PMID- 10464263
OWN - NLM
STAT- MEDLINE
DCOM- 19991007
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 36
DP  - 1999 Sep 3
TI  - Cloning and characterization of a close homologue of human
      UDP-N-acetyl-alpha-D-galactosamine:Polypeptide
      N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic 
      but not functional redundancy.
PG  - 25362-70
AB  - The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated
      GalNAc-T3, exhibits unique functions. Specific acceptor substrates are used by
      GalNAc-T3 and not by other GalNAc-transferases. The expression pattern of
      GalNAc-T3 is restricted, and loss of expression is a characteristic feature of
      poorly differentiated pancreatic tumors. In the present study, a sixth human
      UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated GalNAc-T6,
      with high similarity to GalNAc-T3, was characterized. GalNAc-T6 exhibited high
      sequence similarity to GalNAc-T3 throughout the coding region, in contrast to the
      limited similarity that exists between homologous glycosyltransferase genes,
      which is usually restricted to the putative catalytic domain. The genomic
      organizations of GALNT3 and GALNT6 are identical with the coding regions placed
      in 10 exons, but the genes are localized differently at 2q31 and 12q13,
      respectively. Acceptor substrate specificities of GalNAc-T3 and -T6 were similar 
      and different from other GalNAc-transferases. Northern analysis revealed distinct
      expression patterns, which were confirmed by immunocytology using monoclonal
      antibodies. In contrast to GalNAc-T3, GalNAc-T6 was expressed in WI38 fibroblast 
      cells, indicating that GalNAc-T6 represents a candidate for synthesis of
      oncofetal fibronectin. The results demonstrate the existence of genetic
      redundancy of a polypeptide GalNAc-transferase that does not provide full
      functional redundancy.
FAU - Bennett, E P
AU  - Bennett EP
AD  - Faculty of Health Sciences, School of Dentistry, DK-2200 Copenhagen, Denmark.
FAU - Hassan, H
AU  - Hassan H
FAU - Mandel, U
AU  - Mandel U
FAU - Hollingsworth, M A
AU  - Hollingsworth MA
FAU - Akisawa, N
AU  - Akisawa N
FAU - Ikematsu, Y
AU  - Ikematsu Y
FAU - Merkx, G
AU  - Merkx G
FAU - van Kessel, A G
AU  - van Kessel AG
FAU - Olofsson, S
AU  - Olofsson S
FAU - Clausen, H
AU  - Clausen H
LA  - eng
SI  - GENBANK/AJ133523
SI  - GENBANK/Y08565
GR  - 1 RO1 CA66234/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
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  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.- (UDP-N-acetylgalactosamine polypeptide
      N-acetylgalactosaminyltransferase 6)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cloning, Molecular
MH  - Galactosyltransferases/*genetics/metabolism
MH  - *Genome, Human
MH  - Humans
MH  - Molecular Sequence Data
MH  - N-Acetylgalactosaminyltransferases/*genetics/metabolism
MH  - Organ Specificity
MH  - Sequence Alignment
MH  - *Sequence Homology, Amino Acid
MH  - Substrate Specificity
EDAT- 1999/08/28 00:00
MHDA- 1999/08/28 00:01
CRDT- 1999/08/28 00:00
PHST- 1999/08/28 00:00 [pubmed]
PHST- 1999/08/28 00:01 [medline]
PHST- 1999/08/28 00:00 [entrez]
AID - 10.1074/jbc.274.36.25362 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 3;274(36):25362-70. doi: 10.1074/jbc.274.36.25362.