Susceptibility to Different Carbonylation Pathways and Modifications Cross-Talk [Seite 85]
8.4.1 - 3.4.1 Susceptibility of Proteins to Carbonylation and Possible Sequence Motifs [Seite 85]
8.4.2 - 3.4.2 Protein Modifications Cross-Talk [Seite 87]
8.5 - 3.5 Conclusion [Seite 89]
8.6 - Acknowledgments [Seite 90]
8.7 - References [Seite 90]
9 - Chapter 4 Protein Carbonylation by Reactive Lipids [Seite 101]
9.1 - 4.1 Introduction [Seite 101]
9.2 - 4.2 Chemistry of Protein Carbonylation by Reactive Lipid Aldehydes [Seite 102]
9.3 - 4.3 Antigenicity of Protein Carbonyls [Seite 105]
9.4 - 4.4 Thiolation of Protein Carbonyls [Seite 107]
9.5 - 4.5 Reductive Amination-Based Fluorescent Labeling of Protein Carbonyls [Seite 109]
9.6 - 4.6 Conclusion [Seite 111]
9.7 - References [Seite 112]
10 - Chapter 5 Mechanism and Functions of Protein Decarbonylation [Seite 115]
10.1 - 5.1 Protein Carbonylation [Seite 115]
10.2 - 5.2 Primary Protein Carbonylation in Cell Signaling [Seite 116]
10.3 - 5.3 Discovery and Mechanisms of Protein Decarbonylation [Seite 119]
10.4 - 5.4 Proposed Functions of Protein Decarbonylation in Oxidative Stress and Redox Signaling [Seite 121]
10.5 - Acknowledgments [Seite 125]
10.6 - References [Seite 125]
11 - Chapter 6 Carbonylated Proteins and Their Metabolic Regulation: Overview of Mechanisms, Target Proteins, and Characterization Using Proteomic Methods [Seite 128]
11.1 - 6.1 Metabolic Regulation and Reactive Oxygen Species [Seite 128]
11.2 - 6.2 ROS and Protein Carbonylation [Seite 129]
11.3 - 6.3 Metabolic Control and Characteristics of Carbonylated Proteins [Seite 131]
11.4 - 6.4 Protein Targets of Carbonylation and Implications in Human Health [Seite 132]
11.5 - 6.5 Technologies and Methods for Characterizing Protein Carbonylation [Seite 136]
11.6 - 6.6 Emerging Multifunctional Reagents for Protein Carbonylation Analysis via MS [Seite 137]
11.7 - 6.7 Emerging Methods for Characterizing Carbonylated Protein Networks and Affected Pathways [Seite 141]
11.8 - 6.8 Conclusion [Seite 143]
11.9 - References [Seite 143]
12 - Chapter 7 Oxidative Stress and Protein Carbonylation in Malaria [Seite 149]
12.1 - 7.1 Introduction [Seite 149]
12.2 - 7.2 Oxidative Stress during Malaria Infection [Seite 150]
12.3 - 7.3 Protein Carbonylation in Plasmodium and Oxidative Targeting of Antimalarials [Seite 155]
12.4 - 7.4 Oxidative Dysfunction in Host Tissues [Seite 161]
12.4.1 - 7.4.1 Cerebral Malaria [Seite 162]
12.4.2 - 7.4.2 Acute Kidney Injury [Seite 163]
12.4.3 - 7.4.3 Severe Anemia [Seite 163]
12.4.4 - 7.4.4 Liver Failure [Seite 164]
12.4.5 - 7.4.5 Pregnancy [Seite 165]
12.4.6 - 7.4.6 Pulmonary Edema [Seite 165]
12.4.7 - 7.4.7 Acidosis and Hypoglycemia [Seite 165]
12.5 - 7.5 Host Tolerance to Malaria by Modulation of Oxidative Stress Responses [Seite 166]
12.6 - 7.6 Perspectives [Seite 171]
12.7 - References [Seite 171]
13 - Chapter 8 Protein Carbonylation in Brains of Subjects with Selected Neurodegenerative Disorders [Seite 185]
13.1 - 8.1 Introduction to Protein Carbonylation [Seite 185]
13.2 - 8.2 Relationship between ROS and Oxidative Stress [Seite 187]
13.3 - 8.3 An Overview of Some Neurodegenerative Diseases [Seite 189]
13.3.1 - 8.3.1 Alzheimer Disease [Seite 190]
13.3.2 - 8.3.2 Stages of Alzheimer Disease [Seite 191]
13.3.3 - 8.3.3 Preclinical Alzheimer Disease [Seite 191]
13.3.4 - 8.3.4 Mild Cognitive Impairment [Seite 191]
13.3.5 - 8.3.5 Early-Stage Alzheimer Disease [Seite 192]
13.3.6 - 8.3.6 Late-Stage Alzheimer Disease [Seite 192]
13.4 - 8.4 Role of Protein Carbonylation in Brains of Subjects with AD [Seite 192]
13.4.1 - 8.4.1 Brain Proteins Carbonylated in AD [Seite 193]
13.4.2 - 8.4.2 Brain Proteins Carbonylated in MCI [Seite 196]
13.5 - 8.5 An Introduction to Tauopathies [Seite 203]
13.5.1 - 8.5.1 Role of Protein Carbonylation in Brain in Tauopathies [Seite 204]
13.6 - 8.6 An Introduction to Amyotrophic Lateral Sclerosis [Seite 204]
13.6.1 - 8.6.1 Role of CNS Protein Carbonylation in ALS [Seite 205]
13.7 - 8.7 Discussion [Seite 206]
13.8 - References [Seite 207]
14 - Chapter 9 Cigarette Smoke-Induced Protein Carbonylation: Focus on Recent Human Studies [Seite 224]
14.1 - 9.1 Introduction [Seite 224]
14.1.1 - 9.1.1 Reactive Species of CS and CS-Induced Oxidative Stress [Seite 226]
14.1.2 - 9.1.2 Protein Carbonylation [Seite 227]
14.1.3 - 9.1.3 Methodological Aspects of Protein Carbonylation Detection [Seite 228]
14.2 - 9.2 Protein Carbonylation in Human Smokers [Seite 230]
14.2.1 - 9.2.1 CS-Induced Carbonylation of Salivary Proteins [Seite 230]
14.2.2 - 9.2.2 CS-Induced Protein Carbonylation in the Respiratory System [Seite 230]
14.2.3 - 9.2.3 CS-Induced Protein Carbonylation in the Circulatory System [Seite 234]
14.2.4 - 9.2.4 CS-Induced Protein Carbonylation in the Muscular System [Seite 235]
14.3 - 9.3 Protein Carbonylation in Cultured Human Cell Models of Exposure to CS [Seite 236]
14.3.1 - 9.3.1 In Vitro Models of Exposure to CS [Seite 236]
14.3.2 - 9.3.2 CS-Induced Protein Carbonylation in Oral Cavity Cells [Seite 239]
14.3.3 - 9.3.3 CS-Induced Protein Carbonylation in Airway Epithelial Cells [Seite 242]
14.3.4 - 9.3.4 CS-Induced Protein Carbonylation in Other Epithelial Cells [Seite 244]
14.4 - 9.4 Limitations and Congruence of In Vivo and In Vitro Human Studies [Seite 246]
14.4.1 - 9.4.1 Limitations of In Vivo Human Studies [Seite 246]
14.4.2 - 9.4.2 Limitations of In Vitro Human Studies [Seite 246]
14.4.3 - 9.4.3 Congruence between Findings in Human Smokers and in Human Cell Models of Exposure to CS [Seite 247]
14.5 - 9.5 Conclusion and Future Perspectives [Seite 248]
14.6 - Acknowledgments [Seite 249]
14.7 - References [Seite 249]
15 - Chapter 10 Chronic Obstructive Pulmonary Disease and Oxidative Damage [Seite 259]
15.1 - 10.1 Introduction [Seite 260]
15.2 - 10.2 Protein Oxidation in Tissues [Seite 262]
15.2.1 - 10.2.1 Production of Oxidants in the Skeletal Muscle Fibers [Seite 264]
15.3 - 10.3 Antioxidants in Skeletal Muscle Fibers [Seite 265]
15.4 - 10.4 Implications of Protein Carbonylation in COPD Skeletal Muscle Dysfunction [Seite 267]
15.4.1 - 10.4.1 Identification of Skeletal Muscle Dysfunction in COPD [Seite 267]
15.4.2 - 10.4.2 Evidence of Protein Carbonylation in Skeletal Muscles of COPD Patients [Seite 268]
15.4.3 - 10.4.3 Biological Significance of Protein Carbonylation in COPD Muscles [Seite 268]
15.5 - 10.5 Muscle Protein Carbonylation and Exercise in COPD Patients [Seite 270]
15.6 - 10.6 Protein Carbonylation in Muscles Exposed to Chronic Cigarette Smoke [Seite 271]
15.6.1 - 10.6.1 Studies in Humans [Seite 271]
15.6.2 - 10.6.2 Studies in Animals [Seite 271]
15.7 - 10.7 Protein Carbonylation in Cancer Cachexia Models [Seite 273]
15.7.1 - 10.7.1 Evidence of Protein Carbonylation in Muscles of Cancer Cachexia Models [Seite 273]
15.7.2 - 10.7.2 Protein Oxidation in Cancer Cachectic Muscles [Seite 273]
15.7.2.1 - 10.7.2.1 Studies in Humans [Seite 273]
15.7.2.2 - 10.7.2.2 Cachexia in COPD and Lung Cancer [Seite 274]
15.7.2.3 - 10.7.2.3 Studies in Animals [Seite 274]
15.8 - 10.8 Protein Carbonylation as a Predisposing Mechanism of Lung Cancer in COPD [Seite 275]
15.8.1 - 10.8.1 Protein Oxidation as a Contributing Factor to Lung Cancer in Patients [Seite 275]
15.8.2 - 10.8.2 Evidence of Protein Oxidation in Lung Cancer [Seite 276]
15.8.2.1 - 10.8.2.1 Human Studies [Seite 276]
15.8.2.2 - 10.8.2.2 Studies in Animals [Seite 277]
15.9 - 10.9 Conclusion and Future Perspectives [Seite 277]
15.10 - Acknowledgments [Seite 278]
15.11 - References [Seite 278]
16 - Chapter 11 Protein Carbonylation in Aging and Senescence [Seite 290]
16.1 - 11.1 Introduction [Seite 290]
16.2 - 11.2 Protein Oxidation during Aging [Seite 292]
16.3 - 11.3 Chemistry of Protein Carbonylation and Fate of Carbonylated Proteins [Seite 295]
16.4 - 11.4 Protein Carbonyls in Cellular Aging Models [Seite 297]
16.5 - 11.5 Protein Carbonylation in Aging Organisms [Seite 298]
16.6 - 11.6 Concluding Remarks [Seite 300]
16.7 - References [Seite 301]
17 - Chapter 12 Adipose Carbonylation and Mitochondrial Dysfunction [Seite 309]
17.1 - 12.1 Introduction [Seite 309]
17.2 - 12.2 Reactive Oxygen Species (ROS) [Seite 310]
17.2.1 - 12.2.1 Metabolism of Reactive Lipid Aldehydes [Seite 315]
17.3 - 12.3 Oxidative Stress and Obesity [Seite 316]
17.3.1 - 12.3.1 Oxidative Stress in Obese Adipose Tissue [Seite 316]
17.3.2 - 12.3.2 Protein Carbonylation in the Adipocyte [Seite 318]
17.3.3 - 12.3.3 Additional Outcomes of Oxidative Stress in Fat Cells [Seite 320]
17.4 - 12.4 Detection of Protein Carbonylation [Seite 321]
17.4.1 - 12.4.1 Chemical Derivatization Using Carbonyl-Reactive Probes [Seite 321]
17.5 - 12.5 Outcomes of Protein Carbonylation [Seite 324]
17.5.1 - 12.5.1 Modification of Proteins by 4-HNE and Altered Function [Seite 325]
17.5.2 - 12.5.2 Carbonylation in Cell Signaling [Seite 327]
17.5.3 - 12.5.3 Carbonylation and Mitochondrial Dysfunction [Seite 328]
17.5.4 - 12.5.4 Carbonylation in Human Adipose Tissue [Seite 330]
17.6 - 12.6 Concluding Remarks [Seite 331]
17.7 - Acknowledgments [Seite 332]
17.8 - References [Seite 332]
18 - Chapter 13 Protein Carbonylation in Plants [Seite 339]
18.1 - 13.1 Introduction [Seite 340]
18.2 - 13.2 Turnover of Reactive Oxygen Species in Plants [Seite 341]
18.2.1 - 13.2.1 ROS Are Produced at Multiple Sites in the Plant Cell [Seite 341]
18.2.2 - 13.2.2 Different Types of ROS Are Produced in Different Cellular Compartments [Seite 341]
18.2.3 - 13.2.3 Free Metal Ions Catalyze the Fenton Reaction [Seite 341]
18.2.4 - 13.2.4 Many Enzyme (Systems) Can Remove ROS [Seite 342]
18.2.5 - 13.2.5 The Cellular Steady-State Level of Hydrogen Peroxide Is in the Micromolar Range [Seite 342]
18.2.6 - 13.2.6 Fatty Acid Peroxidation Products Can Accumulate to High Levels in Plant Cells [Seite 342]
18.3 - 13.3 Methods Used in Plants for Quantifying and Identifying Carbonylation Sites [Seite 343]
18.4 - 13.4 Protein Carbonylation in Plants [Seite 344]
18.4.1 - 13.4.1 Physiological Importance [Seite 344]
18.4.2 - 13.4.2 Overall Level [Seite 344]
18.4.3 - 13.4.3 Carbonylation Site [Seite 345]
18.4.4 - 13.4.4 Effect of Carbonylation on Affected Proteins [Seite 345]
18.5 - 13.5 Protein Carbonylation in Plant Mitochondria [Seite 346]
18.5.1 - 13.5.1 ROS Are Produced at Several Places in the Mitochondria [Seite 346]
18.5.2 - 13.5.2 Many Mitochondrial Proteins Are Carbonylated [Seite 346]
18.5.3 - 13.5.3 Many Mitochondrial Proteins Are Conjugated with HNE [Seite 348]
18.5.4 - 13.5.4 Carbonylated Proteins Are Degraded [Seite 348]
18.6 - 13.6 Protein Carbonylation in Seeds [Seite 351]
18.6.1 - 13.6.1 Metabolic Activity Determines the Steady-State Oxygen Concentration inside the Seed [Seite 351]
18.6.2 - 13.6.2 Recalcitrant Seeds Accumulate Carbonylated Proteins during Desiccation [Seite 351]
18.6.3 - 13.6.3 Protein Carbonylation Plays a Role in Breaking Seed Dormancy [Seite 352]
18.6.4 - 13.6.4 Protein Carbonylation Increases with Seed Aging [Seite 352]
18.6.5 - 13.6.5 Protein Carbonylation Increases during Germination [Seite 352]
18.6.6 - 13.6.6 Protein Carbonylation Is Involved in Many Aspects of Seed Physiology [Seite 353]
18.7 - 13.7 Perspectives [Seite 353]
18.8 - Acknowledgments [Seite 353]
18.9 - References [Seite 354]
19 - Chapter 14 Specificity of Protein Carbonylation and Its Relevance in Aging [Seite 358]
19.1 - 14.1 Introduction [Seite 358]
19.2 - 14.2 Specificity of Protein Oxidative Damage [Seite 359]
19.2.1 - 14.2.1 Location [Seite 360]
19.2.2 - 14.2.2 Metals [Seite 363]
19.2.3 - 14.2.3 Sequences Prone to Carbonylation [Seite 364]
19.2.4 - 14.2.4 Nucleotide-Binding Proteins [Seite 365]
19.3 - 14.3 Protein Carbonylation in Aging [Seite 366]
19.3.1 - 14.3.1 Bacteria [Seite 375]
19.3.2 - 14.3.2 Yeast [Seite 377]
19.3.3 - 14.3.3 Plants [Seite 379]
19.3.4 - 14.3.4 Invertebrate Animals [Seite 380]
19.3.5 - 14.3.5 Rodents [Seite 382]
19.3.6 - 14.3.6 Humans [Seite 384]
19.3.7 - 14.3.7 Calorie Restriction, Protein Oxidation, and Aging [Seite 386]
19.3.8 - 14.3.8 "Aging" In Vitro: Storage of Protein Preparations [Seite 387]
19.4 - 14.4 Concluding Remarks [Seite 388]
19.5 - Acknowledgments [Seite 389]
19.6 - References [Seite 389]
20 - Index [Seite 402]
21 - Series Editors [Seite 417]
22 - EULA [Seite 419]

Systemvoraussetzungen

Als PDF speichern Als Link merken