Journal
ACTA BIOCHIMICA ET BIOPHYSICA SINICA
Volume 43, Issue 7, Pages 528-534Publisher
OXFORD UNIV PRESS
DOI: 10.1093/abbs/gmr038
Keywords
glycosylation; glycan analysis; liver disease
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Funding
- National High-Tech Research and Development Program of China [2006AA02A308]
- National Key Projects for Infectious Disease of China [2008ZX10002-021, 2008ZX10002-017]
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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-beta subunit (Hp-beta) 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-beta glycan level was proportional to the protein level. Multilectin blot, high-performance liquid chromatography (HPLC), and western blot analysis were carried out to identify the glycoform of Hp-beta quantitatively. Our experiments showed that the ratio of total serum Hp-beta to the glycosylated form of Hp-beta varied among the patients with different liver diseases. The total Hp-beta protein expression level was much higher in HCC than LC, while an incremental proportion of fucosylated Hp-beta 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 antihuman Sialyl-Lewis X antibody. In conclusion, the aberrant alternation of Hp-beta glycan and total protein expression may be a promising biomarker for early hepatocarcinogenesis.
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