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J Biol Chem, Vol. 273, Issue 52, 34843-34849, December 25, 1998
-1,4-GALACTOSYLTRANSFERASE IV AND
-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE
From the Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037 and § School of
Dentistry, University of Copenhagen, DK-2200 Copenhagen, Denmark
Poly-N-acetyllactosamine is a unique
carbohydrate composed of N-acetyllactosamine repeats and
provides the backbone structure for additional modifications such as
sialyl Lex. Poly-N-acetyllactosamines in
mucin-type O-glycans can be formed in core 2 branched
oligosaccharides, which are synthesized by core 2 Using a -1,6-N-acetylglucosaminyltransferase.
-1,4-galactosyltransferase (4Gal-TI) present in milk and
the recently cloned
-1,3-N-acetylglucosaminyltransferase, the formation of
poly-N-acetyllactosamine was found to be extremely inefficient starting from a core 2 branched oligosaccharide,
GlcNAc1
6(Gal13)GalNAc
R. Since the majority of
synthesized oligosaccharides contained
N-acetylglucosamine at the nonreducing ends,
galactosylation was judged to be inefficient, prompting us to test
novel members of the 4Gal-T gene family for this synthesis. Using
various synthetic acceptors and recombinant 4Gal-Ts, 4Gal-TIV was
found to be most efficient in the addition of a single galactose
residue to GlcNAc16(Gal13)GalNAcR. Moreover, 4Gal-TIV, together with
-1,3-N-acetylglucosaminyltransferase, was capable of
synthesizing poly-N-acetyllactosamine in core 2 branched
oligosaccharides. On the other hand, 4Gal-TI was found to be most
efficient for poly-N-acetyllactosamine synthesis in N-glycans. In contrast to 4Gal-TI, the efficiency of
4Gal-TIV decreased dramatically as the acceptors contained more
N-acetyllactosamine repeats, consistent with the fact that
core 2 branched O-glycans contain fewer and shorter
poly-N-acetyllactosamines than N-glycans in
many cells. These results, as a whole, indicate that 4Gal-TIV is
responsible for poly-N-acetyllactosamine synthesis in core 2 branched O-glycans.
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