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Method optimization for the purification of the human serum IgG by affinity chromatography and determination of N- glycosylation pattern

Laryngeal squamous cell carcinoma (LSCC) is the most common form of head and neck cancers that contributes to 2-5% of newly diagnosed malignancies worldwide [1]. All of the studies made had shown elevated immunoglobulin G (IgG) expression in the serum from LSCC patients compared to healthy controls, or at least a tendency towards such an elevation [2-4]. However, the level of expression itself is not the only parameter of importance. Alteration in the glycosylation of IgG molecules can influence the structure and stability of IgG and even some of the effector functions, such as binding affinity towards IgG Fc receptors. Such aberrations in the IgG glycosylation were observed in a number of different tumours including lung, gastric [5], ovarian [6], prostate [7], colorectal [8, 9] and breast cancer [10]. Those changes in the glycosylation pattern were frequently found to be in correlation with tumour progression and therapy response. Moreover, the sialylation of the Fc fragment of IgG molecule can even result in anti-inflammatory properties through its engagement with distinct Fcγ receptors, thereby influencing immune response to cancer [11]. Here, we have focused on method optimization for the purification of IgG from serum of a healthy donor using affinity chromatography and determination of N- glycosylation pattern of isolated IgG by MALDI-TOF/TOF mass spectrometry . The aim of the method optimisation is to investigate the difference bethween N-glycosilation pattern of IgG from serum of patients that suffer from metastatic and non-metastatic laryngeal squamous cell carcinoma.

IgG, N-glycans, affinity chromatography, MALDI TOF/TOF

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