Journal
FEBS LETTERS
Volume 566, Issue 1-3, Pages 17-24Publisher
WILEY
DOI: 10.1016/j.febslet.2004.03.108
Keywords
UDP-GaINAc : polypeptide; N-acetylgalactosaminyltransferase (EC 2.4.1.41); O-glycosylation; O-glycan; mucin
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We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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