title: Unraveling oxidation-induced modifications in proteins by proteomics.
abstract: Oxidative stress-driven modifications can occur in lipids, proteins, and DNA and form the basis of several chronic pathologies. The metabolites generated during oxidative responses consist of very reactive substances that result in oxidative damage and modulation of redox signaling as the main outcomes. Oxidative modifications occurring in proteins are poorly understood; among the several methods employed to study such modifications, the most promising strategies are based on proteomics approaches. Proteomics has emerged as one of the most powerful and sensitive analytical tools for mapping the oxidative changes present in proteins in a wide range of sample types and disease models. This chapter addresses the main aspects of redox processes, including an overview of oxidative stress and its biological consequences on proteins. Moreover, major proteomic strategies that can be employed as powerful tools for understanding protein oxidative modifications detected in chronic pathologies are discussed, highlighting cancer research as a model.
authors.affiliation: Laboratory of Physiopathology and Free Radicals, Department of General Pathology, State University of Londrina, Londrina, Paraná, Brazil. Electronic address: carolpanis@sercomtel.com.br.
authors.forename: Carolina
authors.initials: C
authors.lastname: Panis
mesh_terms: D000818:Animals; D006706:Homeostasis; D006801:Humans; D009369:Neoplasms / Q000378:metabolism; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics
chemical_list: D011506:Proteins
keywords: Cancer; Cysteine–thiol content; Oxidative stress; Proteomics; Redox homeostasis