Variability of serum IgG sialylation and galactosylation degree in women with advanced endometriosis

Abstract

Endometriosis is an inflammatory disease which diagnostics is difficult and often invasive, therefore non-invasive diagnostics methods and parameters are needed for endometriosis detection. The aim of our study was to analyse the glycosylation of native serum IgG and IgG isolated from sera of women classified as: with endometriosis, without endometriosis but with some benign ginecological disease, and control group of healthy women, in context of its utility for differentiation of advanced endometriosis from the group of healthy women. IgG sialylation and galactosylation/agalactosylation degree was determined using specific lectins: MAA and SNA detecting sialic acid α2,3- and α2,6-linked, respectively, RCA-I and GSL-II specific to terminal Gal and terminal GlcNAc, respectively. The results of ROC and cluster analysis showed that the serum IgG MAA-reactivity, sialylation and agalactosylation factor may be used as supplementary parameters for endometriosis diagnostics and could be taken into account as a useful clinical tool to elucidate women with high risk of endometriosis development. Additionally, we have shown that the analysis of native serum IgG glycosylation, without the prior time-consuming and expensive isolation of the protein, is sufficient to differentiation endometriosis from a group of healthy women.

The Alterations of Serum IgG Fucosylation as a Potential Additional New Diagnostic Marker in Advanced Endometriosis

“…Based on the results of our previous study concerning sialylation of serum IgG in endometriosis 41 we also observed the presence of strong positive correlations between the specific reactivity of s-IgG and i–IgG with AAL, LCA and UEA, and their reactivity with sialo-specific lectin MAA (data not shown). The above observation is in accordance with the fact that highly sialylated IgG with a high content of fucose has a protective effect, because increased expression of fucose in IgG glycans contributes to a decrease in antibody-dependent cytotoxicity, 68–71 increases the stability of the Fc fragment of IgG 62 and, together with an increase in sialic acid expression, enhances the anti-inflammatory properties of IgG.…”

“…The lectin-ELISA test was performed according to the procedure previously described, 41 with slight modification. In short: the microtiter plates were incubated with 0.01 mg/mL protein G solution (Abcam, United States) in 10mM TBS pH 7.4 (2h, 37°C, and next at 4°C overnight).…”

“…Immunoglobulin G was isolated from blood serum using affinity chromatography on a Protein A/Protein G Sepharose column, according to the method described earlier by Ey et al 43 and in our previous study. 41 …”

“…The order of statistical analyses performed in the present study was based on our previous experience. 41 , 42 …”

Clinical Mass Spectrometry Discovered Human IgG Sialylation as a Potential Biosignature for Kidney Function

“…It has been widely applied to biological and clinical samples for small molecule and biomolecule analyses. IgG and glycopeptides have recently been monitored and correlated with many disease statuses as biological signatures for diagnosis or progression [ 19 , 20 ]. In those studies, LC coupled with MS was usually the main analytical tool.…”