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J Biol Chem, Vol. 274, Issue 36, 25362-25370, September 3, 1999
-D-galactosamine:Polypeptide
N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6
,,,
, and
From the 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.
Faculty of Health Sciences, School of
Dentistry, DK-2200 Copenhagen, Denmark, § Eppley Institute
for Research in Cancer and Allied Diseases, University of Nebraska
Medical Center, Omaha, Nebraska 68198, ¶ University Hospital
Nijmegen, Department of Human Genetics, 6500HB Nijmegen, The
Netherlands, and University of Gothernburg, Department of
Virology, S-413 46 Gothernburg, Sweden
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