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A preliminary evaluation of the differences in the glycosylation of alpha-1-acid glycoprotein between individual liver diseases

During the acute phase response (APR) to tissue injury or infection, the liver is responsible for the level of mediators such as cytokines required at the site of inflammation and providing the essential components for wound healing and tissue repair. Additionally there are substantial alterations i...

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Published in:Biomedical chromatography 2002-09, Vol.16 (6), p.365-372
Main Authors: Anderson, Nicola, Pollacchi, Aileen, Hayes, Peter, Therapondos, George, Newsome, Philip, Boyter, Anne, Smith, Kevin
Format: Article
Language:English
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Summary:During the acute phase response (APR) to tissue injury or infection, the liver is responsible for the level of mediators such as cytokines required at the site of inflammation and providing the essential components for wound healing and tissue repair. Additionally there are substantial alterations in the expression of plasma proteins of hepatic origin such as alpha‐1‐acid glycoprotein (AGP). The APR also results in alterations to the branching, sialylation and fucosylation of the oligosaccharide chains of AGP. This study investigated whether liver damage could be correlated with changes in AGP glycosylation in groups of patients with various liver diseases (alcoholic liver disease, hepatitis B, hepatitis C, cirrhosis). Hyperfucosylation occurred in all cases of liver disease, although the hepatitis B and C samples showed a more significant increase in comparison with the others. Additionally N‐acetylgalactosamine (GalNAc) was detected in the majority of the hepatitis C samples, which was unexpected since this monosaccharide is not a usual component of the N‐linked oligosaccharide chains. It was also determined by concanavalin (con) A chromatography that there is a shift towards the increased branching of the oligosaccharide chains in inflammatory liver diseases compared to normal serum. Copyright © 2002 John Wiley & Sons, Ltd.
ISSN:0269-3879
1099-0801
DOI:10.1002/bmc.167