The oxido-redox potential of albumin: Methodological approach and relevance to human diseases |
| |
| Institution: | 1. Laboratory on Pathophysiology of Uremia, G. Gaslini Children Hospital, Genoa, Italy;2. Mass Spectrometry Core Facility and Laboratory of Molecular Medicine, G. Gaslini Children Hospital, Genoa, Italy;3. Renal Child Foundation, Genoa, Italy;4. University of Rome “Tor Vergata”, Department of Internal Medicine, Rome, Italy;5. IRCCS-Fondazione Santa Lucia Centro di Ricerca sul Cervello, Rome, Italy;1. Laboratory of Peptide and Protein Chemistry and Biology, Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 13, 50019, Sesto Fiorentino, Italy;2. Department of Medicine, University of Padova, Diabetology and Dietetics, ULSS 6 Euganea, Via dei Colli, 35143, Padova, Italy;3. Laboratory of Peptide and Protein Chemistry and Biology, Department of Neurosciences, Psychology, Drug Research and Child Health - Section of Pharmaceutical Sciences and Nutraceutics, University of Florence, Via Ugo Schiff 6, 50019, Sesto Fiorentino, Italy;4. Platform of Peptide and Protein Chemistry and Biology – PeptLab@UCP and Laboratory of Chemical Biology EA4505, Université Paris-Seine, 5 Mail Gay-Lussac, 95031, Cergy-Pontoise CEDEX, France;5. Istituto di Ricerca Pediatrica, Città della Speranza, Via Nicolò Giustiniani, 2, 35128 Padova, Italy;1. Institute of Neurobiology, Institutes of Brain Science, State Key Laboratory of Medical Neurobiology and Collaborative Innovation Center for Brain Science, Fudan University, 138 Yixueyuan Road, Shanghai 200032, China;2. Cell Electrophysiology Laboratory, Wannan Medical College, 22 West Wenchang Road, Wuhu, Anhui 241002, China;1. Department of Medical Biochemistry, Medical University of Wroclaw, Chalubinskiego 10, 50-368 Wroclaw, Poland;2. Department of Organic and Pharmaceutical Technology, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland |
| |
| Abstract: | In humans, an increased synthesis of reactive oxygen species (ROS) may be a relevant cause of amplification of physiologic processes resulting in inflammatory organ damage or neoplasia. Efficient anti-oxidative systems targeting oxidative stress are thus essential to prevent tissue damage. In plasma, proteins proved to be the first line of defence against ROS and albumin, the highest concentration plasma protein, has a key role in this antioxidant function. Recent studies have clearly documented that albumin oxido-redox potential changes upon oxidation by different oxidants thus becoming a deputy biomarker of this process.ROS react primarily with the free 34Cysteine (34Cys) residue of albumin to form two reversible intermediate derivatives, sulfenic-(SOH-alb) and sulfinic acid (SO2H-alb), resulting in sulfonic acid (SO3H-alb), the final stable product of the reaction.Upon stable oxidation (SO3H-alb), albumin properties are altered: the protein becomes more susceptible to trypsin digestion and is degraded faster compared to the non-oxidized counterpart.The present review focuses on the characterization of albumin chemical changes induced by ROS, their relevance in human pathology and the most recent advances in the approach to oxidation adduct analysis. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
