Regulation of sialic acid O-acetylation in human colon mucosa
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| 024 | 7 | 0 | |a 10.1515/BC.2004.033 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.033 | ||
| 245 | 0 | 0 | |a Regulation of sialic acid O-acetylation in human colon mucosa |h [Elektronische Daten] |c [Y. Shen, J. Tiralongo, G. Kohla, R. Schauer] |
| 520 | 3 | |a 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. | |
| 540 | |a Copyright © 2004 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Shen |D Y. |4 aut | |
| 700 | 1 | |a Tiralongo |D J. |4 aut | |
| 700 | 1 | |a Kohla |D G. |4 aut | |
| 700 | 1 | |a Schauer |D R. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 385/2(2004-02-05), 145-152 |x 1431-6730 |q 385:2<145 |1 2004 |2 385 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2004.033 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2004.033 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Shen |D Y. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tiralongo |D J. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kohla |D G. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Schauer |D R. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 385/2(2004-02-05), 145-152 |x 1431-6730 |q 385:2<145 |1 2004 |2 385 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||