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Originally published In Press as doi:10.1074/jbc.M001034200 on March 19, 2000

J. Biol. Chem., Vol. 275, Issue 21, 15868-15875, May 26, 2000
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Poly-N-acetyllactosamine Extension in N-Glycans and Core 2- and Core 4-branched O-Glycans Is Differentially Controlled by i-Extension Enzyme and Different Members of the beta 1,4-Galactosyltransferase Gene Family*

Minoru UjitaDagger , Anup K. Misra, Joseph McAuliffe, Ole Hindsgaul, and Minoru Fukuda§

From the Glycobiology Program, Cancer Research Center, the Burnham Institute, La Jolla, California 92037

Poly-N-acetyllactosamines are attached to N-glycans, O-glycans, and glycolipids and serve as underlying glycans that provide functional oligosaccharides such as sialyl LewisX. Poly-N-acetyllactosaminyl repeats are synthesized by the alternate addition of beta 1,3-linked GlcNAc and beta 1,4-linked Gal by i-extension enzyme (iGnT) and a member of the beta 1,4-galactosyltransferase (beta 4Gal-T) gene family. In the present study, we first found that poly-N-acetyllactosamines in N-glycans are most efficiently synthesized by beta 4Gal-TI and iGnT. We also found that iGnT acts less efficiently on acceptors containing increasing numbers of N-acetyllactosamine repeats, in contrast to beta 4Gal-TI, which exhibits no significant change. In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was found to be synthesized most efficiently by iGnT and beta 4Gal-TI, in contrast to core 2 branch synthesis, which requires iGnT and beta 4Gal-TIV. Poly-N-acetyllactosamine extension of core 4 branches is, however, less efficient than that of N-glycans or core 2 branches. Such inefficiency is apparently due to competition between a donor substrate and acceptor in both galactosylation and N-acetylglucosaminylation, since a core 4-branched acceptor contains both Gal and GlcNAc terminals. These results, taken together, indicate that poly-N-acetyllactosamine synthesis in N-glycans and core 2- and core 4-branched O-glycans is achieved by iGnT and distinct members of the beta 4Gal-T gene family. The results also exemplify intricate interactions between acceptors and specific glycosyltransferases, which play important roles in how poly-N-acetyllactosamines are synthesized in different acceptor molecules.

* This work was supported by NCI, National Institutes of Health, Grants R37 CA33000, R01 CA48737, and P01 CA71932.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a Toyobo Biotechnology fellowship. Present address: The Agricultural High-Tech Research Center, Meijo University, Nagoya 468-8502, Japan.

§ To whom correspondence should be addressed: The Burnham Institute, 10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-646-3144; Fax: 858-646-3193; E-mail: minoru@burnham-inst.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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