Elsevier S & T

Nitric Oxide, Part F

Cadenas, Enrique

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Table of contents
  • Contentsv
  • Contributorsxv
  • Volumes in Seriesxxi
  • Section 1: Molecular Methods1
  • Chapter 1: Mass Spectrometric Characterization of Proteins Modified by Nitric Oxide-Derived Species3
  • Abstract3
  • 1. Introduction4
  • 2. Reagents6
  • 3. Preparation of Nitrated BSA6
  • 4. In-Gel Protein Digestion and Mass Spectrometric Analysis6
  • 5. Data Analysis7
  • 6. MALDI-TOF Peptide Mass Fingerprinting8
  • 7. LC-ESI-IT Fragment Fingerprinting upon Collisional Fragmentation9
  • 8. Concluding Remarks9
  • Acknowledgments12
  • References12
  • Chapter 2: Detecting Nitrated Proteins by Proteomic Technologies17
  • Abstract17
  • 1. Introduction18
  • 2. Methods20
  • 3. Conclusions30
  • Acknowledgments30
  • References30
  • Chapter 3: Using Tandem Mass Spectrometry to Quantify Site-Specific Chlorination and Nitration of Pr33
  • Abstract34
  • 1. Introduction34
  • 2. High-Density Lipoprotein Biology36
  • 3. Advantages of HDL as a Model System36
  • 4. Advantages of LC-ESI-MS/MS When Analyzing Posttranslational Modifications of Proteins37
  • 5. Isolating HDL, ApoA-I, and MPO38
  • 6. Oxidative Reactions38
  • 7. Proteolytic Digestion of Proteins39
  • 8. Liquid Chromatography-Electrospray Ionization Mass Spectrometry (LC-ESI-MS and MS/MS)39
  • 9. A Combination of Tryptic and Glu-C Digests Provides Complete Sequence Coverage of ApoA-I40
  • 10. HOCl or MPO Preferentially Chlorinates Tyrosine 192 in Lipid-Free ApoA-I40
  • 11. Reagent ONOO-and MPO Nitrate All the Tyrosine Residues in Lipid-Free ApoA-I, but Tyrosine 192 Is44
  • 12. HOCl Quantitatively Converts All Three Methionine Residues in ApoA-I to Methionine Sulfoxide48
  • 13. HOCl Generates Hydroxytryptophan and Dihydroxytryptophan Residues in ApoA-I53
  • 14. Reactive Nitrogen Species Generates Nitrotryptophan Residues in Lipid-Free ApoA-I57
  • 15. The YXXK Motif Directs ApoA-I Chlorination57
  • 16. Quantitative Analysis of Posttranslational Modifications of Proteins58
  • 17. ApoA-I Oxidation Impairs Cholesterol Transport by the ABCA1 System58
  • 18. Conclusions59
  • Acknowledgments60
  • References60
  • Chapter 4: Influence of Intramolecular Electron Transfer Mechanism in Biological Nitration, Nitrosat65
  • Abstract66
  • 1. Introduction66
  • 2. Methods67
  • 3. Results70
  • Acknowledgments90
  • References90
  • Chapter 5: Protein Thiol Modification by Peroxynitrite Anion and Nitric Oxide Donors95
  • Abstract95
  • 1. Introduction96
  • 2. Protein Cysteine Oxidation by ONOO-97
  • 3. Methodology to Detect Protein Thiol Modification97
  • 4. Iodoacetamide Labeling of Proteins after Oxidant Treatment98
  • 5. HPLC Separation of Fluorescein-Labeled Peptides99
  • 6. Detection of Interchain Disulfides by Western Blot100
  • 7. Repair of Protein Disulfides by Thioredoxin Reductase and Glutaredoxin Systems101
  • 8. Thioredoxin Reductase Repair of Protein Disulfides102
  • 9. Quantitation of Protein Disulfides by Measuring NADPH Oxidation103
  • 10. Quantitation of Total Cysteine Oxidation Using DTNB103
  • 11. Glutaredoxin/Glutathione (GSH) Reductase Repair of Protein Disulfides104
  • 12. Detection of Protein S-Glutathionylation105
  • 13. Thiol/disulfide Exchange with Oxidized Glutathione105
  • 14. Protein Thiol Modification by Nitric Oxide Donors106
  • 15. Conclusions108
  • References108
  • Chapter 6: Indirect Mechanisms of DNA Strand Scission by Peroxynitrite111
  • Abstract111
  • 1. Introduction112
  • 2. Materials and Methods112
  • 3. Results and Discussion116
  • Acknowledgments119
  • References119
  • Chapter 7: Nitric Oxide: Interaction with the Ammonia Monooxygenase and Regulation of Metabolic Acti121
  • Abstract121
  • 1. Ammonia-Oxidizing Bacteria122
  • 2. Aerobic Ammonia Oxidation122
  • 3. Anaerobic Ammonia Oxidation with Nitrogen Dioxide as Oxidant Releases NO as Product123
  • 4. Aerobic Ammonia Oxidation with Nitrogen Dioxide as Oxidant125
  • 5. Regulation of Metabolic Activities in Ammonia Oxidizers127
  • 6. Nitric Oxide Induces Denitrification in N. europaea128
  • 7. Nitric Oxide Induces the Biofilm Formation of N. europaea129
  • 8. Nitric Oxide Is Required in N. europaea to Restore Ammonia Oxidation after Chemoorganotrophic Den132
  • References133
  • Chapter 8: Chemiluminescent Detection of S-Nitrosated Proteins: Comparison of Tri-iodide, Copper/CO/137
  • Abstract137
  • 1. Introduction138
  • 2. Methods for Detection of S-Nitrosothiols139
  • 3. Chemiluminescent-Based Detection of S-Nitrosothiols140
  • 4. Advantages and Disadvantages146
  • 5. Comparisons and Validations147
  • 6. Conclusions151
  • References153
  • Chapter 9: S-Nitrosothiol Assays That Avoid the Use of Iodine157
  • Abstract157
  • 1. Introduction158
  • 2. S-Nitrosothiol Synthesis158
  • 3. S-Nitrosothiol Assays160
  • 4. S-Nitrosothiols in Health and Disease: The Importance of Getting the Assay Right171
  • 5. Summary171
  • References171
  • Chapter 10: Analysis of Citrulline, Arginine, and Methylarginines Using High-Performance Liquid Chro177
  • Abstract177
  • 1. Introduction178
  • 2. The HPLC Apparatus179
  • 3. Chemicals and Materials179
  • 4. General Precautions in Sample Preparation and HPLC Analysis180
  • 5. Analysis of Citrulline and Arginine in Physiological Samples181
  • 6. Analysis of Methylarginines in Physiological Samples185
  • 7. Conclusion188
  • Acknowledgments188
  • References188
  • Chapter 11: Quantitative Proteome Mapping of Nitrotyrosines191
  • Abstract191
  • 1. Introduction192
  • 2. Multidimensional LC-MS/MS Provides Large Data Sets for Identification of Nitrotyrosine-Modified P193
  • 3. Retention of Complexity in Samples Prepared from Global Proteomic Analysis195
  • 4. Confident Identification of Nitrotyrosine-Containing Peptides197
  • 5. Comparative Quantitation of Nitrotyrosine-Modified Peptide/Proteins198
  • 6. Summary203
  • References203
  • Section 2: Cellular Methods207
  • Chapter 12: Protein S-Nitrosation in Signal Transduction: Assays for Specific Qualitative and Quanti209
  • Abstract209
  • 1. Introduction210
  • 2. Examples Demonstrating the Contribution of Protein S-Nitrosation to Intracellular Signal Transduc210
  • 3. Assays for Analysis of S-Nitrosation of Specific Cellular Proteins214
  • 4. Conclusions217
  • Acknowledgments218
  • References218
  • Chapter 13: Determination of Mammalian Arginase Activity221
  • Abstract221
  • 1. Introduction222
  • 2. Principle of Assay222
  • 3. Preparation of Cell and Tissue Extracts223
  • 4. Buffers, Reagents and Other Materials for Assay Protocol I224
  • 5. Assay Protocol I225
  • 6. Buffers, Reagents, and Other Materials for Assay Protocol II226
  • 7. Assay Protocol II226
  • 8. Limitations of Assay227
  • 9. Determination of Arginase Activity in Cultured Cells228
  • Acknowledgments229
  • References229
  • Chapter 14: Measurement of Protein S-Nitrosylation during Cell Signaling231
  • Abstract231
  • 1. Introduction232
  • 2. Biotin Switch Technique233
  • 3. Protocol for Analyzing Protein S-Nitrosylation in Tissue Samples Using the Biotin Switch Assay235
  • 4. Chemical Reduction/Chemiluminescence236
  • 5. Protocol for Chemical Reduction/Chemiluminescence Measurements of S-Nitrosylation of Immunoprecip238
  • 6. Conclusion240
  • References240
  • Chapter 15: Pivotal Role of Arachidonic Acid in the Regulation of Neuronal Nitric Oxide Synthase Act243
  • Abstract243
  • 1. Introduction244
  • 2. Materials and Methods245
  • 3. Results and Discussion246
  • Acknowledgments250
  • References250
  • Chapter 16: Red Blood Cells as a Model to Differentiate between Direct and Indirect Oxidation Pathwa253
  • Abstract254
  • 1. Introduction254
  • 2. Direct Reactions of Peroxynitrite with Biological Targets255
  • 3. Peroxynitrite Homolysis: Indirect Radical Chemistry256
  • 4. Red Blood Cells as an Experimental Model to Test the Fate of Peroxynitrite in a Biological Enviro257
  • 5. Red Blood Cell Modifications Induced by Extracellular Peroxynitrite Decay260
  • 6. Red Blood Cell Modifications Induced by Intracellular Peroxynitrite Decay260
  • 7. Peroxynitrite-Dependent Phosphorylation Signaling of RBC261
  • 8. Peroxynitrite-Induced Biomarkers of RBC Senescence262
  • 9. Peroxynitrite-Induced Biomarkers of RBC Apoptosis264
  • 10. Methods265
  • 11. Data and Statistics268
  • Acknowledgments269
  • References269
  • Chapter 17: Detection and Proteomic Identification of S-Nitrosated Proteins in Human Hepatocytes273
  • Abstract273
  • 1. Introduction274
  • 2. Preparation of CSNO276
  • 3. Preparation of Primary Human Hepatocytes and Cell Culture276
  • 4. Treatment of Hepatocytes and Sample Preparation277
  • 5. Biotin Switch Assay277
  • 6. Detection and Purification of Biotinylated Proteins278
  • 7. Final Considerations279
  • Acknowledgments280
  • References280
  • Chapter 18: Identification of S-Nitrosylated Proteins in Plants283
  • Abstract283
  • 1. Introduction283
  • 2. Generation of Protein Nitrosothiols285
  • 3. Blocking Reaction of Free Thiols287
  • 4. Reduction of Nitrosothiols and S-Biotinylation288
  • 5. Affinity Purification of Biotinylated Proteins by NeutrAvidin289
  • 6. Modified Techniques Related to the Biotin Switch Assay290
  • References291
  • Chapter 19: Identification of 3-Nitrotyosine-Modified Brain Proteins by Redox Proteomics295
  • Abstract296
  • 1. Introduction296
  • 2. Materials297
  • 3. Method298
  • 4. Comments305
  • Acknowledgments305
  • References305
  • Chapter 20: Slot-Blot Analysis of 3-Nitrotyrosine-Modified Brain Proteins309
  • Abstract309
  • 1. Introduction309
  • 2. Materials311
  • 3. Solutions312
  • 4. Sample Preparation for 3-NT Determination312
  • 5. Comments313
  • Acknowledgments314
  • References314
  • Chapter 21: Detection Assays for Determination of Mitochondrial Nitric Oxide Synthase Activity; Adva317
  • Abstract317
  • 1. Introduction318
  • 2. Colorimetric Nitric Oxide Synthase Assay319
  • 3. Determination of Mitochondrial Nitric Oxide Synthase Activity Using Radioassay320
  • 4. Spectrophotometric Determination of Mitochondrial Nitric Oxide Synthase Activity322
  • 5. Polarographic Nitric Oxide Synthase Assays322
  • 6. Chemiluminescence Assay323
  • 7. Fluorescent-Based Nitric Oxide Detection Assays326
  • 8. Conclusion331
  • References332
  • Section 3: Organism Methods335
  • Chapter 22: Assay of 3-Nitrotyrosine in Tissues and Body Fluids by Liquid Chromatography with Tandem337
  • Abstract337
  • 1. 3-Nitrotyrosine (3-NT) in Physiological Systems338
  • 2. Measurement of 3-NT339
  • 3. Liquid Chromatography with Tandem Mass Spectrometric Detection (LC-MS/MS) Assay of 3-NT Residues340
  • 4. Estimates of 3-NT Residues and Free 3-NT in Plasma and Red Blood Cells under Basal Conditions and342
  • 5. 3-Nitrotyrosine Residues in Lipoproteins351
  • 6. 3-Nitrotyrosine Residues and Free Adduct in Cerebrospinal Fluid353
  • 7. 3-Nitrotyrosine Residue Content of Tissues353
  • 8. Concluding Remarks354
  • Acknowledgments355
  • References355
  • Chapter 23: Nitrite and Nitrate Measurement by Griess Reagent in Human Plasma: Evaluation of Interfe361
  • Abstract361
  • 1. Introduction362
  • 2. Experimental Procedures364
  • 3. Results366
  • 4. Discussion373
  • Acknowledgments378
  • References378
  • Chapter 24: Detection of Nitric Oxide and Its Derivatives in Human Mixed Saliva and Acidified Saliva381
  • Abstract381
  • 1. Introduction382
  • 2. Formation of Reactive Nitrogen Oxide Species (RNOS) in Mixed Whole Saliva and the Bacterial Fract382
  • 3. Detection of RNOS in Mixed Whole Saliva and the Bacterial Fraction384
  • 4. Formation of RNOS in Acidified Saliva390
  • 5. Detection of RNOS in Acidified Saliva392
  • 6. Concluding Remarks393
  • References394
  • Chapter 25: Imaging of Reactive Oxygen Species and Nitric Oxide In Vivo in Plant Tissues397
  • Abstract397
  • 1. Introduction398
  • 2. Imaging Reactive Oxygen Species and Nitric Oxide In Vivo by Confocal Laser Microscopy399
  • 3. Plant Tissue Preparation and Procedure402
  • 4. Conclusions406
  • Acknowledgments406
  • References406
  • Chapter 26: Examining Nitroxyl in Biological Systems411
  • Abstract412
  • 1. Introduction412
  • 2. Nitroxyl Donors412
  • 3. Biological HNO Chemistry419
  • 4. Use of HNO Donors in Biological Studies423
  • 5. Nitroxyl Pharmacological Effects: In Vivo and In Vitro Studies424
  • 6. Summary426
  • References427
  • Author Index433
  • Subject Index459
Book details
  • Vendor Elsevier S & T
  • SKU 9780123739674
  • ISBN-13 9780080877617
  • Author Cadenas, Enrique
  • Category Science
  • Subject Microbiology

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The discovery that nitrogen monoxide or nitric oxide (NO)is a biologically produced free radical has revolutionized our thinking about physiological and pathological processes. This discovery has ignited enormous interest in the scientific community. When generated at low levels, NO is a signaling molecule, but at high concentration, NO is a cytotoxic molecule. The physiological and pathological processes of NO production and metabolism and its targets, currently areas of intensive research, have important pharmacologic implications for health and disease.