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dc.contributor.authorShen, Yanqinen_US
dc.contributor.authorKohla, Guidoen_US
dc.contributor.authorL. Lrhorfi, Aichiaen_US
dc.contributor.authorSipos, Benceen_US
dc.contributor.authorKalthoff, Holgeren_US
dc.contributor.authorJ. Gerwig, Gerriten_US
dc.contributor.authorP. Kamerling, Johannisen_US
dc.contributor.authorSchauer, Rolanden_US
dc.contributor.authorTiralongo, Joeen_US
dc.date.accessioned2017-04-24T11:32:20Z
dc.date.available2017-04-24T11:32:20Z
dc.date.issued2004en_US
dc.date.modified2009-09-01T05:59:48Z
dc.identifier.issn1742464Xen_US
dc.identifier.doi10.1046/j.1432-1033.2003.03927.xen_AU
dc.identifier.urihttp://hdl.handle.net/10072/16676
dc.description.abstractAdecrease 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.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherBlackwell Publishingen_US
dc.publisher.placeCambridge, Englanden_US
dc.publisher.urihttp://www3.interscience.wiley.com/journal/119877016/grouphome/home.htmlen_AU
dc.relation.ispartofpagefrom281en_US
dc.relation.ispartofpageto290en_US
dc.relation.ispartofjournalEuropean Journal of Biochemistryen_US
dc.relation.ispartofvolume271en_US
dc.subject.fieldofresearchcode320302en_US
dc.subject.fieldofresearchcode270108en_US
dc.titleO-Acetylation and de-O-acetylation of sialic acids in human colorectal carcinomaen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightCopyright 2004 Blackwell Publishing. The definitive version is available at www.interscience.wiley.comen_AU
gro.date.issued2004
gro.hasfulltextNo Full Text


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