The Proteomic Analysis of Sera for the Discovery of Biomarkers for Multiple Myeloma.

Multiple Myeloma (MM) fits in the group of plasm cell disorders characterized by neoplastic proliferation of single clone of plasma cell engaged in the production of a monoclonal immunoglobulin. The cause of MM is unclear, but a genetic predisposition may play a role and cytogenetic abnormalities are considered to be the most important prognostic factor. The proteomic analysis of MM emerges as a key complement to gene expression profiling, primarily because regulation of protein expression can buffer the magnitude of changes occurring at the gene transcription level. In the present study, to identify biomarkers of initial diagnosis, detection of relapse, monitoring for minimal residual disease and prognostic marker in MM by a lesser invasive method, serum proteins reflecting alteration in their proteomes were analyzed. We compared two-dimensional electrophoresis patterns of human sera of twelve patients with multiple myeloma with that of normal twelve subjects. The differentially expressed spots were identified by matrix-assisted laser desorption/ionization-time-of flight (MALDI-TOF) and electrospray ionization quadupole time of flight (ESI-Q-TOF) mass spectrometry. We identified several proteins altered in sera of MM patients. These results suggest that these proteins can be used as a lesser invasive diagnostic, monitoring and prognositic biomarkers of MM if further studies were done.