Mass spectrometry for the detection of differentially expressed proteins: a comparison of surface‐enhanced laser desorption/ionization and capillary electrophoresis/mass spectrometry

Abstract

The discovery of biomarkers is currently attracting much interest as it harbors great potential for the diagnosis and monitoring of human diseases. Here we have used two advanced mass spectroscopy based technologies, surface enhanced laser desorption ionization (SELDI‐MS) and capillary electrophoresis/mass spectrometry (CE/MS), to obtain proteomic patterns of urine samples from patients suffering from membranous glomerulonephritis (MGN) and healthy volunteers. The results indicate that CE/MS analysis is able to display a rich and complex pattern of polypeptides with high resolution and high mass accuracy. In order to analyze these patterns, the MosaiqueVisu software was developed for peak identification, deconvolution and the display of refined maps in a three‐dimensional format. The polypeptide profiles obtained with SELDI‐MS from the same samples are much sparser and show lower resolution and mass accuracy. The SELDI‐MS profiles are further heavily dependent on analyte concentration. SELDI‐MS analysis identified three differentially expressed polypeptides, which are potential biomarkers that can distinguish healthy donors from patients with MGN. In contrast, approximately 200 potential biomarkers could be identified by CE/MS. Thus, while SELDI‐MS is easy to use and requires very little sample, CE/MS generates much richer data sets that enable an in‐depth analysis. Copyright © 2003 John Wiley & Sons, Ltd.