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.
Зміст
1. Oxidatively Modified Proteins and Proteomic Technologies.
1.1 Chemical Modification of Proteins by Reactive Oxygen Species
(E. Stadtman & R. Levine).
1.2 The Chemistry of Protein Modifications Elicited By Nitric
Oxide and Related Nitrogen Oxides (D. Thomas, et al.).
1.3 Mass Spectrometry Approaches for the Molecular
Characterization of Oxidatively/Nitrosatively Modified Proteins (A.
Scaloni).
1.4 Thiol-disulfide Oxidoreduction of Protein Cysteines: Old
Methods Revisted for Proteomics (V. Bonetto & P. Ghezzi).
1.5 Carbonylated Proteins and their Implication in Physiology
and Pathology (R. Levine & E. Stadtman).
1.6 S-Nitrosation of Cysteine thiols as a Redox Signal
(Y. Zhang & N. Hogg).
1.7 Detection of Glycated and Glyco Oxidated Proteins (A.
Lapolla, et al.).
1.8 Mud PIT (Multidimensaional Protein Identification Technology)
for Identification of Post-translational Protein Modifications in
Complex Biological Mixtures (S. Thomas, et al.).
1.9 Use of a Proteomic Technique to Identify Oxidant-Sensitive
Thiol Proteins in Cultured Cells (M. Hampton, et al.).
1.10 ICAT (Isotope-Code Affinity Tag) Approach to Redox
Proteomics: Identification and Quantification of Oxidant-Sensitive
Protein Thiols (M. Sethuraman, et al.).
1.11 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 (D.
Tsikas).
2. Cellular Aspects of Protein Oxidation.
2.1 The Covalent Advantage: A New Paradigm for Cell Signaling
Mediated by Thiol Reactive Lipid Oxidation Products (D. Dickinson,
et al.).
2.2 Early Molecular Events During Response to Oxidative Stress
in Human Cells by Differential Proteomics (G. Tell).
2.3 Oxidative Damage to Proteins: Structural Modifications and
Consequences in Cell Function (E. Cabiscol & J. Ros).
2.4 Oxidative Damage and Cellular Senescence: Lessons from
Bacteria and Yeast (T. Nyström).
3. Redox Proteomic Analysis in Human Diseases.
3.1 Proteins as Sensitive Biomarkers of Human Conditions
Associated with Oxidative Stress (I. Dalle-Donne, et al.).
3.2 Degradation and Accumulation of Oxidized Proteins in
Age-Related Diseases (P. Voss & T. Grune).
3.3 Redox Proteomics: A New Approach to Investgate Oxidative
Stress in Alzheimer’s Diseases (D. Butterfield, et al.).
3.4 Oxidized Proteins in Cardiac Ischemia-Reperfusion (J.
Brennan & P. Eaton).
3.5 Proteome Anaylsis of Oxidative Stress: Glutathionyl
Hemoglobin in Diabetic and Uremic Patients (T. Niwa).
3.6 Glyco-Oxidative Biochemistry in Diabetic Renal Injury (T.
Miyata).
3.7 Quantitative Screnning of Protein Glycation, Oxidation, and
Nitration Adducts by LC-MS/MS: Protein Damage in Diabetes, Uremia,
Cirrhosis, and Alzheimer’s Disease (P. Thornalley).
3.8 Protein Targets and Functional Consequences of Tyrosine
Nitration in Vascular Disease (L. Baker, et al.).
3.9 Oxidation of Artery Wall Proteins by Myeloperoxidase: A
proteomics Approach (T. Vaisar & J. Heinecke).
3.10 Oxidative Stress and Protein Oxidation in Pre-Eclampsia (M.
Raijmakers, et al.).
3.11 The Involvement of Oxidants in the Etiology of Chronic
Airway Diseases: Proteomic Approaches to Identify Redox Processes
in Epithelial Cell Signal and Inflammation (A. van der Vliet, et
al.).
3.12 Sequestering Agents of Intermediate Reactive Aldehydes as
Inhibitors of Advanced Lipoxidation End-Products (ALEs) (M. Carini,
et al.).
Про автора
ISABELLA DALLE-DONNE, PHD, is Assistant Professor in the
Department of Biology at the University of Milan, Italy. She has a
Ph D in cellular and molecular biology from the University of Milan.
ANDREA SCALONI, PHD, is First Investigator at the
Proteomics & Mass Spectrometry Laboratory, ISPAAM, National
Research Council in Naples, Italy. He received his Ph D in chemical
sciences from the University of Rome ‘La Sapienza’ in Italy.
D. ALLAN BUTTERFIELD, PHD, is Alumni Professor of
Chemistry and Director of the University of Kentucky Center of
Membrane Sciences in Lexington, Kentucky, USA. He received his Ph D
in physical chemistry from Duke University.