Glycoprotein biomarkers and analysis in chronic obstructive pulmonary disease and lung cancer with special focus on serum immunoglobulin G

Komàromy, András M.; Reider, Balazs; Járvás, Gábor; Guttman, András

doi:10.1016/j.cca.2020.03.041

Cited by 23 publications

(9 citation statements)

References 123 publications

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“…However, for s-IgG in NE group significantly lower SNA-reactivity and galactose expression, and significantly higher agalactosylation factor GSL-II/RCA-I in comparison to E group were observed. Reduced sialylation and galactosylation is typical for inflammatory condition and abnormal glycosylation patterns of glycoproteins are associated with various diseases, such as inflammation or cancer, what was reported in many independent studies 24,36,37 . Also endometriosis is a disease accompanied by the development of inflammation 10,38 .…”

Section: Discussionmentioning

confidence: 58%

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

Sołkiewicz

Krotkiewski

Jędryka

et al. 2021

Sci Rep

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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.

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Section: Discussionmentioning

confidence: 58%

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

Sołkiewicz

Krotkiewski

Jędryka

et al. 2021

Sci Rep

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“…IgG is one of the most abundant glycoproteins in circulation, with a serum concentration ranging from 7 to 18 mg/mL in healthy adults (16). Dysregulation of IgG glycosylation has been revealed in various cancers including TC (19,20,(30)(31)(32)(33)(34). In our previous study, we found the distribution of IgG galactosylation referred to IgG Gal-ratio had a common feature and was increased in multiple types of cancer (not including TC) compared to non-cancer controls.…”

Section: Discussionmentioning

confidence: 94%

Diagnostic Potential of Plasma IgG N-glycans in Discriminating Thyroid Cancer from Benign Thyroid Nodules and Healthy Controls

Zhang

Liu

et al. 2021

Front. Oncol.

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BackgroundNovel biomarkers are urgently needed to distinguish between benign and malignant thyroid nodules and detect thyroid cancer in the early stage. The associations between serum IgG N-glycosylation and thyroid cancer risk have been revealed. We aimed to explore the potential of IgG N-glycan traits as biomarkers in the differential diagnosis of thyroid cancer.MethodsPlasma IgG N-glycome analysis was applied to a discovery cohort followed by independent validation. IgG N-glycan profiles were obtained using a robust quantitative strategy based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. IgG N-glycans were relatively quantified, and classification performance was evaluated based on directly detected and derived glycan traits.ResultsFour directly detected glycans were significantly changed in thyroid cancer patients compared to that in non-cancer controls. Derived glycan traits and a classification glycol-panel were generated based on the directly detected glycan traits. In the discovery cohort, derived trait BN (bisecting type neutral N-glycans) and the glyco-panel showed potential in distinguishing between thyroid cancer and non-cancer controls with AUCs of 0.920 and 0.917, respectively. The diagnostic potential was further validated. Derived trait BN and the glycol-panel displayed “accurate” performance (AUC>0.8) in discriminating thyroid cancer from benign thyroid nodules and healthy controls in the validation cohort. Meanwhile, derived trait BN and the glycol-panel also showed diagnostic potential in detecting early-stage thyroid cancer.ConclusionsIgG N-glycome analysis revealed N-glycomic differences that allow classification of thyroid cancer from non-cancer controls. Our results suggested that derived trait BN and the classification glyco-panel rather than single N-glycans may serve as candidate biomarkers for further validation.

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“…As mentioned before, many surface proteins are glycosylated with aberrant glycosylation patterns often related to disease (Komaromy et al, 2020). Cancer cells, for instance, have altered glycosylation patterns (e.g., core fucosylation [Miyoshi, 2008], alternative branching [Chandler et al, 2019], O-glycan alteration [Kudelka et al, 2015], and sialylation [Almaraz et al, 2012, Saeui et al, 2020).…”

Section: Glycocapturementioning

confidence: 99%

Mass spectrometry and the cellular surfaceome

Pauwels

Fijałkowska

Eyckerman

et al. 2021

Mass Spectrometry Reviews

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The collection of exposed plasma membrane proteins, collectively termed the surfaceome, is involved in multiple vital cellular processes, such as the communication of cells with their surroundings and the regulation of transport across the lipid bilayer. The surfaceome also plays key roles in the immune system by recognizing and presenting antigens, with its possible malfunctioning linked to disease. Surface proteins have long been explored as potential cell markers, disease biomarkers, and therapeutic drug targets. Despite its importance, a detailed study of the surfaceome continues to pose major challenges for mass spectrometry‐driven proteomics due to the inherent biophysical characteristics of surface proteins. Their inefficient extraction from hydrophobic membranes to an aqueous medium and their lower abundance compared to intracellular proteins hamper the analysis of surface proteins, which are therefore usually underrepresented in proteomic datasets. To tackle such problems, several innovative analytical methodologies have been developed. This review aims at providing an extensive overview of the different methods for surfaceome analysis, with respective considerations for downstream mass spectrometry‐based proteomics.

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Glycoprotein biomarkers and analysis in chronic obstructive pulmonary disease and lung cancer with special focus on serum immunoglobulin G

Cited by 23 publications

References 123 publications

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

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

Diagnostic Potential of Plasma IgG N-glycans in Discriminating Thyroid Cancer from Benign Thyroid Nodules and Healthy Controls

Mass spectrometry and the cellular surfaceome

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