Nitric Oxide, Part F

Name: Nitric Oxide, Part F
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Academic Press

Published on 2. September 2011

512 pages

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978-0-08-087761-7 (ISBN)

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Cover
Contents
Contributors
Volumes in Series
Section 1: Molecular Methods
Chapter 1: Mass Spectrometric Characterization of Proteins Modified by Nitric Oxide-Derived Species
Abstract
1. Introduction
2. Reagents
3. Preparation of Nitrated BSA
4. In-Gel Protein Digestion and Mass Spectrometric Analysis
5. Data Analysis
6. MALDI-TOF Peptide Mass Fingerprinting
7. LC-ESI-IT Fragment Fingerprinting upon Collisional Fragmentation
8. Concluding Remarks
Acknowledgments
References
Chapter 2: Detecting Nitrated Proteins by Proteomic Technologies
Abstract
1. Introduction
2. Methods
3. Conclusions
Acknowledgments
References
Chapter 3: Using Tandem Mass Spectrometry to Quantify Site-Specific Chlorination and Nitration of Proteins: Model System Studies with High-Density Lipoprotein Oxidized by Myeloperoxidase
Abstract
1. Introduction
2. High-Density Lipoprotein Biology
3. Advantages of HDL as a Model System
4. Advantages of LC-ESI-MS/MS When Analyzing Posttranslational Modifications of Proteins
5. Isolating HDL, ApoA-I, and MPO
6. Oxidative Reactions
7. Proteolytic Digestion of Proteins
8. Liquid Chromatography-Electrospray Ionization Mass Spectrometry (LC-ESI-MS and MS/MS)
9. A Combination of Tryptic and Glu-C Digests Provides Complete Sequence Coverage of ApoA-I
10. HOCl or MPO Preferentially Chlorinates Tyrosine 192 in Lipid-Free ApoA-I
11. Reagent ONOO-and MPO Nitrate All the Tyrosine Residues in Lipid-Free ApoA-I, but Tyrosine 192 Is the Main Target
12. HOCl Quantitatively Converts All Three Methionine Residues in ApoA-I to Methionine Sulfoxide
13. HOCl Generates Hydroxytryptophan and Dihydroxytryptophan Residues in ApoA-I
14. Reactive Nitrogen Species Generates Nitrotryptophan Residues in Lipid-Free ApoA-I
15. The YXXK Motif Directs ApoA-I Chlorination
16. Quantitative Analysis of Posttranslational Modifications of Proteins
17. ApoA-I Oxidation Impairs Cholesterol Transport by the ABCA1 System
18. Conclusions
Acknowledgments
References
Chapter 4: Influence of Intramolecular Electron Transfer Mechanism in Biological Nitration, Nitrosation, and Oxidation of Redox-Sensitive Amino Acids
Abstract
1. Introduction
2. Methods
3. Results
Acknowledgments
References
Chapter 5: Protein Thiol Modification by Peroxynitrite Anion and Nitric Oxide Donors
Abstract
1. Introduction
2. Protein Cysteine Oxidation by ONOO-
3. Methodology to Detect Protein Thiol Modification
4. Iodoacetamide Labeling of Proteins after Oxidant Treatment
5. HPLC Separation of Fluorescein-Labeled Peptides
6. Detection of Interchain Disulfides by Western Blot
7. Repair of Protein Disulfides by Thioredoxin Reductase and Glutaredoxin Systems
8. Thioredoxin Reductase Repair of Protein Disulfides
9. Quantitation of Protein Disulfides by Measuring NADPH Oxidation
10. Quantitation of Total Cysteine Oxidation Using DTNB
11. Glutaredoxin/Glutathione (GSH) Reductase Repair of Protein Disulfides
12. Detection of Protein S-Glutathionylation
13. Thiol/disulfide Exchange with Oxidized Glutathione
14. Protein Thiol Modification by Nitric Oxide Donors
15. Conclusions
References
Chapter 6: Indirect Mechanisms of DNA Strand Scission by Peroxynitrite
Abstract
1. Introduction
2. Materials and Methods
3. Results and Discussion
Acknowledgments
References
Chapter 7: Nitric Oxide: Interaction with the Ammonia Monooxygenase and Regulation of Metabolic Activities in Ammonia Oxidizers
Abstract
1. Ammonia-Oxidizing Bacteria
2. Aerobic Ammonia Oxidation
3. Anaerobic Ammonia Oxidation with Nitrogen Dioxide as Oxidant Releases NO as Product
4. Aerobic Ammonia Oxidation with Nitrogen Dioxide as Oxidant
5. Regulation of Metabolic Activities in Ammonia Oxidizers
6. Nitric Oxide Induces Denitrification in N. europaea
7. Nitric Oxide Induces the Biofilm Formation of N. europaea
8. Nitric Oxide Is Required in N. europaea to Restore Ammonia Oxidation after Chemoorganotrophic Denitrification
References
Chapter 8: Chemiluminescent Detection of S-Nitrosated Proteins: Comparison of Tri-iodide, Copper/CO/Cysteine, and Modified Copper/Cysteine Methods
Abstract
1. Introduction
2. Methods for Detection of S-Nitrosothiols
3. Chemiluminescent-Based Detection of S-Nitrosothiols
4. Advantages and Disadvantages
5. Comparisons and Validations
6. Conclusions
References
Chapter 9: S-Nitrosothiol Assays That Avoid the Use of Iodine
Abstract
1. Introduction
2. S-Nitrosothiol Synthesis
3. S-Nitrosothiol Assays
4. S-Nitrosothiols in Health and Disease: The Importance of Getting the Assay Right
5. Summary
References
Chapter 10: Analysis of Citrulline, Arginine, and Methylarginines Using High-Performance Liquid Chromatography
Abstract
1. Introduction
2. The HPLC Apparatus
3. Chemicals and Materials
4. General Precautions in Sample Preparation and HPLC Analysis
5. Analysis of Citrulline and Arginine in Physiological Samples
6. Analysis of Methylarginines in Physiological Samples
7. Conclusion
Acknowledgments
References
Chapter 11: Quantitative Proteome Mapping of Nitrotyrosines
Abstract
1. Introduction
2. Multidimensional LC-MS/MS Provides Large Data Sets for Identification of Nitrotyrosine-Modified Proteins
3. Retention of Complexity in Samples Prepared from Global Proteomic Analysis
4. Confident Identification of Nitrotyrosine-Containing Peptides
5. Comparative Quantitation of Nitrotyrosine-Modified Peptide/Proteins
6. Summary
References
Section 2: Cellular Methods
Chapter 12: Protein S-Nitrosation in Signal Transduction: Assays for Specific Qualitative and Quantitative Analysis
Abstract
1. Introduction
2. Examples Demonstrating the Contribution of Protein S-Nitrosation to Intracellular Signal Transduction
3. Assays for Analysis of S-Nitrosation of Specific Cellular Proteins
4. Conclusions
Acknowledgments
References
Chapter 13: Determination of Mammalian Arginase Activity
Abstract
1. Introduction
2. Principle of Assay
3. Preparation of Cell and Tissue Extracts
4. Buffers, Reagents and Other Materials for Assay Protocol I
5. Assay Protocol I
6. Buffers, Reagents, and Other Materials for Assay Protocol II
7. Assay Protocol II
8. Limitations of Assay
9. Determination of Arginase Activity in Cultured Cells
Acknowledgments
References
Chapter 14: Measurement of Protein S-Nitrosylation during Cell Signaling
Abstract
1. Introduction
2. Biotin Switch Technique
3. Protocol for Analyzing Protein S-Nitrosylation in Tissue Samples Using the Biotin Switch Assay
4. Chemical Reduction/Chemiluminescence
5. Protocol for Chemical Reduction/Chemiluminescence Measurements of S-Nitrosylation of Immunoprecipitated Proteins
6. Conclusion
References
Chapter 15: Pivotal Role of Arachidonic Acid in the Regulation of Neuronal Nitric Oxide Synthase Activity and Inducible Nitric Oxide Synthase Expression in Activated Astrocytes
Abstract
1. Introduction
2. Materials and Methods
3. Results and Discussion
Acknowledgments
References
Chapter 16: Red Blood Cells as a Model to Differentiate between Direct and Indirect Oxidation Pathways of Peroxynitrite
Abstract
1. Introduction
2. Direct Reactions of Peroxynitrite with Biological Targets
3. Peroxynitrite Homolysis: Indirect Radical Chemistry
4. Red Blood Cells as an Experimental Model to Test the Fate of Peroxynitrite in a Biological Environment
5. Red Blood Cell Modifications Induced by Extracellular Peroxynitrite Decay
6. Red Blood Cell Modifications Induced by Intracellular Peroxynitrite Decay
7. Peroxynitrite-Dependent Phosphorylation Signaling of RBC
8. Peroxynitrite-Induced Biomarkers of RBC Senescence
9. Peroxynitrite-Induced Biomarkers of RBC Apoptosis
10. Methods
11. Data and Statistics
Acknowledgments
References
Chapter 17: Detection and Proteomic Identification of S-Nitrosated Proteins in Human Hepatocytes
Abstract
1. Introduction
2. Preparation of CSNO
3. Preparation of Primary Human Hepatocytes and Cell Culture
4. Treatment of Hepatocytes and Sample Preparation
5. Biotin Switch Assay
6. Detection and Purification of Biotinylated Proteins
7. Final Considerations
Acknowledgments
References
Chapter 18: Identification of S-Nitrosylated Proteins in Plants
Abstract
1. Introduction
2. Generation of Protein Nitrosothiols
3. Blocking Reaction of Free Thiols
4. Reduction of Nitrosothiols and S-Biotinylation
5. Affinity Purification of Biotinylated Proteins by NeutrAvidin
6. Modified Techniques Related to the Biotin Switch Assay
References
Chapter 19: Identification of 3-Nitrotyosine-Modified Brain Proteins by Redox Proteomics
Abstract
1. Introduction
2. Materials
3. Method
4. Comments
Acknowledgments
References
Chapter 20: Slot-Blot Analysis of 3-Nitrotyrosine-Modified Brain Proteins
Abstract
1. Introduction
2. Materials
3. Solutions
4. Sample Preparation for 3-NT Determination
5. Comments
Acknowledgments
References
Chapter 21: Detection Assays for Determination of Mitochondrial Nitric Oxide Synthase Activity
Advantages and Limitations
Abstract
1. Introduction
2. Colorimetric Nitric Oxide Synthase Assay
3. Determination of Mitochondrial Nitric Oxide Synthase Activity Using Radioassay
4. Spectrophotometric Determination of Mitochondrial Nitric Oxide Synthase Activity
5. Polarographic Nitric Oxide Synthase Assays
6. Chemiluminescence Assay
7. Fluorescent-Based Nitric Oxide Detection Assays
8. Conclusion
References
Section 3: Organism Methods
Chapter 22: Assay of 3-Nitrotyrosine in Tissues and Body Fluids by Liquid Chromatography with Tandem Mass Spectrometric Detection
Abstract
1. 3-Nitrotyrosine (3-NT) in Physiological Systems
2. Measurement of 3-NT
3. Liquid Chromatography with Tandem Mass Spectrometric Detection (LC-MS/MS) Assay of 3-NT Residues and 3-NT-Free Adducts: Thornalley Group Method
4. Estimates of 3-NT Residues and Free 3-NT in Plasma and Red Blood Cells under Basal Conditions and Effect of Disease
5. 3-Nitrotyrosine Residues in Lipoproteins
6. 3-Nitrotyrosine Residues and Free Adduct in Cerebrospinal Fluid
7. 3-Nitrotyrosine Residue Content of Tissues
8. Concluding Remarks
Acknowledgments
References
Chapter 23: Nitrite and Nitrate Measurement by Griess Reagent in Human Plasma: Evaluation of Interferences and Standardization
Abstract
1. Introduction
2. Experimental Procedures
3. Results
4. Discussion
Acknowledgments
References
Chapter 24: Detection of Nitric Oxide and Its Derivatives in Human Mixed Saliva and Acidified Saliva
Abstract
1. Introduction
2. Formation of Reactive Nitrogen Oxide Species (RNOS) in Mixed Whole Saliva and the Bacterial Fraction
3. Detection of RNOS in Mixed Whole Saliva and the Bacterial Fraction
4. Formation of RNOS in Acidified Saliva
5. Detection of RNOS in Acidified Saliva
6. Concluding Remarks
References
Chapter 25: Imaging of Reactive Oxygen Species and Nitric Oxide In Vivo in Plant Tissues
Abstract
1. Introduction
2. Imaging Reactive Oxygen Species and Nitric Oxide In Vivo by Confocal Laser Microscopy
3. Plant Tissue Preparation and Procedure
4. Conclusions
Acknowledgments
References
Chapter 26: Examining Nitroxyl in Biological Systems
Abstract
1. Introduction
2. Nitroxyl Donors
3. Biological HNO Chemistry
4. Use of HNO Donors in Biological Studies
5. Nitroxyl Pharmacological Effects: In Vivo and In Vitro Studies
6. Summary
References
Author Index
Subject Index

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Nitric Oxide, Part F

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