Protein profiling of Guillain-Barre syndrome cerebrospinal fluid by two-dimensional electrophoresis and mass spectrometry

NEUROSCIENCE LETTERS

卷:485

Article

D'Aguanno, Simona^1,2  Franciotta, Diego³  Lupisella, Santina^1,2  Barassi, Alessandra⁴  Pieragostino, Damiana^6,7  Lugaresi, Alessandra^6,7  Centonze, Diego^2,8  D'Eril, Gianlodovico Melzi⁴  Bernardini, Sergio^1,5  Federici, Giorgio^1,5  Urbani, Andrea^1,2 

[1] Univ Roma Tor Vergata, Dept Internal Med, I-001339 Rome, Italy

[2] IRCCS Fdn Santa Lucia, Ctr Europeo Ric Cervello, Rome, Italy

[3] IRCCS, Inst C Mondino, Fdn Neurol, Pavia, Italy

[4] Univ Milan, Dipartimento Med Chirurg & Odontoiatria, I-20122 Milan, Italy

[5] Osped Pediat Bambin Gesu IRCCS, Lab Ric, Rome, Italy

[6] Ctr Studi Sull Invecchiamento CeSI, Chieti, Italy

[7] Univ G DAnnunzio, Chieti, Italy

[8] Univ Roma Tor Vergata, Dipartimento Neurosci, I-00173 Rome, Italy

关键词: Guillain-Barre syndrome;    CSF;    Proteomics;    Biomarkers;    Oxidative damage;    Protein carbonylation;   

DOI  :  10.1016/j.neulet.2010.08.060

来源: Elsevier

【 摘 要 】

Protein profiling of cerebrospinal fluid in Guillain-Barre syndrome (GBS), an acute and immune-mediated disease affecting the peripheral nervous system, was performed by two-dimensional electrophoresis. Significant modulated spots in GBS patients vs. control groups (a group of multiple sclerosis patients and one of healthy donors) underwent MALDI-TOF/TOF investigation. Inflammation-related proteins, such as vitamin D-binding protein, beta-2 glycoprotein I (ApoH), and a complement component C3 isoform were up-regulated in GBS, whereas transthyretin (the monomer and the dimer forms), apolipoprotein E, albumin and five of its fragments were down-regulated. Then, we used an isoelectric-focusing-dinitrophenylhydrazine-based technique to analyse the extent of carbonylation and, as a result, of oxidative damage of GBS CSF proteome. We observed a major sensitivity to carbonylation for albumin and alpha-glycoprotein in inflammation and a selective increase of reactivity for a glycosylated Fab from an IgM globulin in GBS CSF. Our results add new proteins to candidate CSF features of GBS, and suggest that oxidative stress could contribute to the immunopathological mechanisms in this syndrome. (C) 2010 Elsevier Ireland Ltd. All rights reserved.

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