Regulation of sialic acid O-acetylation in human colon mucosa

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Title Regulation of sialic acid O-acetylation in human colon mucosa
Author Shen, Yanqin; Tiralongo, Giuseppe; Kohla, Guido; Schauer, Roland
Journal Name Biological Chemistry
Year Published 2004
Place of publication Germany
Publisher Walter de Gruyter
Abstract The expression of O-acetylated sialic acids in human colonic mucins is developmentally regulated, and a reduction of O-acetylation has been found to be associated with the early stages of colorectal cancer. Despite this, however, little is known about the enzymatic process of sialic acid O-acetylation in human colonic mucosa. Recently, we have reported on a human colon sialate 7(9)-O-acetyltransferase capable of incorporating acetyl groups into sialic acids at the nucleotidesugar level [Shen et al., Biol. Chem. 383 (2002), 307317]. In this report, we show that the CMP-N-acetyl-neuraminic acid (CMPNeu5Ac) and acetyl-CoA (AcCoA) transporters are critical components for the O-acetylation of CMPNeu5Ac in Golgi lumen, with specific inhibition of either transporter leading to a reduction in the formation of CMP-5-Nacetyl-9-O-acetylneuraminic acid (CMP-Neu5,9Ac2). Moreover, the finding that 5-Nacetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) could be transferred from neo-synthesised CMP-Neu5,9Ac2 to endogenous glycoproteins in the same Golgi vesicles, together with the observation that asialofetuin and asialo-human colon mucin are much better acceptors for Neu5,9Ac2 than asialo-bovine submandibular gland mucin, suggests that a sialyltransferase exists that preferentially utilises CMPNeu5,9Ac2 as the donor substrate, transferring Neu5,9Ac2 to terminal Galβ1,3(4)R- residues.
Peer Reviewed Yes
Published Yes
Publisher URI http://www.reference-global.com/loi/bchm
Alternative URI http://dx.doi.org/10.1515/BC.2004.033
Volume 385
Issue Number 2
Page from 145
Page to 152
ISSN 1431-6730
Date Accessioned 2006-07-28
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Enzymes; PRE2009-Medical Biochemistry: Carbohydrates
URI http://hdl.handle.net/10072/21492
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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