Alterations of glycan branching and differential expression of sialic acid on alpha fetoprotein among hepatitis patients

Mondal, Gautam; Chatterjee, Urmimala; Chawla, Yogesh; Chatterjee, Bishnu P.

doi:10.1007/s10719-010-9316-z

Cited by 24 publications

(16 citation statements)

References 48 publications

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“…Alpha 1-Acid Glycoprotein (AGP) Highly branched N-linked glycan Cirrhosis and HCC, congenital disorders, RA, SLE [35,36] Increased sialylation Cancer [37] Decreased sialylation Cirrhosis and HCC [35,38] Increased fucosylation liver cancer [39] Alpha-Fetoprotein Elevated bisecting N-acetylglucosamine, decrease in sialylation and increase in fucosylation Cirrhosis, hepatitis and HCC [40][41][42] Alpha -1-antitrypsin (ATT)…”

Section: Glycoprotein Glycation Change Related Diseases Referencesmentioning

confidence: 99%

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Fuertes-Martín

Correig

Vallvé

et al. 2020

JCM

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Several studies suggest that variations in the concentration of plasma glycoproteins can influence cellular changes in a large number of diseases. In recent years, proton nuclear magnetic resonance (1H-NMR) has played a major role as an analytical tool for serum and plasma samples. In recent years, there is an increasing interest in the characterization of glycoproteins through 1H-NMR in order to search for reliable and robust biomarkers of disease. The objective of this review was to examine the existing studies in the literature related to the study of glycoproteins from an analytical and clinical point of view. There are currently several techniques to characterize circulating glycoproteins in serum or plasma, but in this review, we focus on 1H-NMR due to its great robustness and recent interest in its translation to the clinical setting. In fact, there is already a marker in H-NMR representing the acetyl groups of the glycoproteins, GlycA, which has been increasingly studied in clinical studies. A broad search of the literature was performed showing a general consensus that GlycA is a robust marker of systemic inflammation. The results also suggested that GlycA better captures systemic inflammation even more than C-reactive protein (CRP), a widely used classical inflammatory marker. The applications reviewed here demonstrated that GlycA was potentially a key biomarker in a wide range of diseases such as cancer, metabolic diseases, cardiovascular risk, and chronic inflammatory diseases among others. The profiling of glycoproteins through 1H-NMR launches an encouraging new paradigm for its future incorporation in clinical diagnosis.

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Section: Glycoprotein Glycation Change Related Diseases Referencesmentioning

confidence: 99%

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Fuertes-Martín

Correig

Vallvé

et al. 2020

JCM

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“…Three biotinylated lectins (Vector Laboratories, Burlingame, CA, USA) were used in the current study: Aleuria Aurantia Lectin (AAL) (18) for fucose detection, Ricinus Communis Agglutinin I (RCA I) (19) for galactose detection, and Elderberry lectin (EBL) (20) for sialic acid detection. Similar assay procedures as mentioned earlier were conducted to detect sera TgAb glycosylation.…”

Section: Detection Of Carbohydrate Residues On Sera Tgab By Lectin-elmentioning

confidence: 99%

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Zhao

Liu

Gao

et al. 2013

European Journal of Endocrinology

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Objective: Thyroglobulin antibody (TgAb) is an important autoantibody in thyroid diseases, which is a glycoprotein, predominantly of IgG class. Glycosylation of the IgG-Fc contributes to many effector functions exhibited by antibodies. The aim of our study was to investigate the glycosylation of sera TgAb in patients with different thyroid diseases. Design and methods: Sera from 146 patients were collected and divided into four groups: Hashimoto's thyroiditis (HT, nZ90), Graves' disease (GD, nZ20), papillary thyroid carcinoma (PTC, nZ17), and PTC with histological lymphocytic thyroiditis (PTC-T, nZ19). HT patients were further divided into euthyroidism and subclinical and overt hypothyroidism groups. Lectin-ELISAs were performed to detect the relative amount of core fucose, terminal galactose, and sialic acid on each TgAb respectively. Results: Among HT, GD, and PTC groups, HT patients had significantly lower core fucose content on TgAb than the other two groups; an increasing trend of sialylation was found in PTC sera (PZ0.076) compared with HT groups. PTC-T patients had significantly higher sialylated TgAb than HT and GD patients, and no significant difference was found between PTC and PTC-T. There was no significant difference in the three carbohydrate residue contents on sera TgAb among HT subgroups. In all the patients, negative correlation was found between sialic acid content and TgAb IgG levels (rZK0.736, P!0.001). Conclusions: Our study showed that glycosylation of sera TgAb varied in different thyroid diseases and it might be involved in pathogenesis of thyroid disorders.

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“…used Sambucus nigra agglutinin and Maackia amurensis agglutinin lectin materials to identify the levels of α‐2,6 and α‐2,3 linkage of sialic acids associated with AFP . Elevated levels of α‐2,6 linked sialic acid expression in AFP was observed in patients with hepatitis B cirrhosis while elevated levels of α‐2,3 linked sialic acids in AFP was observed in patients with hepatitis C cirrhosis, respectively . Thus, it is rational to assume that the profiling of isomeric glycan structure of haptoglobin might effectively discriminate between cirrhosis and HCC.…”

Section: Introductionmentioning

confidence: 99%

LC‐MS/MS isomeric profiling of permethylated N‐glycans derived from serum haptoglobin of hepatocellular carcinoma (HCC) and cirrhotic patients

et al. 2017

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Early stage detection and cancer treatment demand the identification of reliable biomarkers. Over the past decades, efforts have been devoted to assess the variation of glycosylation level as well as the glycan structures of proteins in blood or serum, associated with the development and/or progression of several cancers, including liver. Herein, an LC-MS/MS-based analysis was conducted to define the glycosylation patterns of haptoglobin glycoprotein derived from sera collected from cirrhotic and hepatocellular carcinoma (HCC) patients. The haptoglobin samples were extracted from serum using an antibody-immobilized column prior to the release of N-glycans. A comparison of non-isomeric and isomeric permethylated glycan forms was achieved using C18 and porous graphitic carbon (PGC) columns, respectively. In the case of C18-LC-MS/MS analysis, 25 glycan structures were identified of which 10 sialylated structures were found to be statistically significant between the two cohorts. Also, 8 out of 34 glycan structures identified by PGC-LC-MS/MS were found to be statistically significant, suggesting that isomeric distributions of a particular glycan composition were different in abundances between the two cohorts. The glycan isoform patterns distinguished early stage HCC from cirrhotic patients. Both retention times and tandem mass spectra were utilized to determine the specific isomeric glycan structures. All of the glycan isomers, which were statistically significant, were either branch fucosylated or composed of α-2,6 linked sialic acid moieties. The result of this study demonstrates the potential importance of isomeric separation for defining disease prompted aberrant glycan changes. The levels of several glycan isomers effectively distinguished early stage HCC from cirrhosis.

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Alterations of glycan branching and differential expression of sialic acid on alpha fetoprotein among hepatitis patients

Cited by 24 publications

References 48 publications

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Title: Human Serum/Plasma Glycoprotein Analysis by 1H-NMR, an Emerging Method of Inflammatory Assessment

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

LC‐MS/MS isomeric profiling of permethylated N‐glycans derived from serum haptoglobin of hepatocellular carcinoma (HCC) and cirrhotic patients

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