Pregled bibliografske jedinice broj: 947392
Method optimization for the purification of the human serum IgG by affinity chromatography and determination of N- glycosylation pattern
Method optimization for the purification of the human serum IgG by affinity chromatography and determination of N- glycosylation pattern // Godišnja skupština Hrvatskog društva za proteomiku, 2017, Rijeka.
Rijeka, Hrvatska, 2017. (poster, domaća recenzija, neobjavljeni rad, znanstveni)
CROSBI ID: 947392 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Method optimization for the purification of the human serum IgG by affinity chromatography and determination of N- glycosylation pattern
Autori
Visentin, Sarah ; Klobučar, Marko ; Martinović, Tamara ; Josić, Đuro ; Kraljević Pavelić, Sandar
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni
Skup
Godišnja skupština Hrvatskog društva za proteomiku, 2017, Rijeka.
Mjesto i datum
Rijeka, Hrvatska, 11.10.2017. - 12.10.2017
Vrsta sudjelovanja
Poster
Vrsta recenzije
Domaća recenzija
Ključne riječi
IgG, N-glycans, affinity chromatography, MALDI TOF/TOF
Sažetak
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.
Izvorni jezik
Engleski
