O-Acetylation and de-O-acetylation of sialic acids in human colorectal carcinoma

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Title O-Acetylation and de-O-acetylation of sialic acids in human colorectal carcinoma
Author Shen, Yanqin; Kohla, Guido; Lrhorfi, Aichia L.; Sipos, Bence; Kalthoff, Holger; Gerwig, Gerrit J.; Kamerling, Johannis P.; Schauer, Roland; Tiralongo, Giuseppe
Journal Name European Journal of Biochemistry
Year Published 2004
Place of publication Cambridge, England
Publisher Blackwell Publishing
Abstract Adecrease in the level ofO-acetylated sialic acids observed in colorectal carcinoma may lead to an increase in the expression of sialyl LewisX, a tumor-associated antigen, which is related to progression of colorectal cancer to metastasis. The underlying mechanism for this reduction is, however, not fully understood. Two enzymes are thought to be primarily responsible for the turnover of O-acetyl ester groups on sialic acids; sialate-O-acetyltransferase (OAT) and sialate-O-acetylesterase (OAE). We have previously reported the characterization of OAT activity from normal colon mucosa, which efficiently O-acetylates CMP-Neu5Ac exclusively in the Golgi apparatus prior to the action of sialyltransferase [Shen, Y., Tiralongo, J., Iwersen, M., Sipos, B., Kalthoff, H. & Schauer, R. (2002) Biol. Chem. 383, 307–317]. In this report we describe the identification of a lysosomal and a cytosolic OAE activity in human colonic mucosa that specifically hydrolyses 9-O-acetyl groups on sialic acid. Utilizingmatched resection margin and cancer tissue from colorectal carcinoma patients we provide strong evidence suggesting that the level of O-acetylated sialic acids present in normal and diseased human colon may be dependent on the relative activities of OAT to lysosomal OAE. Furthermore, we show that the level of free cytosolic Neu5,9Ac2 in human colon is regulated by the relative activity of the cytosolic OAE.
Peer Reviewed Yes
Published Yes
Publisher URI http://www3.interscience.wiley.com/journal/119877016/grouphome/home.html
Alternative URI http://dx.doi.org/10.1046/j.1432-1033.2003.03927.x
Copyright Statement Copyright 2004 Blackwell Publishing. The definitive version is available at www.interscience.wiley.com
Volume 271
Page from 281
Page to 290
ISSN 1742-464X
Date Accessioned 2006-06-29
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Enzymes; PRE2009-Medical Biochemistry: Carbohydrates
URI http://hdl.handle.net/10072/16676
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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