N-glycopeptide Signatures of IgA2 in Serum from Patients with Hepatitis B Virus-related Liver Diseases

Zhang, Shu; Cao, Xinyi; Liu, Chao; Li, Wei; Zeng, Wenfeng; Li, Baiwen; Chi, Hao; Liu, Mingqi; Qin, Xue; Tang, Lingyi; Yan, Guoquan; Ge, Zefan; Liu, Yinkun; Gao, Qiang; Lu, Haojie

doi:10.1074/mcp.ra119.001722

Cited by 29 publications

(30 citation statements)

References 53 publications

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“…In our previous study, N-glycopeptides of 40-55 kDa band in LC and HCC were quantified. TPLTAN 205 ITK (H5N4S2F1) and (H5N5S1F1) of IgA 2 were changed significantly during the development of HCC (22).…”

Section: Introductionmentioning

confidence: 95%

“…The mixture was loaded onto the trap column (2 cm × 100 µm, PepMap C18) and the analytical column (25 cm × 75 µm, PepMap C18) by using a gradient of 1 to 25% solvent B in 60 min, followed by an increase to 45% B in 20 min. Parameters used for MS data acquisition were as described (22). The intact glycopeptides were identified by pGlyco (http://pfind.ict.ac.cn/software/pGlyco/index.html) (Version 2020.05.27) and quantified by pQuant (22,30).…”

Section: Mass Spectrometry Analysismentioning

confidence: 99%

“…Parameters used for MS data acquisition were as described (22). The intact glycopeptides were identified by pGlyco (http://pfind.ict.ac.cn/software/pGlyco/index.html) (Version 2020.05.27) and quantified by pQuant (22,30).…”

Section: Mass Spectrometry Analysismentioning

confidence: 99%

“…16 Oand 18 O-labeled digests were pooled by equal volumes before mass spectrometry analysis. The 16 O/ 18 O labeled Nglycopeptides were identified and quantified according to a previous study (22).…”

Section: O/ 18 O Labeling Of Glycopeptidesmentioning

confidence: 99%

“…It has been reported that the trifucosylated tetra-antennary glycan structure of AGP could distinguish HCC from cirrhosis. There are increasing pieces of evidence that glycosylation changes of serum proteins are closely related to cancer progression (20)(21)(22). Unique alterations of tumor-associated N-glycosylation have several inherent advantages, such as providing distinct biomarkers indicating significant and amplified changes (23).…”

Section: Introductionmentioning

confidence: 99%

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Analysis of Serum Paraoxonase 1 Using Mass Spectrometry and Lectin Immunoassay in Patients With Alpha-Fetoprotein Negative Hepatocellular Carcinoma

Cao

Shao

et al. 2021

Front. Oncol.

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The diagnosis of AFP (alpha-fetoprotein)-negative HCC (hepatocellular carcinoma) mostly relies on imaging and pathological examinations, and it lacks valuable and practical markers. Protein N-glycosylation is a crucial post-translation modifying process related to many biological functions in an organism. Alteration of N-glycosylation correlates with inflammatory diseases and infectious diseases including hepatocellular carcinoma. Here, serum N-linked intact glycopeptides with molecular weight (MW) of 40–55 kDa were analyzed in a discovery set (n = 40) including AFP-negative HCC and liver cirrhosis (LC) patients using label-free quantification methodology. Quantitative lens culinaris agglutin (LCA) ELISA was further used to confirm the difference of glycosylation on serum PON1 in liver diseases (n = 56). Then, the alteration of site-specific intact N-glycopeptides of PON1 was comprehensively assessed by using Immunoprecipitation (IP) and mass spectrometry based 16O/18O C-terminal labeling quantification method to distinguish AFP-negative HCC from LC patients in a validation set (n = 64). Totally 195 glycopeptides were identified using a dedicated search engine pGlyco. Among them, glycopeptides from APOH, HPT/HPTR, and PON1 were significantly changed in AFP-negative HCC as compared to LC. In addition, the reactivity of PON1 with LCA in HCC patients with negative AFP was significantly elevated than that in cirrhosis patients. The two glycopeptides HAN253WTLTPLK (H5N4S2) and (H5N4S1) corresponding to PON1 were significantly increased in AFP-negative HCC patients, as compared with LC patients. Variations in PON1 glycosylation may be associated with AFP-negative HCC and might be helpful to serve as potential glycomic-based biomarkers to distinguish AFP-negative HCC from cirrhosis.

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Section: Introductionmentioning

confidence: 95%

Section: Mass Spectrometry Analysismentioning

confidence: 99%

Section: Mass Spectrometry Analysismentioning

confidence: 99%

Section: O/ 18 O Labeling Of Glycopeptidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Analysis of Serum Paraoxonase 1 Using Mass Spectrometry and Lectin Immunoassay in Patients With Alpha-Fetoprotein Negative Hepatocellular Carcinoma

Cao

Shao

et al. 2021

Front. Oncol.

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Methods for quantification of glycopeptides by liquid separation and mass spectrometry

Yin

Zhu

2022

Mass Spectrometry Reviews

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Recent advances in analytical techniques provide the opportunity to quantify even low‐abundance glycopeptides derived from complex biological mixtures, allowing for the identification of glycosylation differences between healthy samples and those derived from disease states. Herein, we discuss the sample preparation procedures and the mass spectrometry (MS) strategies that have facilitated glycopeptide quantification, as well as the standards used for glycopeptide quantification. For sample preparation, various glycopeptide enrichment methods are summarized including the columns used for glycopeptide separation in liquid chromatography separation. For MS analysis strategies, MS1 level‐based quantification and MS2 level‐based quantification are described, either with or without labeling, where we have covered isotope labeling, TMT/iTRAQ labeling, data dependent acquisition, data independent acquisition, multiple reaction monitoring, and parallel reaction monitoring. The strengths and weaknesses of these methods are compared, particularly those associated with the figures of merit that are important for clinical biomarker studies and the pathological and functional studies of glycoproteins in various diseases. Possible future developments for glycopeptide quantification are discussed.

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Histomolecular characterisation of hepatitis B virus induced liver cancer

Adugna

2023

Reviews in Medical Virology

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Hepatitis B virus (HBV)‐associated liver cancer is the third most prevalent cancer‐related cause of death worldwide. Different studies have been done on the histomolecular analysis of HBV induced‐liver cancer including epigenetics which are dynamic molecular mechanisms to control gene expression without altering the host deoxyribonucleic acid, genomics characterise the integration of the viral genome with host genome, proteomics characterise how gene modifies and results overexpression of proteins, glycoproteomics discover different glyco‐biomarker candidates and show glycosylation in malignant hepatocytes, metabolomics characterise how HBV impairs a variety of metabolic functions during hepatocyte immortalisation, exosomes characterise immortalised liver cells in terms of their differentiation and proliferation, and autophagy plays a role in the development of hepatocarcinogenesis linked to HBV infection.

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N-glycopeptide Signatures of IgA2 in Serum from Patients with Hepatitis B Virus-related Liver Diseases

Cited by 29 publications

References 53 publications

Analysis of Serum Paraoxonase 1 Using Mass Spectrometry and Lectin Immunoassay in Patients With Alpha-Fetoprotein Negative Hepatocellular Carcinoma

Analysis of Serum Paraoxonase 1 Using Mass Spectrometry and Lectin Immunoassay in Patients With Alpha-Fetoprotein Negative Hepatocellular Carcinoma

Methods for quantification of glycopeptides by liquid separation and mass spectrometry

Histomolecular characterisation of hepatitis B virus induced liver cancer

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