Alteration in N-acetylglucosaminyltransferase activities and glycan structure in tissue and bile glycoproteins from extrahepatic bile duct carcinoma |
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Authors: | Xiao-ling Jin Hou-bao Liu Ying Zhang Bing-sheng Wang Hui-Li Chen |
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Affiliation: | (1) Department of General Surgery, Zhong-Shan Hospital, Fu-Dan University, China;(2) Key Laboratory of Glycoconjugate Research, Ministry of Health, Department of Biochemistry, Shanghai Medical College, Fu-Dan University, China |
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Abstract: | The activities of three N-acetylglucosaminyltransferases (GnT)-III, IV and V, as well as the structural alterations of N-glycans on the glycoproteins
in cancer tissues and bile specimens from 28 cases of extrahepatic bile duct carcinoma (EBDC) were compared with those from
18 cases of benign biliary duct diseases (BBDD). GnT activities were determined with fluorescence-labeled substrate using
a HPLC method. It was found that GnT-III and GnT-V activities in EBDC were increased to 3.14 and 15.96 times respectively
of the mean BBDD values, but GnT-IV remained unchanged. The activity of GnT-V was correlated with the grade of differentiation
and TMN stage of EBDC. The up-regulation of GnT-III resulted in the increased bisecting-GlcNAc on the N-glycans of glycoproteins
in cancer tissues and a 201 kDa bile glycoprotein when analyzed with HRP-labeled E4-PHA. The increased GnT-V activity led to the elevation of the β1,6GlcNAc branch (or antennary number) on the N-glycans in
cancer tissue glycoproteins and 201, 163, 122 kDa proteins in the bile as probed with HRP-labeled DSA. These findings suggest
that the alteration in GnT activities may be involved in the malignant transformation and development of EBDC, resulting in
the aberrant glycosylation of some tissue and bile proteins. The latter was expected to be used in the clinical diagnosis
and prognosis evaluation in EBDC patients. Published in 2004.
This revised version was published online in July 2006 with corrections to the Cover Date. |
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Keywords: | extrahepatic bile duct carcinoma (EBDC) N-acetylglucosaminyltransferase (GnT) asparagine-linked glycan (N-glycan) bile glycoprotein lectin |
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