| Objectives: Guillain–Barrésyndrome (GBS) is an immune-mediated inflammatory disease of the peripheral nerves involving mainly the myelin sheath. It is now the most common cause of acute flaccid paralysis in the world. Increased protein level without pleocytosis in the cerebrospinal fluid (CSF) is a characteristic of patients with GBS.GBS occurs worldwide and with an often severe course and poor prognosis. Even when patients are treated in well-equipped intensive care units, mortality rates are still 3–7%. Moreover, about 7–15% of patients have permanent neurological sequelae, which severely affect the patients daily life. There is a high morbidity rate of GBS in northern China , since 1973, the total number of hospital patients of GBS is more than 2200 in The Second Hospital of Hebei Medical University. High invalidity rate and mortality rate of GBS have caused high attention to it. However, the molecular mechanisms underlying the disease remain poorly understood and so far no reliable disease-related markers are available. Recently the treatment of intravenous immunoglobulin (IVIg) is testified to be effective for GBS patients. If we could know what the relevant antibody, complement and cytokine in the blood of GBS patients are and how these proteins content change through the treatment of large dose of IVIg , it will be significant in comprehending the molecular pathomechanisms underlying GBS and the mechanisms of immunoglobulin.Proteomics has increasingly been used to the studies of differentially expressed proteins related to diseases. Proteomics offers scientists the possibility of identifying disease-associated protein markers to assist in diagnosis or prognosis and to select potential targets for specific drug therapy. Proteomics is a sign of the post-genome era.In this study, by means of comparative proteomic analysis with high-resolution two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (MS) and database searching, we have studied the serum of GBS patients without IVIG (without IVIG group) compared with GBS patients with IVIG (IVIG group) to provide new insight into the pathomechanisms underlying GBS, aim at understanding the molecular mechanisms of immunoglobulin.Methods: The serum of GBS patients was obtained at The Second Hospital of Hebei Medical University. The serum proteins extracted with mixture of urea, CHAPS, DTT, IPG buffer were run IPG isoelectric focusing electrophoresis as the first dimension, and then run vertical SDS-PAGE as the second dimension. The gels were visualized by colloidal coomassive blue staining and analysised with ImageMaster 2D Elite software, The proteins of interest were in-gel digested and identified using MALDI-TOF /TOF tandem mass spectrometry.Results: With the help of Image Master 2D Elite software, 20 down-regulated protein spots in 2D gels of IVIG group were found compared with without IVIG group, which were identified as Complement C3,Complement C4-A,Complement C4-B, Alpha-2-macroglobulin, Peroxiredoxin-2, Ceruloplasmin, Serotransferrin, Vitamin D-binding protein,Serum amyloid P-component,Clusterin,Haptoglobin,Beta-2-glycoprotein1, Alpha-1-antichymotrypsin, Apolipoprotein A-I, Apolipoprotein A-IV, Complement factor B, Complement factor H, Afamin,Hemopexin, Ficolin-3. While 10 up-regulated proteins in IVIG group were identified as Transthyretin, Alpha-1-antitrypsin, ApolipoproteinE, Retinol-binding protein 4,Complement C1s subcomponent,Inter-alpha-trypsin inhibitor heavy chain H4,Ig gamma-1 chain C region, Ig alpha-1 chain C region, Ig kappa chain C region, CD5 antigen-like.Conclusions: We discovered a number of differential expression proteins by proteomics ,which will help us to deeply understand the pathogenesis of GBS and the molecular mechanisms of immunoglobulin,and some of which will be expected to produce a marked effect on new drugs exploitation.
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