Glycosylation of Immunoglobulin G Associates With Clinical Features of Inflammatory Bowel Diseases

Šimurina, Mirna; Haan, Noortje de; Vučković, Frano; Kennedy, Nicholas A; Štambuk, Jerko; Falck, David; Trbojević‐Akmačić, Irena; Clerc, Florent; Razdorov, Genadij; Хон, А.Д.; Latiano, Anna; D’Incà, R.; Danese, Silvio; Targan, Stephan R.; Landers, Carol J.; Dubinsky, Marla; Campbell, Harry; Zoldoš, Vlatka; Permberton, Iain K.; Kolarich, Daniel; Fernandes, Daryl L.; Theorodorou, Evropi; Merrick, Victoria; Spencer, Daniel I. R.; Gardner, Richard A.; Doran, Ray; Shubhakar, Archana; Boyapati, Ray; Rudan, Igor; Lionetti, Paolo; Krištić, Jasminka; Novokmet, Mislav; Pučić‐Baković, Maja; Gornik, Olga; Andriulli, Angelo; Cantoro, Laura; Sturniolo, G.C.; Fiorino, Gionata; Manetti, Natalia; Arnott, Ian; Noble, Colin; Lees, Charlie W; Shand, Alan G.; Ho, Gwo‐Tzer; Dunlop, Malcolm G.; Murphy, Lee; Gibson, Jude; Evenden, Louise; Wrobel, Nicola; Gilchrist, T. L.; Fawkes, Angie; Kammeijer, Guinevere S. M.; Vojta, Aleksandar; Samaržija, Ivana; Markulin, Dora; Klasić, Marija; Dobrinić, Paula; Aulchenko, Yurii S.; Heuve, Tim van den; Jonkers, Daisy; Pierik, Marieke; McGovern, Dermot; Annese, Vito; Wuhrer, Manfred; Lauc, Gordan

doi:10.1053/j.gastro.2018.01.002

Cited by 131 publications

(110 citation statements)

References 93 publications

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“…When looking at IgG-Fc glycans, bisection in both TPSNG (A2FS0B) and isolated-IgG data was decreased in UC. However, the latter trait showed contradicting trends between discovery and replication cohort [10,50]. Different medication regimens might have affected the disease associations in this case and should be considered in future studies on TPSNG disease markers.…”

Section: Association Of N-glycome With Inflammatory Bowel Diseasesmentioning

confidence: 77%

“…). Interestingly, IgG‐Fc fucosylation changes differed between UC and CD . Similarly, the bisection of fucosylated, sialylated glycans (A2FSB), which is mostly attributable to IgA, IgM, and possibly also IgG‐Fab glycans, was increased in CD, but not significantly affected in UC .…”

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 94%

“…A high ratio between multibranched sialylated and galactosylated diantennary glycans in UC patients showed higher prognostic value than the two commonly used markers . In inflammatory diseases including IBD, the altered fucosylation and galactosylation of diantennary glycans can be attributed to changes in relative levels and the glycosylation of Igs, especially IgG , while the increased branching and sialylation were mostly caused by glycans derived from α1‐acid glycoprotein and other acute‐phase proteins released mainly by the liver (Fig. ).…”

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 97%

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N‐glycome signatures in human plasma: associations with physiology and major diseases

Dotz

Wuhrer

2019

FEBS Letters

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N‐glycome analysis in total plasma or serum yields information about the levels and glycosylation patterns of major plasma glycoproteins, including immunoglobulins, acute‐phase proteins, and apolipoproteins. Until recently, glycomic studies in disease settings largely suffered from small cohort sizes, poor analytical resolution, and poor comparability of results owing to the diversity of analytical techniques. Here, we report on recent advances in high‐throughput mass spectrometry glycomics technology that enabled elucidation of N‐glycome signatures in the plasma of patients with type 2 diabetes, inflammatory bowel disease, or colorectal cancer. Use of this technology revealed both commonalities and differences among disease fingerprints. Moreover, we summarize findings on glycomic signatures associated with age, sex, and body mass index. High‐throughput, high‐resolution glycomics technologies, together with robust data analysis workflows, will advance clinical translation.

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Section: Association Of N-glycome With Inflammatory Bowel Diseasesmentioning

confidence: 77%

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 94%

Section: N‐glycomic Signatures Of Major Human Diseasesmentioning

confidence: 97%

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N‐glycome signatures in human plasma: associations with physiology and major diseases

Dotz

Wuhrer

2019

FEBS Letters

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“…The discovery of N ‐glycan biomarkers in serum could lead to clinical implementation for disease detection. The majority of serum N ‐glycan methods focus on the analysis of a pool of N ‐glycans released from all proteins in the serum (Gornik et al., ; Kirmiz et al., ; Novokmet et al., ; Reiding et al., ; Ruhaak et al., ; Ruhaak, Xu, Li, Goonatilleke, & Lebrilla, ), or the analysis of one target protein's N ‐glycan profile (Comunale et al., ; Pompach et al., ; Ruhaak et al., , ; Shubhakar et al., ; Simunovic et al., ; Šimurina et al., ; Theodoratou et al., ; Zhang et al., ). Pooled serum analyses have shown trends in overall N ‐glycan changes in the presence of cancer, such as increased fucosylation, branching, and bisects (Gebrehiwot et al., ; Hecht et al., ; Snyder et al., ; Vučković et al., ).…”

Section: Commentarymentioning

confidence: 99%

Antibody Panel Based N‐Glycan Imaging for N‐Glycoprotein Biomarker Discovery

et al. 2019

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Antibody panel based N‐glycan imaging is a novel platform for N‐glycan analysis of immunocaptured proteins. N‐glycosylation is a post‐translational modification of pathophysiological importance and is often studied in the context of disease biomarkers. Determination of protein‐specific N‐glycosylation changes in patient samples has traditionally been laborious or limited to study of a single protein per analysis. This novel technique allows for the multiplexed analysis of N‐glycoproteins from biofluids. Briefly, this platform consists of antibodies spotted in an array panel to a microscope slide, specific capture of glycoproteins from a biological sample, and then enzymatic release of N‐glycans for analysis by matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry (MS). N‐glycans are detected at each individual spot, allowing N‐glycan information to easily be linked back to its protein carrier. Using this protocol, multiplexed analysis of N‐glycosylation on serum glycoproteins can be performed. Human serum is discussed here, but this method has potential to be applied to other biofluids and to any glycoprotein that can be captured by a validated antibody. © 2019 by John Wiley & Sons, Inc. Basic Protocol: Antibody panel based N‐glycan imaging by MALDI MS Support Protocol: Confirmation of antibody capture by IR‐labeled proteins

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“…Among all Igs, glycosylation within the IgG‐Fc region is relatively well‐studied. Many researchers have investigated IgG‐Fc glycosylation in different diseases, such as rheumatoid arthritis, lupus erythematosus, myasthenia gravis, hemolytic anemia, gastric cancer and inflammatory bowel disease . Some studies have also investigated the glycosylation pattern on the IgG‐Fab region.…”

Section: Introductionmentioning

confidence: 99%

Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry

Chen

Shiao

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid chromatography/tandem mass spectrometry (UHPLC/MS/MS). Only micro‐volumes of plasma were required from each sample and we also applied the method to discover IgA and IgA‐glycopeptide profiles in patients with chronic kidney diseases and IgA nephropathy. Methods Peptide M affinity beads were used to purify IgA, and a cost‐effective peptide analogue was added as internal standard. With an efficient on‐bead digestion process, purified samples were analyzed by UHPLC/MS/MS in multiple reaction monitoring mode. Results Correlation coefficients were greater than 0.999 for the IgA1 and IgA2 calibration curves and greater than 0.994 for glycopeptide regression curves. Intraday and interday precisions for IgA1 and IgA2 were <1.6% and <5.1% RSD, respectively. Intraday and interday accuracies ranged from 102.6 to 114.9% and 103.5 to 113.5% for IgA1 and IgA2, respectively. Stabilities of IgA1 and IgA2 at −80°C for 7 to 15 days ranged from 96.0 to 109.4%, respectively. The Pearson's correlation coefficient was 0.916 when comparing the IgA quantification results of the 30 clinical samples by using ELISAs and the developed UHPLC/MS/MS method. Compared with healthy controls, IgA and IgA‐glycopeptides showed different profiles in patients with chronic kidney diseases and IgA nephropathy. Conclusions The developed method showed good validation results, and the absolute quantification results of IgA correlated with those from ELISA. The pilot application study showed that IgA and IgA‐glycopeptides can be potential biomarker candidates for kidney diseases, and more clinical sample applications are worth investigating.

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Glycosylation of Immunoglobulin G Associates With Clinical Features of Inflammatory Bowel Diseases

Cited by 131 publications

References 93 publications

N‐glycome signatures in human plasma: associations with physiology and major diseases

N‐glycome signatures in human plasma: associations with physiology and major diseases

Antibody Panel Based N‐Glycan Imaging for N‐Glycoprotein Biomarker Discovery

Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry

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