title: Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15.
abstract: 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.
authors.affiliation: Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
authors.forename: Lamei
authors.initials: L
authors.lastname: Cheng
authors.forename: Kouichi
authors.initials: K
authors.lastname: Tachibana
authors.forename: Hiroko
authors.initials: H
authors.lastname: Iwasaki
authors.forename: Akihiko
authors.initials: A
authors.lastname: Kameyama
authors.forename: Yan
authors.initials: Y
authors.lastname: Zhang
authors.forename: Tomomi
authors.initials: T
authors.lastname: Kubota
authors.forename: Toru
authors.initials: T
authors.lastname: Hiruma
authors.forename: Kahori
authors.initials: K
authors.lastname: Tachibana
authors.forename: Takashi
authors.initials: T
authors.lastname: Kudo
authors.forename: Jian-Ming
authors.initials: JM
authors.lastname: Guo
authors.forename: Hisashi
authors.initials: H
authors.lastname: Narimatsu
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002384:Catalysis; D006031:Glycosylation; D006801:Humans; D007527:Isoenzymes; D008969:Molecular Sequence Data; D017350:N-Acetylgalactosaminyltransferases / Q000235:genetics* / Q000378:metabolism*; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D013379:Substrate Specificity; D014018:Tissue Distribution; D014158:Transcription, Genetic; D014536:Uridine Diphosphate N-Acetylgalactosamine / Q000378:metabolism; D000097763:Polypeptide N-acetylgalactosaminyltransferase
chemical_list: D007527:Isoenzymes; D017350:N-Acetylgalactosaminyltransferases; D009842:Oligopeptides; D011994:Recombinant Proteins; D014536:Uridine Diphosphate N-Acetylgalactosamine; D000097763:Polypeptide N-acetylgalactosaminyltransferase