PMID- 10488133
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 39
DP  - 1999 Sep 24
TI  - Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
      that displays glycopeptide N-acetylgalactosaminyltransferase activity.
PG  - 27867-74
AB  - We report the cloning, expression, and characterization of a novel member of the 
      mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase)
      family that transfers GalNAc to a GalNAc-containing glycopeptide. Northern blot
      analysis revealed that the gene encoding this enzyme, termed ppGaNTase-T6, is
      expressed in a highly tissue-specific manner. Significant levels of transcript
      were found in rat and mouse sublingual gland, stomach, small intestine, and
      colon; trace amounts were seen in the ovary, cervix, and uterus. Recombinant
      constructs were expressed transiently in COS7 cells but demonstrated no
      transferase activity in vitro against a panel of unmodified peptides, including
      GTTPSPVPTTSTTSAP (MUC5AC). However, when incubated with the total glycosylated
      products obtained by action of ppGaNTase-T1 on MUC5AC (mainly
      GTT(GalNAc)PSPVPTTSTT(GalNAc)SAP), additional incorporation of GalNAc was
      achieved, resulting in new hydroxyamino acids being modified. The MUC5AC
      glycopeptide failed to serve as a substrate for ppGaNTase-T6 after modification
      of the GalNAc residues by periodate oxidation and sodium borohydride reduction,
      indicating a requirement for the presence of intact GalNAc. This suggests that
      O-glycosylation of multisite substrates may proceed in a specific hierarchical
      manner and underscores the potential complexity of the processes that regulate
      O-glycosylation.
FAU - Ten Hagen, K G
AU  - Ten Hagen KG
AD  - Center for Oral Biology, Rochester Institute of Biomedical Sciences, University
      of Rochester, Rochester, New York 14642, USA.
FAU - Tetaert, D
AU  - Tetaert D
FAU - Hagen, F K
AU  - Hagen FK
FAU - Richet, C
AU  - Richet C
FAU - Beres, T M
AU  - Beres TM
FAU - Gagnon, J
AU  - Gagnon J
FAU - Balys, M M
AU  - Balys MM
FAU - VanWuyckhuyse, B
AU  - VanWuyckhuyse B
FAU - Bedi, G S
AU  - Bedi GS
FAU - Degand, P
AU  - Degand P
FAU - Tabak, L A
AU  - Tabak LA
LA  - eng
SI  - GENBANK/AF076167
GR  - DE-08108/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Isoenzymes)
RN  - 0 (Peptides)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Consensus Sequence
MH  - Conserved Sequence
MH  - Humans
MH  - Isoenzymes/chemistry/genetics/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - N-Acetylgalactosaminyltransferases/chemistry/genetics/*metabolism
MH  - Organ Specificity
MH  - Peptides/chemistry/*metabolism
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
EDAT- 1999/09/17 00:00
MHDA- 1999/09/17 00:01
CRDT- 1999/09/17 00:00
PHST- 1999/09/17 00:00 [pubmed]
PHST- 1999/09/17 00:01 [medline]
PHST- 1999/09/17 00:00 [entrez]
AID - 10.1074/jbc.274.39.27867 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 24;274(39):27867-74. doi: 10.1074/jbc.274.39.27867.