Protein expression and fucosylated glycans of the serum haptoglobin-{beta} subunit in hepatitis B virus-based liver diseases.
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| 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.
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| Authors | Hong Shu, Shu Zhang, Xiaonan Kang, Shan Li, Xue Qin, Chun Sun, Haojie Lu, Yinkun Liu |
| Journal | Acta biochimica et biophysica Sinica (Acta Biochim Biophys Sin (Shanghai)) Vol. 43 Issue 7 Pg. 528-34 (Jul 2011) ISSN: 1745-7270 [Electronic] China |
| PMID | 21606158 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
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