0000000000076853
AUTHOR
Pierluigi Mauri
Feasibility of shotgun urinary proteomics for investigating prematurely born preschoolers (PBP)
Background: Preterms and twins are at higher risk of respiratory morbidity later in life. Advances in proteomic approaches may allow the characterization of biomarkers involved in respiratory diseases (Mauri et al. Imm. Lett. 2014;162:2-10). Gel-free approach quantitatively identify differentially expressed proteins in relation to physiopathological conditions (Mauri&Dehò, Meth Enzymology 2008;447:99-117). This can improve the clinical reliability of the next generation of biomarkers to discriminate multiple phenotypes of childhood respiratory diseases. Aim: To assess the ability of gel-free proteomics for identifying specific protein profiles related to PBP. Methods: Urine samples were…
Shotgun Proteomics of Isolated Urinary Extracellular Vesicles for Investigating Respiratory Impedance in Healthy Preschoolers
Urine proteomic applications in children suggested their potential in discriminating between healthy subjects from those with respiratory diseases. The aim of the current study was to combine protein fractionation, by urinary extracellular vesicle isolation, and proteomics analysis in order to establish whether different patterns of respiratory impedance in healthy preschoolers can be characterized from a protein fingerprint. Twenty-one 3–5-yr-old healthy children, representative of 66 recruited subjects, were selected: 12 late preterm (LP) and 9 full-term (T) born. Children underwent measurement of respiratory impedance through Forced Oscillation Technique (FOT) and no significant differen…
Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry
The formation of multiple proteoforms by post-translational modifications (PTMs) enables a single protein to acquire distinct functional roles in its biological context. Oxidation of methionine residues (Met) is a common PTM, involved in physiological (e.g., signaling) and pathological (e.g., oxidative stress) states. This PTM typically maps at multiple protein sites, generating a heterogeneous population of proteoforms with specific biophysical and biochemical properties. The identification and quantitation of the variety of oxidized proteoforms originated under a given condition is required to assess the exact molecular nature of the species responsible for the process under investigation…