Redox Proteomics From Protein Modifications to Cellular Dysfunction and Diseases

, by Dalle-Donne, Isabella; Scaloni, Andrea; Butterfield, D. Allan; Desiderio, Dominic M.; Nibbering, Nico M.

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ISBN: 9780471723455 | 0471723452
Cover: Hardcover
Copyright: 6/12/2006

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Methodology and applications of redox proteomics The relatively new and rapidly changing field of redox proteomics has the potential to revolutionize how we diagnose disease, assess risks, determine prognoses, and target therapeutic strategies for people with inflammatory and aging-associated diseases. This collection brings together, in one comprehensive volume, a broad array of information and insights into normal and altered physiology, molecular mechanisms of disease states, and new applications of the rapidly evolving techniques of proteomics.Written by some of the finest investigators in this area, Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases examines the key topics of redox proteomics and redox control of cellular function, including: The role of oxidized proteins in various disorders Pioneering studies on the development of redox proteomics Analytical methodologies for identification and structural characterization of proteins affected by oxidative/nitrosative modifications The response and regulation of protein oxidation in different cell types The pathological implications of protein oxidation for conditions, including asthma, cardiovascular disease, diabetes, preeclampsia, and Alzheimer's disease Distinguished by its in-depth discussions, balanced methodological approach, and emphasis on medical applications and diagnosis development, Redox Proteomics is a rich resource for all professionals with an interest in proteomics, cellular physiology and its alterations in disease states, and related fields.

Preface

xxiii

Contributors

xxvii

PART I OXIDATIVELY MODIFIED PROTEINS AND PROTEOMIC TECHNOLOGIES

(342)

1 Chemical Modification of Proteins by Reactive Oxygen Species

(22)

Earl R. Stadtman and Rodney L. Levine

1.1 Introduction,

(2)

1.2 Peptide Bond Cleavage,

(1)

1.3 β-Scission,

(1)

1.4 Oxidation of Amino Acid Residue Side Chains,

(18)

1.4.1 Oxidation of Aromatic and Heterocyclic Amino Acid Residues,

(1)

1.4.2 Methionine Oxidation,

(2)

1.4.3 Protein Carbonylation,

(1)

1.4.4 Protein–Protein Cross-Linkage,

(1)

1.4.5 Protein Modification by Reactive Nitrogen Species,

(1)

1.4.6 Chlorination Reactions,

(2)

1.4.7 Accumulation of Oxidized Proteins,

(12)

2 The Chemistry of Protein Modifications Elicited by Nitric Oxide and Related Nitrogen Oxides

(34)

Douglas D. Thomas, Lisa Ridnour, Sonia Donzelli, Michael Graham Espey, Daniele Mancardi, Jeffery S. Isenberg, Martin Feelisch, David D. Roberts, and David A. Wink

2.1 Introduction,

(1)

2.2 Chemical Biology of NO,

(14)

2.2.1 Direct Effects,

(3)

2.2.2 Indirect Mechanisms,

(9)

2.3 Chemistry of Metabolite Formation,

(19)

2.3.1 Nitrite and Nitrate Formation,

(1)

2.3.2 Metal Nitrosyl Formation,

(1)

2.3.3 Nitrosation,

(2)

2.3.4 Nitration,

(16)

3 Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively/Nitrosatively Modified Proteins

(42)

Andrea Scaloni

3.1 Introduction,

(2)

3.2 Mass Spectrometry Analysis of Oxidatively/Nitrosatively Modified Proteins,

(15)

3.2.1 Analysis of Oxidized/Nitrosated Products of Protein Thiols,

(3)

3.2.2 Analysis of Oxidized/Nitrated Products of Tyrosine,

(4)

3.2.3 Analysis of Oxidized Products of Methionine,

(1)

3.2.4 Analysis of Protein Carbonylation Products,

(3)

3.2.5 Analysis of Oxidatively/Nitr(os)atively Products of Tryptophan and Histidine,

(2)

3.3 Proteornic Strategies for the Identification of ROS/RNS Protein Targets in Biological Matrices,

(8)

3.4 Conclusions,

(17)

4 Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics

101

(22)

Valentina Bonetto and Pietro Ghezzi

4.1 Introduction: Protein Thiols from Oxidative Stress to Redox Regulation,

101

(1)

4.2 Different Redox States of Protein Cysteines,

102

(2)

4.2.1 Disulfides,

102

(1)

4.2.2 Mixed Disulfides,

103

(1)

4.2.3 Higher Oxidation States,

104

(1)

4.3 Methodologies to Identify and Quantify the Redox State of Protein Cysteines,

104

(4)

4.3.1 Methods Based on Reagents That Label Free Cysteine,

104

(2)

4.3.2 Methods Based on Different Electrophoretic Mobility: Diagonal Electrophoresis,

106

(2)

4.4 Methods to Detect Specific Modifications,

108

(3)

4.4.1 Methods Based on a Series of Alkylation, Reduction, and Labeling Steps,

108

(1)

4.4.2 Methods Based on Incorporation of Labeled Glutathione to Identify Glutathionylated Proteins,

108

(2)

4.4.3 Immunological Methods,

110

(1)

4.5 Methods for Enriching Redox-Regulated Proteins,

111

(1)

4.5.1 Enrichment of Proteins with Specific Forms of Cysteine Oxidation,

111

(1)

4.5.2 Membrane Proteins,

112

(1)

4.6 Structural and Physicochemical Determinants for the Susceptibility of Cysteines toward Oxidation,

112

(2)

4.7 Perspective,

114

(9)

5 Carbonylated Proteins and Their Implication in Physiology and Pathology

123

(46)

Rodney L. Levine and Earl. R. Stadtman

5.1 Introduction,

123

(10)

5.2 Types of Oxidative Modifications and Choice of Marker,

133

(1)

5.3 Methodological Considerations,

134

(2)

5.4 Selected Studies,

136

(1)

5.5 Carbonylation during Aging,

136

(33)

6 S-Nitrosation of Cysteine Thiols as a Redox Signal

169

(20)

Yanhong Zhang and Neil Hogg

6.1 Introduction,

169

(1)

6.2 Mechanisms of Formation of S-Nitrosothiols,

170

(6)

6.3 Cellular Transduction of the S-Nitroso Group,

176

(2)

6.4 S-Nitrosothiols and Redox Proteomics,

178

(1)

6.5 S-Nitrosothiols as an Intracellular Signal,

179

(3)

6.6 Conclusions,

182

(7)

7 Detection of Glycated and Glyco-Oxidated Proteins

189

(44)

Annunziata Lapolla, Elisa Basso, and Pietro Traldi

7.1 Introduction,

189

(7)

7.2 MALDI-MS in the Study of In vitro Glycated Proteins,

196

(5)

7.3 MALDI-MS in the Evaluation of Glycation Levels of HSA and IgG in Diabetic Patients,

201

(4)

7.4 HbAI, and the Real Globin Glycation and Glyco-Oxidation,

205

(4)

7.5 Determination of Dicarbonyl Compound Levels in Diabetic and Nephropathic Patients,

209

(3)

7.6 AGE/Peptides: An In vitro Study and In vivo Preliminary Results,

212

(14)

7.7 Expected Future Trends,

226

(7)

8 MudPIT (Multidimensional Protein Identification Technology) for Identification of Post-translational Protein Modifications in Complex Biological Mixtures

233

(20)

Stefani N. Thomas, Bing-Wen Lu, Tatiana Nikolskaya, Yuri Nikolsky, and Austin J. Yang

8.1 Introduction,

233

(1)

8.2 Proteomic Analysis of Oxidatively Modified Proteins,

234

(7)

8.2.1 Affinity Purification of Carbonylated Proteins,

234

(4)

8.2.2 MudPIT Incorporating Liquid Chromatography–Tandem Mass Spectrometry (LC-MS/MS),

238

(1)

8.2.3 MudPIT Analysis of Carbonylated Proteins in Mouse Brain,

239

(1)

8.2.4 Peptide Sequencing and Protein Assignment via Database Searching of MS/MS Spectra,

240

(1)

8.2.5 Bioinformatic Determination of Amino Acid Sites of Post-translational Oxidative Modifications,

241

(1)

8.3 Statistical Validation and Interpretation of MudPIT Data,

241

(8)

8.3.1 Statistical Models to Assess the Quality of Peptide and Protein Assignments,

242

(2)

8.3.2 Issues to Consider in the Statistical Validation of Proteomic Data Sets.

244

(3)

8.3.3 Functional Categorization and Pathway Analysis of Proteomic Data Sets,

247

(2)

8.4 Concluding Remarks,

249

(4)

9 Use of a Proteomic Technique to Identify Oxidant-Sensitive Thiol Proteins in Cultured Cells

253

(14)

Mark B. Hampton, James W. Baty, and Christine C. Winterbourn

9.1 Introduction,

253

(1)

9.2 Fluorescence Labeling and Proteomic Analysis of Oxidized Thiol Proteins,

254

(2)

9.3 Detection of Thiol Protein Oxidation in Jurkat Cells,

256

(2)

9.4 Detection of Reversible and Irreversible Thiol Oxidation,

258

(1)

9.5 Oxidized Thiol Compared with Reduced Thiol Measurements,

259

(1)

9.6 More Selective Thiol Labeling Protocols,

260

(1)

9.7 Identification of Oxidant-Sensitive Proteins,

261

(1)

9.8 Conclusions and Future Directions,

261

(6)

10 ICAT (Isotope-Coded Affinity Tag) Approach to Redox Proteomics: Identification and Quantification of Oxidant-Sensitive Protein Thiols

267

(1)

Mahadevan Sethuraman, Mark E. McComb, Hua Huang, Sequin Huang, Tyler Heibeck, Catherine E. Costello, and Richard A. Cohen

10.1 Introduction,

267

(1)

10.2 Oxidant-Sensitive Cys,

268

(1)

10.3 Challenges in Redox Proteomics,

268

(1)

10.4 Iodoacetamide-Based Redox Proteomics,

269

(2)

10.5 ICAT Approach to Redox Proteomics,

271

(1)

10.6 Validation of the ICAT Approach Using the Recombinant Protein Creatine Kinase,

271

(4)

10.7 ICAT Approach to the Complex Protein Mixtures,

275

(7)

10.8 Perspectives,

282

(5)

11 Quantitative Determination of Free and Protein-Associated 3-Nitrotyrosine and S-Nitrosothiols in the Circulation by Mass Spectrometry and Other Methodologies: A Critical Review and Discussion from the Analytical and Review Point of View

287

(1)

Dimitrios Tsikas

11.1 Introduction,

287

(8)

11.1.1 The L-Arginine/Nitric Oxide Pathway as a Producer of Reactive Nitrogen Species,

287

(2)

11.1.2 S-Nitrosothiols,

289

(3)

11.1.3 3-Nitrotyrosine,

292

(2)

11.1.4 Quantity of Circulating S-Nitrosothiols and 3-Nitrotyrosine as Indicator of Health and Disease,

294

(1)

11.2 Methods of Analysis,

295

(19)

11.2.1 General Considerations,

295

(4)

11.2.2 Methodological Problems and Pitfalls,

299

(5)

11.2.3 Mass Spectrometry Based Methodologies,

304

(10)

11.3 S-Nitrosothiols and 3-Nitrotyrosine in Health and Disease,

314

(12)

11.3.1 S-Nitrosothiols,

315

(7)

11.3.2 3-Nitrotyrosine,

322

(4)

11.4 Considerations from the Analytical and Review Points of View,

326

(3)

11.4.1 Aspects of Method Validation and Quality Control,

326

(2)

11.4.2 Considerations from the Review Point of View,

328

(1)

11.5 Concluding Remarks and Future Prospects,

329

(14)

PART II CELLULAR ASPECTS OF PROTEIN OXIDATION

343

(1)

12 The Covalent Advantage: A New Paradigm for Cell Signaling Mediated by Thiol Reactive Lipid Oxidation Products

345

(140)

Dale A. Dickinson, Victor M. Darley-Usmar, and Aimee Landar

12.1 Introduction,

345

(1)

12.2 Cyclooxygenase and the Conversion of Nonreactive Lipids to Thiol Switching Molecules,

346

(3)

12.3 Lipid Peroxidation and the Nonenzymatic Formation of Lipid Adducts Capable of Modifying Proteins,

349

(2)

12.4 The Thiol Switch and Redox Cell Signaling,

351

(2)

12.5 Biological Responses to Endogenous Electrophilic Lipid Production,

353

(1)

12.6 A New Paradigm of Oxidized Lipid Signaling The Covalent Advantage,

353

(3)

12.7 Implications for the Pathophysiology of Disease,

356

(2)

12.8 Summary,

358

(11)

13 Early Molecular Events during Response to Oxidative Stress in Human Cells by Differential Proteomics

369

(1)

Gianluca Tell

13.1 Introduction,

369

(5)

13.1.1 General Overview on Cellular Redox State,

369

(1)

13.1.2 Major Types of Oxygen Free Radicals and Their Derivatives,

370

(3)

13.1.3 A Model of Redox Signaling Is Represented by Cellular Oxidative Stress Response,

373

(1)

13.2 Cellular Response to Oxidative Stress: From Membrane Receptors to Gene Expression Control,

374

(8)

13.2.1 The Problem of the Pritnummovens (Redox Sensors) in Monitoring the Intracellular Redox State and Its Conversion into a Biological Response: The Role of "Antenna" Molecules,

375

(1)

13.2.2 Role of Kinases, Phosphatases, and Intracellular Redox Sensors in Redox Signaling,

376

(6)

13.3 Gene Expression Control during Cell Response to Oxidative Stress: Redox-Regulated Transcription Factors,

382

(1)

13.4 The Power of Differential Proteomics in Detecting Early Molecular Markers of Oxidative Stress: Examples from Human Cell Lines,

383

(5)

13.5 Conclusions,

388

(11)

14 Oxidative Damage to Proteins: Structural Modifications and Consequences in Cell Function

399

(1)

Elisa Cabiscol and Joaquim Ros

14.1 Introduction,

399

(1)

14.2 Glycolysis,

400

(26)

14.2.1 Fructose 1,6-Bisphosphate Aldolase,

400

(21)

14.2.2 Triose Phosphate Isomerase,

421

(1)

14.2.3 Glyceraldehyde 3-Phosphate Dehydrogenase,

422

(2)

14.2.4 Enolase,

424

(2)

14.3 Pyruvate Metabolism,

426

(6)

14.3.1 Pyruvate Dehydrogenase Complex,

427

(2)

14.3.2 Pyruvate Decarboxylase,

429

(1)

14.3.3 Alcohol Dehydrogenase,

430

(1)

14.3.4 Alcohol Dehydrogenase E,

431

(1)

14.4 Tricarboxylic Acid Cycle,

432

(5)

14.4.1 Aconitase,

433

(3)

14.4.2 Alpha-Ketoglutarate Dehydrogenase Complex,

436

(1)

14.5 Electron Transport Chain and Oxidative Phosphorylation,

437

(6)

14.5.1 Complex I,

438

(1)

14.5.2 Complex II,

439

(1)

14.5.3 Complex III,

440

(1)

14.5.4 Complex IV,

441

(1)

14.5.5 Complex V,

442

(1)

14.6 Antioxidant Defenses,

443

(4)

14.6.1 Superoxide Di smutase,

444

(1)

14.6.2 Catalase,

445

(1)

14.6.3 Glutathione Peroxidase,

446

(1)

14.7 Molecular Chaperones,

447

(4)

14.7.1 Hsp70,

448

(1)

14.7.2 Hsp60,

449

(1)

14.7.3 Chaperones of Endoplasmic Reticulum,

450

(1)

14.7.4 Alpha-Crystallin,

451

(1)

14.8 Cytoskeleton,

451

(3)

14.9 Conclusions,

454

(19)

15 Oxidative Damage and Cellular Senescence: Lessons from Bacteria and Yeast

473

(1)

Thomas Nystrom

15.1 Microbial Senescence,

473

(1)

15.2 Protein Carbonylation—An Irreversible Oxidative Damage to Proteins,

474

(2)

15.3 Bacterial Senescence and Protein Carbonylation,

476

(2)

15.4 Replicative Senescence and Segregation of Carbonylated Proteins,

478

(1)

15.5 Yeast Senescence, Protein Oxidation, and Oncogenesis,

479

(1)

15.6 Perspective,

479

(6)

PART III REDOX PROTEOMIC ANALYSIS IN HUMAN DISEASES

485

(1)

16 Proteins as Sensitive Biomarkers of Human Conditions Associated with Oxidative Stress

487

(444)

Isabella Dalle-Donne, Ranieri Rossi, Fabrizio Ceciliani, Daniela Giustarini, Roberto Colombo, and Aldo Milzani

16.1 Introduction,

487

(2)

16.2 Oxidative Stress in Human Diseases and Animal Models,

489

(4)

16.3 Biomarkers of Oxidative Stress Status (BOSS),

493

(11)

16.3.1 Glutathione,

496

(2)

16.3.2 Oxidative DNA Damage,

498

(1)

16.3.3 Lipid Peroxidation Products,

499

(5)

16.4 Proteins as Biomarkers of Oxidative Stress Status,

504

(8)

16.4.1 Protein Carbonyls,

505

(2)

16.4.2 Oxidative Tyrosine Modifications,

507

(2)

16.4.3 S-Nitrosation and S-Glutathionylation,

509

(1)

16.4.4 Methionine Oxidation,

509

(1)

16.4.5 Pros and Cons of Using Proteins as Biomarkers of Oxidative Damage,

510

(2)

16.5 Conclusions,

512

(15)

17 Degradation and Accumulation of Oxidized Proteins in Age-Related Diseases

527

(1)

Peter Voss and Tilman Grune

17.1 Oxidative Modifications of Amino Acids and Protein Damage,

527

(5)

17.1.1 Oxidative Modifications of Amino Acids in Proteins,

528

(3)

17.1.2 Cross-Linking of Proteins due to Oxidation,

531

(1)

17.2 Degradation and Accumulation of Oxidatively Modified Proteins,

532

(11)

17.2.1 Degradation of Oxidatively Modified Proteins,

532

(9)

17.2.2 Accumulation of Oxidized Proteins,

541

(1)

17.2.3 The Vicious Cycle of Accumulation of Oxidatively Damaged Proteins and Decreased Proteolysis,

542

(1)

17.3 Oxidized Proteins in Age-Related Diseases,

543

(4)

17.4 Summary,

547

(16)

18 Redox Proteomics: A New Approach to Investigate Oxidative Stress in Alzheimer's Disease

563

(1)

D. Allan Butterfield, Rukhsana Sultana, and H. Fai Poon

18.1 Introduction,

563

(2)

18.2 Brain Tissue and Models Used in Studying Aβ(1-42)-Induced Oxidative Stress and Neurotoxicity in AD,

565

(2)

18.2.1 AD Brain Tissue,

565

(1)

18.2.2 Senescence-Accelerated Mice Prone 8 (SAMP8),

565

(1)

18.2.3 Aβ(1-42) In vivo,

566

(1)

18.2.4 Aβ(1-42) In vitro,

566

(1)

18.2.5 Caenorhabditis elegans (C. elegans),

567

(1)

18.3 Redox Proteomics,

567

(5)

18.3.1 Sample Preparation,

567

(1)

18.3.2 Two-dimensional (2D) Gel Electrophoresis,

567

(2)

18.3.3 Image Analysis and Statistical Analysis,

569

(1)

18.3.4 In-gel Digestion and Mass Spectrometry,

570

(2)

18.3.5 Bioinformatics and Identification,

572

(1)

18.4 Oxidatively Modified Proteins in AD and AD Models by Redox Proteomics,

572

(13)

18.4.1 Oxidatively Modified Proteins in AD Brain Tissue,

572

(5)

18.4.2 Oxidatively Modified Proteins in Aged Senescence-Accelerated Mice Prone 8 (SAMP8),

577

(2)

18.4.3 Oxidatively Modified Proteins by Aβ(1-42) In vivo,

579

(1)

18.4.4 Oxidatively Modified Proteins by Aβ(1-42) In vitro,

580

(3)

18.4.5 Oxidatively Modified Proteins in Caenorhabditis elegans (C. elegans) Expressing Human Aβ(1-42),

583

(2)

18.5 Conclusion,

585

(20)

19 Oxidized Proteins in Cardiac Ischemia and Reperfusion

605

(1)

Jonathan P. Brennan and Philip Eaton

19.1 Introduction to Cardiac Ischemia and Reperfusion,

605

(11)

19.1.1 Definition and Consequences of Ischemia and Reperfusion,

605

(2)

19.1.2 Oxidative Stress and Injury during Ischemia and Reperfusion,

607

(5)

19.1.3 Consequences of Ischemia and Reperfusion in the Heart,

612

(4)

19.2 Oxidatively Modified Proteins in the Heart,

616

(8)

19.2.1 What Proteins Are Targeted by Oxidants and How Are They Modified?,

616

(8)

19.3 Established Targets of Post-translational Oxidation,

624

(4)

19.3.1 Metabolic Enzymes,

625

(1)

19.3.2 Structural and Myofibrillar Proteins,

626

(1)

19.3.3 Ion Channels,

626

(1)

19.3.4 Molecular Chaperones,

627

(1)

19.3.5 Signaling Molecules,

628

(1)

19.4 Oxidative Stress in Myocardial Adaptation to Ischemia and Reperfusion,

628

(3)

19.4.1 Free Radical Generation and Ischemic Preconditioning,

629

(2)

19.5 Conclusions, Therapeutic Implications, and Future Directions,

631

(20)

20 Proteome Analysis of Oxidative Stress: Glutathionyl Hemoglobin in Diabetic and Uremic Patients

651

(1)

Toshinlitsu Niwa

20.1 Introduction,

651

(2)

20.1.1 Oxidative Stress,

651

(1)

20.1.2 Glutathione,

652

(1)

20.1.3 Diabetes Mellitus and Oxidative Stress,

652

(1)

20.1.4 Uremia and Oxidative Stress,

652

(1)

20.1.5 Markers of Oxidative Stress,

653

(1)

20.2 Glutathionyl Hb as a Marker of Oxidative Stress,

653

(10)

20.2.1 Pretreatment of Blood Samples,

653

(1)

20.2.2 Liquid Chromatography–Electrospray Ionization–Mass Spectrometry (LC–ESI–MS),

654

(1)

20.2.3 Glutathionyl Hb in Diabetic Patients,

654

(1)

20.2.4 Glutathionyl Hb in Uremic Patients,

655

(1)

20.2.5 Glutathionyl Hb in Patients with Friedreich's Ataxia,

656

(2)

20.2.6 Oxygen Affinity of Glutathionyl Hb,

658

(1)

20.2.7 Formation of Glutathionyl Hb,

658

(4)

20.2.8 Matrix-Assisted Laser Desorption Ionization–Time-of-Flight Mass Spectrometry (MALDI–TOF–MS),

662

(1)

20.2.9 High-Performance Liquid Chromatography (HPLC) of Glutathionyl Hb,

662

(1)

20.3 Conclusion,

663

(6)

21 Glyco-oxidative Biochemistry in Diabetic Renal Injury

669

(1)

Toshio Miyata

21.1 Presence of Local, but not Generalized, Oxidative Stress in Diabetes,

669

(1)

21.2 Oxidative Protein Damage In vivo,

670

(1)

21.3 Antioxidative Properties of Medical Agents,

671

(1)

21.4 Therapeutic Perspectives for AGE Inhibitors,

672

(1)

21.4.1 Aminoguanidine and Other Hydrazine Derivatives,

672

(1)

21.4.2 Angiotensin II Receptor Blockers (ARB) and Angiotensin Converting Enzyme Inhibitors (ACEI),

673

(1)

21.5 AGE Inhibition and Renoprotection,

673

(3)

21.6 Future Prospects,

676

(5)

22 Quantitative Screening of Protein Glycation, Oxidation, and Nitration Adducts by LC-MS/MS: Protein Damage in Diabetes, Uremia, Cirrhosis, and Alzheimer's Disease

681

(1)

Paul J. Thornalley

22.1 Introduction: Derivatization Free Detection with Application to Modified Proteins and Amino Acids,

681

(8)

22.2 Physiological Sources of Glycated, Oxidized, and Nitrated Amino Acid Residues and Free Adducts,

689

(5)

22.3 Protein Glycation and Oxidation in Diabetes: Damage to Cellular and Extracellular Proteins,

694

(8)

22.3.1 Sources of Increased Protein Glycation, Oxidation, and Nitration in Diabetes,

694

(1)

22.3.2 Protein Glycation, Oxidation, and Nitration Adducts in Experimental Diabetes,

695

(1)

22.3.3 Protein Glycation Adducts as Markers of Glycemic Control in Clinical Diabetes,

696

(2)

22.3.4 Protein Glycation, Oxidation, and Nitration Adducts and Protein Damage in Clinical Diabetes,

698

(3)

22.3.5 Protein Damage in the Diabetic State and Future Therapeutics,

701

(1)

22.4 Profound Mishandling of Glycated, Oxidized, and Nitrated Amino Acids in Uremia,

702

(2)

22.5 Increased Glycated and Oxidized Amino Acids of Blood Plasma in Liver Cirrhosis—A Signature of Hepatic Oxidative Stress,

704

(3)

22.5.1 Cirrhosis,

704

(1)

22.5.2 Increased Protein Glycation, Oxidation, and Nitration Adduct Residues and Free Adducts of Plasma in Cirrhosis,

705

(1)

22.5.3 Countering Glycation in Cirrhosis,

705

(2)

22.6 Increased Methylglyoxal-Derived Hydroimidazolone and 3-Nitrotyrosine Free Adducts in Cerebrospinal Fluid of Subjects with Alzheimer's Disease—A Signature of Neuronal Damage,

707

(3)

22.6.1 Importance of the Early Diagnosis of Alzheimer's Disease,

710

(1)

22.7 Glycation Adducts in Food and Beverages,

710

(4)

22.8 Concluding Remarks: Physiological Formation and Proteolytic Processing of Glycated, Oxidized, and Nitrated Proteins in Disease Processes—The Importance of Measuring "Damage and Debris",

714

(15)

23 Protein Targets and Functional Consequences of Tyrosine Nitration in Vascular Disease

729

(1)

Laura M.S. Baker, Bruce A. Freeman, and Mutav Aslan

23.1 Association of Vascular Disease with Increased Production of Reactive Oxygen/Nitrogen Species and Accumulation of Nitrated Proteins,

729

(2)

23.2 Production of Reactive Oxygen and Nitrogen Species in the Vasculature,

731

(3)

23.2.1 Sources of Nitric Oxide,

732

(1)

23.2.2 Sources of Superoxide,

732

(2)

23.3 Tyrosine Nitration Mechanisms,

734

(8)

23.3.1 Nonenzymatic Nitrogen Dioxide Formation,

734

(5)

23.3.2 Enzymatic Formation of Nitrogen Dioxide by Heine Peroxidases,

739

(2)

23.3.3 Other Biologically Relevant Reactions of Nitric Oxide Leading to Nitrotyrosine Formation,

741

(1)

23.4 Methods for Detecting Nitrotyrosine,

742

(3)

23.5 Selectivity of Tyrosine Nitration,

745

(2)

23.6 Mechanistic Consequences of Nitrotyrosine Formation: Protein Nitration In vivo and Vascular Disease,

747

(17)

23.6.1 Actin Nitration in Sickle Cell Disease,

748

(1)

23.6.2 Inducible Nitric Oxide Synthase Nitration in Sepsis,

749

(2)

23.6.3 Myofibrillar Creatine Kinase Nitration in Heart Failure,

751

(2)

23.6.4 Prostacyclin Synthase Nitration in Atherosclerosis and Hyperglycemia,

753

(2)

23.6.5 Succinyl-CoA:3 Oxoacid CoA-Transferase Nitration in Diabetes,

755

(2)

23.6.6 Alpha-l-Protease Inhibitor and Ceruloplasmin Nitration in Acute Respiratory Distress Syndrome,

757

(1)

23.6.7 Fibrinogen Nitration in Coronary Artery Disease,

758

(2)

23.6.8 Apolipoprotein A-1 Nitration in Cardiovascular Disease,

760

(4)

23.6.9 MnSOD in Angiotensin II-Induced Hypertension,

764

(1)

23.7 Metabolism, Reversibility, and Stability of the Nitrated Tyrosine,

764

(3)

23.8 Tyrosine Nitration as a Cell Signaling Event,

767

(2)

23.9 Summary,

769

(18)

24 Oxidation of Artery Wall Proteins by Myeloperoxidase: A Proteomics Approach

787

(1)

Tomas Vaisar and Jay W. Heinecke

24.1 Oxidative Stress in Atherosclerosis,

787

(2)

24.2 Potential Role of Redox-Active Metal Ions and Glucose in Oxidative Stress,

789

(1)

24.2.1 Redox-Active Metal Ions,

789

(1)

24.2.2 Redox-Active Metal Ions plus Glucose,

790

(1)

24.3 Potential Role of Cellular Pathways in Oxidative Stress,

790

(3)

24.3.1 Reactive Nitrogen Species,

791

(1)

24.3.2 Myeloperoxidase,

791

(2)

24.4 Evidence for Oxidative Modification of LDL in the Human Artery Wall,

793

(3)

24.4.1 Redox-Active Metal Ions,

793

(1)

24.4.2 Glucose,

794

(1)

24.4.3 Reactive Nitrogen Species,

794

(1)

24.4.4 Myeloperoxidase,

795

(1)

24.5 Oxidative Modification of HDL,

796

(2)

24.5.1 Oxidized HDL in Humans,

796

(1)

24.5.2 Site-Specific Modification of ApoA-I,

797

(1)

24.6 Oxidative Regulation of Matrix Metalloproteinases,

798

(6)

24.6.1 Site-Specific Oxidative Activation of MMP-7,

800

(2)

24.6.2 Site-Specific Oxidative Inactivation of MMP-7,

802

(2)

24.7 Conclusions,

804

(9)

25 Oxidative Stress and Protein Oxidation in Pre-Eclampsia

813

(1)

Maarten T.M. Raijmakers, Wilbert H.M. Peters, Christianne J. de Groot, and Eric A.P. Steegers

25.1 Introduction,

813

(1)

25.2 Oxidative Stress and Pre-Eclampsia,

814

(6)

25.2.1 Sources of Oxidative Stress during Pregnancy,

814

(2)

25.2.2 Evidence of Placental Oxidative Stress in Pre-Eclampsia,

816

(1)

25.2.3 Evidence of Maternal Oxidative Stress in Pre-Eclampsia,

816

(4)

25.3 Proteomics,

820

(11)

26 Involvement of Oxidants in the Etiology of Chronic Airway Diseases: Proteomic Approaches to Identify Redox Processes in Epithelial Cell Signaling and Inflammation

831

(1)

Albert ran der Vliet, Niki L. Revnaert, Peter F. Bove, Karina Ckless, Anne-Katrin Great, Milena Hristora, and Yvonne M. Janssen-Heininger

26.1 Introduction,

831

(1)

26.2 Chronic Airway Inflammation: Conditions Associated with Oxidative and Nitrosative Stress,

832

(4)

26.2.1 Asthma as a Paradigm for Chronic Airway Inflammation.

832

(1)

26.2.2 Inflammatory Oxidants: NADPH Oxidases and Peroxidases,

833

(1)

26.2.3 Nitric Oxide and Its Metabolism,

834

(1)

26.2.4 Alterations in Antioxidant Defenses,

834

(2)

26.3 Biological Significance of Protein Oxidation,

836

(11)

26.3.1 Protein Oxidation: Biomarker of Disease or Mediator of Inflammation and Injury?,

836

(4)

26.3.2 Redox Signaling: Cysteine Oxidation, Thiolation, and Nitrosylation,

840

(3)

26.3.3 Redox Regulation of Inflammation: A Central Role for NF-KB,

843

(4)

26.4 Proteomic Approaches to Study Protein Oxidation in Airway Disease,

847

(10)

26.4.1 General Concepts and Current Applications,

847

(2)

26.4.2 Redox Proteomics: Definitions and Approaches,

849

(3)

26.4.3 Analysis of Protein S-Nitrosylation: Direct and Indirect Approaches,

852

(4)

26.4.4 Visualization of Cysteine Oxidation and Nitrosylation in Intact Cells and Tissues,

856

(1)

26.5 Tissue Proteomics and Application to Study Protein Oxidation,

857

(4)

26.5.1 Approaches to Tissue Proteomics,

857

(1)

26.5.2 Approaches to Collect Airway Epithelial Proteins for Proteomic Analysis,

858

(3)

26.6 Summary and Conclusions,

861

(16)

27 Sequestering Agents of Intermediate Reactive Aldehydes as Inhibitors of Advanced Lipoxidation End-Products (ALEs)

877

(1)

Marina Carini, Giancarlo Aldini, and Roberto Maffei Facino

27.1 Introduction,

877

(3)

27.2 Lipoxidation-Derived Reactive Aldehydes,

880

(13)

27.2.1 Mechanisms of Formation, Biological Effects, and Protein Adduction,

880

(8)

27.2.2 Protein-Aldehyde Adducts: Occurrence and Detection in Biological Matrices,

888

(5)

27.3 Intervention against Lipoxidation-Derived Carbonyl Stress: ALE Inhibitors,

893

(20)

27.3.1 Advanced Lipoxidation End-Products (ALEs),

893

(1)

27.3.2 Aldehyde-Sequestering Agents,

894

(19)

27.4 Conclusions and Future Perspective,

913

(18)

Index

931

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Redox Proteomics From Protein Modifications to Cellular Dysfunction and Diseases

Summary

Author Biography

Table of Contents

Supplemental Materials

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Redox Proteomics From Protein Modifications to Cellular Dysfunction and Diseases

Summary

Author Biography

Table of Contents

Supplemental Materials

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