N-glycopeptide signatures of IgA2  in serum from patients with hepatitis B virus-related liver diseases.

N-glycopeptide signatures of IgA2 in serum from patients with hepatitis B virus-related liver diseases. Mol Cell Proteomics. 2019 Sep 09;: Authors: Zhang S, Cao X, Liu C, Li W, Zeng W, Li B, Chi H, Liu M, Qin X, Tang L, Yan G, Ge Z, Liu Y, Gao Q, Lu H Abstract N-glycosylation alteration has been reported in liver diseases. Characterizing N-glycopeptides that correspond to N-glycan structure with specific site information enable better understanding of the molecular pathogenesis of liver damage and cancer. Here, unbiased quantification of N-glycopeptides of a cluster of serum glycoproteins with 40-55 kDa molecular weight (40 kDa-band) was investigated in hepatitis B virus (HBV)-related liver diseases. We used a N-glycopeptide method based on 18O/16O C-terminal labelling to obtain 82 comparisons of serum from patients with HBV-related hepatocellular carcinoma (HCC) and liver cirrhosis (LC). Then, Multiple Reaction Monitoring (MRM) was performed to quantify N-glycopeptide relative to the protein content, especially in healthy donor-HBV-LC-HCC cascade. TPLTAN 205ITK (H5N5S1F1) and (H5N4S2F1) corresponding to the glycopeptides of IgA2 were significantly elevated in serum from patients with HBV infection and even higher in HBV-related LC patients, as compared with healthy donor. In contrast, the two glycopeptides of IgA2 fell back down in HBV-related HCC patients. In addition, the variation in the abundance of two glycopeptides was...
Source: Molecular and Cellular Proteomics : MCP - Category: Molecular Biology Authors: Tags: Mol Cell Proteomics Source Type: research