Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 300, Issue 3, Pages 738-744Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0006-291X(02)02908-X
Keywords
glycosyltransferase; polypeptide N-acetylgalactosaminyltransferase; O-glycosylation; O-glycan; mucin
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A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motif's that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. Quantitative real time PCR analysis revealed significantly high expression of the pp-GalNAc-T14 transcript in kidney, although the transcripts were ubiquitously expressed in all tissues examined. Furthermore, the recombinant pp-GalNAc-T14 transferred GalNAc to a panel of mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney. (C) 2002 Elsevier Science (USA). All rights reserved.
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