Proteomic identification of potential protein markers in cerebrospinal fluid of GBS patients

Jin, Taiyi; Hu, Lifen; Chang, Ming; Wu, Jing; Winblad, Bengt; Zhu, Jiajia

doi:10.1111/j.1468-1331.2007.01761.x

Cited by 55 publications

(50 citation statements)

References 22 publications

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“…Candidate markers are reviewed with regard to their clinical relevance as potential surrogates for disease activity, prognosis assessment and predictors of treatment response. In addition, we review the first proteome analysis studies using two-dimensional differences in gel analysis (2D-DIGE) [27,37] and thereby show perspectives in CSF biomarker research in GBS.…”

Section: ■ Guillain-barré Syndromementioning

confidence: 99%

Cerebrospinal fluid biomarkers in Guillain-Barré syndrome – Where do we stand?

Brettschneider

Petzold²,

Süßmuth

et al. 2009

J Neurol

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Guillain-Barré syndrome (GBS) is an acute inflammatory polyneuropathy affecting the myelin-protein sheathing and the axons themselves to various degrees. Damage to these structures causes biomarkers to be released into the adjacent body fluid compartment. In case of the proximal nerve roots these biomarkers diffuse into the cerebrospinal fluid (CSF). Here we review the literature on CSF biomarkers in GBS, including a discussion of CSF basic findings, myelin sheath-associated markers (myelin basic protein), axonal damage markers (neurofilaments, tau, anti-ganglioside antibodies), glial and neuronal markers (neuron specific enolase, 14-3-3 proteins, S100B, hypocretin-1), immunological markers (different chemokines and complement factors, cystatin C, tumor necrosis factor-alpha) as well as recent advances in the field of CSF proteome analysis in GBS. Second, the different pathophysiological mechanisms reflected by these biomarkers are discussed. Finally, candidate biomarkers are reviewed with regard to their clinical relevance to act as a surrogate for the disease process, their value for improving prognostic accuracy and their potential to be used as predictors of treatment response.

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Section: ■ Guillain-barré Syndromementioning

confidence: 99%

Cerebrospinal fluid biomarkers in Guillain-Barré syndrome – Where do we stand?

Brettschneider

Petzold²,

Süßmuth

et al. 2009

J Neurol

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“…This fact must considerably simplify the identification of neuro-specific proteins and their fragments in the CSF. Previously, the CSF proteome of GBS patients was studied using exclusively the 2D-PAGE technique in search for proteins specifically up-or downregulated in GBS patients (25)(26)(27)(28). In total, Ͻ20 such proteins were identified in all those studies, and most were highly abundant plasma proteins.…”

mentioning

confidence: 99%

The Pathogenesis of the Demyelinating Form of Guillain-Barre Syndrome (GBS): Proteo-peptidomic and Immunological Profiling of Physiological Fluids

Ziganshin

Ivanova

Lomakin

et al. 2016

Molecular & Cellular Proteomics

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Acute inflammatory demyelinating polyneuropathy (AIDP) -the main form of Guillain-Barre syndrome-is a rare and severe disorder of the peripheral nervous system with an unknown etiology. One of the hallmarks of the AIDP pathogenesis is a significantly elevated cerebrospinal fluid (CSF) protein level. In this paper CSF peptidome and proteome in AIDP were analyzed and compared with multiple sclerosis and control patients. A total protein concentration increase was shown to be because of even changes in all proteins rather than some specific response, supporting the hypothesis of protein leakage from blood through the blood-nerve barrier. The elevated CSF protein level in AIDP was complemented by activization of protein degradation and much higher peptidome diversity. Because of the studies of the acute motor axonal form, Guillain-Barre syndrome as a whole is thought to be associated with autoimmune response against neurospecific molecules. Thus, in AIDP, autoantibodies against cell adhesion proteins localized at Ranvier's nodes were suggested as possible targets in AIDP. Indeed, AIDP CSF peptidome analysis revealed cell adhesion proteins degradation, however no reliable dependence on the corresponding autoantibodies levels was found. Proteome analysis revealed overrepresentation of Gene Ontology groups related to responses to bacteria and virus infections, which were earlier suggested as possible AIDP triggers. Immunoglobulin blood serum analysis against most common neuronal viruses did not reveal any specific pathogen; however, AIDP patients were more immunopositive in average and often had polyinfections. Cytokine analysis of both AIDP CSF and blood did not show a systemic adaptive immune response or general inflammation, whereas innate immunity cytokines were up-regulated. To supplement the widely-accepted though still unproven autoimmunity-based AIDP mechanism we propose a hypothesis of the primary peripheral nervous system damaging initiated as an innate immunity-associated local inflammation following neurotropic viruses egress, whereas the autoantibody production might be an optional complementary secondary process. Molecular & Cellular

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“…2-D DIGE effectively eliminates gel-togel variability that is associated with standard 2-D PAGE and improves the accuracy of quantitative protein profi ling (Friedman, 2007). This technology has been used for protein profi ling in numerous organisms including bacteria (Rathsam et al 2005), yeast , plants (Bohler et al 2007;Keeler et al 2007), animals (Henkel et al 2006;Kisby et al 2006), and human (Jin et al 2007;Reynolds et al 2007). It is also used for analysis of phosphoproteins (Stasyk et al 2005) and protein-protein interaction (Lyakhovich et al 2007).…”

Section: Polyacrylamide Gel Electrophoresis (Page)mentioning

confidence: 99%

Use of Proteomics Analysis for Molecular Precision Approaches in Cancer Therapy

Shen¹,

Senzer

Nemunaitis

2008

Drug Target�Insights

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Abstract:The rapidly expanding data sets derived from genomic and transcriptomic analyses have allowed greater understanding of structural and functional network patterns within the genome resulting in a realignment of thinking within a systems biologic framework of cancer. However, insofar as spatially and temporally dynamic differential gene expression at the protein level is the mediate effector of cellular behavior and, in view of extensive post translational modifi cation (PTM), the need for sensitive, quantitative, and high throughput proteomic analytic techniques has emerged. To circumvent the problems of tissue sample heterogeneity, laser capture microdissection (LCM) allows for the acquisition of homogeneous cell populations. Using different fl uorescent dyes to label protein samples prior to gel electrophoresis, 2-D DIGE (twodimensional differential in-gel electrophoresis) can, with reasonable sensitivity, process three protein samples on the same gel allowing for intragel relative quantifi cation. MudPIT (multidimensional protein identifi cation technology) is a non-gel approach exploiting the unique physical properties of charge and hydrophobicity which allows the separation of peptide mixtures as well as direct MS (mass spectrometry) and database searching. The introduction of iTRAQ (isobaric tags for relative and absolute quantifi cation) achieves labeling of all peptides by employing an 8-plex set of amine reactive tags to derivatize peptides at the N-terminus and lysine side chains allowing for absolute quantifi cation and assessment of PTM. These and other new laboratory technologies, along with improved bioinformatics tools, have started to make signifi cant contributions in cancer diagnostics and treatments.

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Proteomic identification of potential protein markers in cerebrospinal fluid of GBS patients

Cited by 55 publications

References 22 publications

Cerebrospinal fluid biomarkers in Guillain-Barré syndrome – Where do we stand?

Cerebrospinal fluid biomarkers in Guillain-Barré syndrome – Where do we stand?

The Pathogenesis of the Demyelinating Form of Guillain-Barre Syndrome (GBS): Proteo-peptidomic and Immunological Profiling of Physiological Fluids

Use of Proteomics Analysis for Molecular Precision Approaches in Cancer Therapy

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