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Matsumura, K., Higashida, K., Ishida, H., Hata, Y., Ya- mamoto, K., Shigeta, M., Mizuno-Horikawa, Y., Wang, X., Miyoshi, E., Gu, J. and Taniguchi, N. (2007) Carbo- hydrate binding specificity of a fucose-specific lectin from Aspergillus oryzae: A novel probe for core fucose. The Journal of Biological Chemistry, 282, 15700-15708. doi:10.1074/jbc.M701195200

has been cited by the following article:

• TITLE: Alteration of liver N-glycome in patients with hepatocellular carcinoma

  AUTHORS: Ling Wang, Valerie Vanhooren, Sylviane Dewaele, Xue-En Liu, Claude Libert, Feng-Min Lu, Hui Zhuang, Cuiying Chitty Chen

  KEYWORDS: N-Glycome; DSA-FACE; Fucosylation, HCC; Cirrhosis

  JOURNAL NAME: Open Journal of Gastroenterology, Vol.2 No.1, February 15, 2012

  ABSTRACT: Purpose: Alteration of liver function during pro- gression of hepatocellular carcinoma (HCC) and cirrhosis affects the serum glycoprotein pattern. In this study, the changes in the N-glycome in liver tis- sue from patients with hepatocellular carcinoma and cirrhosis caused by hepatitis B virus infection were investigated to find out the relationship between this maker and liver disease. Methods: Twenty patients, 11 with cirrhosis and 9 with hepatocellular carcinoma, and 15 healthy donors were involved in this study. Liver protein N-glycans were profiled using the DSA-FACE technique developed in our laboratory. To further analyze the fucosylation status of these liver glycans Western lectin blots of total liver proteins were performed using Aspergillus oryzae lectin (AOL) as probe, which is a carbohydrate- binding protein that recognizes specifically α-1,6-fu- cosylated glycans. Results: The N-glycome of liver proteins in patients with HBV related HCC and cirrhosis was analyzed. Compared with healthy donors, the N-glycome had significantly less (p