title: Protein expression and fucosylated glycans of the serum haptoglobin-{beta} subunit in hepatitis B virus-based liver diseases.
abstract: Glycosylation, which regulates the configuration and function of glycoproteins, is the most important post-translational modification. The aim of this study was to observe the differential patterns in glycan and protein parts of the serum haptoglobin-β subunit (Hp-β) purified from patients with hepatitis B virus (HBV) infection, liver cirrhosis (LC), or hepatocellular carcinoma (HCC). 2-D gel electrophoresis and multiplexed proteomics staining technique were employed to investigate whether the Hp-β glycan level was proportional to the protein level. Multi-lectin blot, high-performance liquid chromatography (HPLC), and western blot analysis were carried out to identify the glycoform of Hp-β quantitatively. Our experiments showed that the ratio of total serum Hp-β to the glycosylated form of Hp-β varied among the patients with different liver diseases. The total Hp-β protein expression level was much higher in HCC than LC, while an incremental proportion of fucosylated Hp-β was also observed in LC and HCC patients compared with that in HBV and healthy controls. Differential fucosylation was further identified as a Lewis X structure by HPLC and anti-human Sialyl-Lewis X antibody. In conclusion, the aberrant alternation of Hp-β glycan and total protein expression may be a promising biomarker for early hepatocarcinogenesis.
authors: Liver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai, China.
authors: Hong
authors: H
authors: Shu
authors: Shu
authors: S
authors: Zhang
authors: Xiaonan
authors: X
authors: Kang
authors: Shan
authors: S
authors: Li
authors: Xue
authors: X
authors: Qin
authors: Chun
authors: C
authors: Sun
authors: Haojie
authors: H
authors: Lu
authors: Yinkun
authors: Y
authors: Liu