Capillary electrophoresis analysis of N-glycosylation changes of serum paraproteins in multiple myeloma.

Research paper by Zsuzsanna Z Kovacs, Adam A Simon, Zoltan Z Szabo, Zsolt Z Nagy, Laszlo L Varoczy, Ildiko I Pal, Eszter E Csanky, Andras A Guttman

Indexed on: 25 Jan '17Published on: 25 Jan '17Published in: ELECTROPHORESIS


Multiple myeloma (MM) is an immedicable malignancy of the human plasma cells producing abnormal antibodies (also referred to as paraproteins) leading to kidney problems and hyperviscosity syndrome. In this paper we report on the N-glycosylation analysis of paraproteins from total human serum as well as the Fc and Fab κ/λ light chain fractions of papain digested immunoglobulins from multiple myeloma patients. Capillary electrophoresis with laser induced fluorescence detection (CE-LIF) was used for the analysis of the N-glycans after endoglycosidase (PNGase F) mediated sugar release and fluorophore labeling (APTS). While characteristic N-glycosylation pattern differences were found between normal control and untreated, treated and remission stage multiple myeloma patient samples at the global serum level, less distinctive changes were observed at the immunoglobulin level. Principal component analysis adequately differentiated the four groups (control and three patient groups) on the basis of total serum N-glycosylation analysis. 12 N-glycan features showed statistically significant differences (p<0.05) among various stages of the disease in comparison to the control at the serum level, while only 6 features were identified with similar significance at the immunoglobulin level, including the analysis of the partitioned Fc fragment as well as the Fab κ and Fab λ chains. This article is protected by copyright. All rights reserved.