title: Capillary electrophoresis analysis of N-glycosylation changes of serum paraproteins in multiple myeloma.
abstract: 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 fragment crystallizable region (Fc) and fragment antigen binding (Fab) κ/λ light chain fractions of papain digested immunoglobulins from multiple myeloma patients. CE-LIF detection 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 six features were identified with similar significance at the immunoglobulin level, including the analysis of the partitioned Fcfragment as well as the Fabκ and Fabλ chains.
authors.affiliation: Horváth Csaba Memorial Institute for Bioanalytical Research, University of Debrecen, Hungary.
authors.forename: Zsuzsanna
authors.initials: Z
authors.lastname: Kovacs
authors.affiliation: Horváth Csaba Memorial Institute for Bioanalytical Research, University of Debrecen, Hungary.
authors.forename: Adam
authors.initials: A
authors.lastname: Simon
authors.affiliation: Thermo Fisher Scientific, Sunnyvale, CA, USA.
authors.forename: Zoltan
authors.initials: Z
authors.lastname: Szabo
authors.affiliation: 1st Department of Internal Medicine, Semmelweis University, Budapest, Hungary.
authors.forename: Zsolt
authors.initials: Z
authors.lastname: Nagy
authors.affiliation: Department of Hematology, Institute for Medicine, University of Debrecen, Debrecen, Hungary.
authors.forename: Laszlo
authors.initials: L
authors.lastname: Varoczy
authors.affiliation: Department of Hematology, Institute for Medicine, University of Debrecen, Debrecen, Hungary.
authors.forename: Ildiko
authors.initials: I
authors.lastname: Pal
authors.affiliation: Semmelweis Hospital, Miskolc, Hungary.
authors.forename: Eszter
authors.initials: E
authors.lastname: Csanky
authors.affiliation: Horváth Csaba Memorial Institute for Bioanalytical Research, University of Debrecen, Hungary.|MTA-PE Translational Glycomics Research Group, University of Pannonia, Veszprem, Hungary.
authors.forename: Andras
authors.initials: A
authors.lastname: Guttman
mesh_terms: D019075:Electrophoresis, Capillary / Q000379:methods*; D005260:Female; D006031:Glycosylation; D006801:Humans; D008297:Male; D009101:Multiple Myeloma / Q000097:blood* / Q000378:metabolism; D010266:Paraproteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D011134:Polysaccharides / Q000097:blood* / Q000737:chemistry / Q000378:metabolism
chemical_list: D010266:Paraproteins; D011134:Polysaccharides
keywords: CE-LIF; Multiple myeloma; N-glycans