Objective: To better understand the pathophysiological mechanisms underlying Guillain-Barré Syndrome (GBS) and to ascertain the protein that presents with the most observable changes in the cerebrospinal fluid (CSF) of patients GBS.
Methods: we analyzed individually the proteomes of CSF of patients with GBS (the experiment group) and control subjects suffering from other neurological disorders (the control group) with two-dimensional gel electrophoresis (2-DE). The harvested gel images analyzed with software to ascertain the most significant differential protein between the two groups and identify it by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF/TOF MS). We based the enzyme linked immuno-absorbent assay (ELISA) experiment, which followed, on the results of the first experiment.
Results: There are six of the protein spots had significant difference in expression between two group and identification made by mass spectrography revealed that the most significant disparity was cystatin C, which was decrease in the gels. The subsequent ELISA confirmed a considerable decrease in the level of cystatin C (P < 0.01) in the patients with GBS.
Conclusion: The level of cystatin C decreases significantly in the CSF of GBS and calls for further studying the role in the pathogenesis of GBS.