c-MET associated with osteogenesis in multiple myeloma patients by induction of MMP9 expression by HGF in BMSCs

e248 interaction ultra-performance liquid chromatography (HILICUPLC). Isolation of IgG dominant clones was achieved using charge variant analysis. Glycan structures and localisation were elucidated by anion-exchange chromatography(AEC) and LC-MS analysis. Non-supervised principal component analysis(PCA) was employed to detect distinguishable chromatographic features in the studied groups. Results: 75 unique N-glycan peaks with statistically significant(p<0.05) chromatogram variation were observed across the 4 studied groups. Multivariate analysis of integrated data of these glycan peaks showed distinct clustering of disease states(MGUS vs. newly-diagnosed MM). Across the myeloma spectrum, differences were observed in the chromatographic profile of each IgG dominant clone. Further glycan-localisation analysis of these dominant clones showed increased sialylation on the Fab region. Discussion: The observed variation in N-glycosylation profiles of serum IgG across the spectrum of plasma cell disorder showed promising potential as biomarkers in disease progression. The unique glycan profile of each IgG monoclonal paraprotein reflected the heterogenous nature of myeloma. Further study in our group is in progress to investigate the effect of Fab sialylation on the functional aspect of the IgGparaprotein such as immune complex formation and receptor binding.