Dalle-Donne / Scaloni / Butterfield Redox Proteomics

From Protein Modifications to Cellular Dysfunction and Diseases
1. Auflage 2006
ISBN: 978-0-471-97311-9
Verlag: John Wiley & Sons
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 960 Seiten, E-Book

Reihe: Wiley-Interscience Series on Mass Spectrometry

Methodology and applications of redox proteomics
The relatively new and rapidly changing field of redox proteomicshas the potential to revolutionize how we diagnose disease, assessrisks, determine prognoses, and target therapeutic strategies forpeople with inflammatory and aging-associated diseases. Thiscollection brings together, in one comprehensive volume, a broadarray of information and insights into normal and alteredphysiology, molecular mechanisms of disease states, and newapplications of the rapidly evolving techniques ofproteomics.
Written by some of the finest investigators in this area, RedoxProteomics: From Protein Modifications to Cellular Dysfunction andDiseases examines the key topics of redox proteomics and redoxcontrol 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 structuralcharacterization of proteins affected by oxidative/nitrosativemodifications
* The response and regulation of protein oxidation in differentcell types
* The pathological implications of protein oxidation forconditions, including asthma, cardiovascular disease, diabetes,preeclampsia, and Alzheimer's disease
Distinguished by its in-depth discussions, balanced methodologicalapproach, and emphasis on medical applications and diagnosisdevelopment, Redox Proteomics is a rich resource for allprofessionals with an interest in proteomics, cellular physiologyand its alterations in disease states, and related fields.

Autoren/Hrsg.

Dalle-Donne, Isabella

Scaloni, Andrea

Butterfield, D. Allan

Weitere Mitwirkende

Desiderio, Dominic M.

Nibbering, Nico M.

Inhaltsverzeichnis

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 NitricOxide and Related Nitrogen Oxides (D. Thomas, et al.).
1.3 Mass Spectrometry Approaches for the MolecularCharacterization of Oxidatively/Nitrosatively Modified Proteins (A.Scaloni).
1.4 Thiol-disulfide Oxidoreduction of Protein Cysteines: OldMethods Revisted for Proteomics (V. Bonetto & P. Ghezzi).
1.5 Carbonylated Proteins and their Implication in Physiologyand 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 GlycoOxidated Proteins (A.Lapolla, et al.).
1.8 MudPIT (Multidimensaional Protein Identification Technology)for Identification of Post-translational Protein Modifications inComplex Biological Mixtures (S. Thomas, et al.).
1.9 Use of a Proteomic Technique to Identify Oxidant-SensitiveThiol Proteins in Cultured Cells (M. Hampton, et al.).
1.10 ICAT (Isotope-Code Affinity Tag) Approach to RedoxProteomics: Identification and Quantification of Oxidant-SensitiveProtein Thiols (M. Sethuraman, et al.).
1.11 Quantitative Determination of Free and Protein-Associated3-nitrotyrosine and S-nitrosothiols in the Circulation by MassSpectrometry and Other Methodologies: A Critical Review andDiscussion 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 SignalingMediated by Thiol Reactive Lipid Oxidation Products (D. Dickinson,et al.).
2.2 Early Molecular Events During Response to Oxidative Stressin Human Cells by Differential Proteomics (G. Tell).
2.3 Oxidative Damage to Proteins: Structural Modifications andConsequences in Cell Function (E. Cabiscol & J. Ros).
2.4 Oxidative Damage and Cellular Senescence: Lessons fromBacteria and Yeast (T. Nyström).
3. Redox Proteomic Analysis in Human Diseases.
3.1 Proteins as Sensitive Biomarkers of Human ConditionsAssociated with Oxidative Stress (I. Dalle-Donne, et al.).
3.2 Degradation and Accumulation of Oxidized Proteins inAge-Related Diseases (P. Voss & T. Grune).
3.3 Redox Proteomics: A New Approach to Investgate OxidativeStress 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: GlutathionylHemoglobin 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, andNitration 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 TyrosineNitration in Vascular Disease (L. Baker, et al.).
3.9 Oxidation of Artery Wall Proteins by Myeloperoxidase: Aproteomics 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 ChronicAirway Diseases: Proteomic Approaches to Identify Redox Processesin Epithelial Cell Signal and Inflammation (A. van der Vliet, etal.).
3.12 Sequestering Agents of Intermediate Reactive Aldehydes asInhibitors of Advanced Lipoxidation End-Products (ALEs) (M. Carini,et al.).

Über Autor(innen)

ISABELLA DALLE-DONNE, PHD, is Assistant Professor in theDepartment of Biology at the University of Milan, Italy. She has aPhD in cellular and molecular biology from the University of Milan.
ANDREA SCALONI, PHD, is First Investigator at theProteomics & Mass Spectrometry Laboratory, ISPAAM, NationalResearch Council in Naples, Italy. He received his PhD in chemicalsciences from the University of Rome "La Sapienza" in Italy.
D. ALLAN BUTTERFIELD, PHD, is Alumni Professor ofChemistry and Director of the University of Kentucky Center ofMembrane Sciences in Lexington, Kentucky, USA. He received his PhDin physical chemistry from Duke University.