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J Biol Chem, Vol. 274, Issue 24, 16717-16726, June 11, 1999
1,4-Galactosyltransferase I
From The Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037 and § Tokyo
Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Machida,
Tokyo 194, Japan
Poly-N-acetyllactosamine is a unique
carbohydrate that can carry various functional oligosaccharides, such
as sialyl Lewis X. It has been shown that the amount of
poly-N-acetyllactosamine is increased in
N-glycans, when they contain
Gal
1
4GlcNAc16(Gal14GlcNAc12)Man
16 branched structure. To determine how this increased synthesis of
poly-N-acetyllactosamines takes place, the branched
acceptor was incubated with a mixture of i-extension enzyme (iGnT) and 1,4galactosyltransferase I (4Gal-TI). First,
N-acetyllactosamine repeats were more readily added to
the branched acceptor than the summation of
poly-N-acetyllactosamines formed individually on each
unbranched acceptor. Surprisingly,
poly-N-acetyllactosamine was more efficiently formed on
Gal14GlcNAc12ManR side chain than in
Gal14GlcNAc16ManR, due to preferential action of iGnT
on Gal14GlcNAc12ManR side chain. On the other hand, galactosylation was much more efficient on 1,6-linked GlcNAc than
1,2-linked GlcNAc, preferentially forming
Gal14GlcNAc16(GlcNAc12)Man16Man R.
Starting with this preformed acceptor,
N-acetyllactosamine repeats were added almost equally
to Gal14GlcNAc16ManR and Gal14GlcNAc12ManR side chains. Taken together, these
results indicate that the complemental branch specificity of iGnT
and 4Gal-TI leads to efficient and equal addition of
N-acetyllactosamine repeats on both side chains of
GlcNAc16(GlcNAc12)Man16ManR structure,
which is consistent with the structures found in nature. The results
also suggest that the addition of Gal14GlcNAc16 side chain
on Gal14GlcNAc12ManR side chain converts the acceptor to
one that is much more favorable for iGnT and 4Gal-TI.
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