![]()
|
|
||||||||
J Biol Chem, Vol. 274, Issue 14, 9296-9304, April 2, 1999
1,4-GALACTOSYLTRANSFERASE I
From the Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037 and the § School of
Dentistry, University of Copenhagen, DK-2200 Copenhagen, Denmark
I-branched poly-N-acetyllactosamine
is a unique carbohydrate composed of N-acetyllactosamine
branches attached to linear poly-N-acetyllactosamine, which
is synthesized by I-branching
1,6-N-acetylglucosaminyltransferase. I-branched
poly-N-acetyllactosamine can carry bivalent functional oligosaccharides such as sialyl Lewisx, which provide much
better carbohydrate ligands than monovalent functional
oligosaccharides. In the present study, we first demonstrate that
I-branching
1,6-N-acetylglucosaminyltransferase cloned
from human PA-1 embryonic carcinoma cells transfers
1,6-linked
GlcNAc preferentially to galactosyl residues of
N-acetyllactosamine close to nonreducing terminals. We then
demonstrate that among various
1,4-galactosyltransferases
(
4Gal-Ts),
4Gal-TI is most efficient in adding a galactose to
linear and branched poly-N-acetyllactosamines. When a
1,6-GlcNAc branched poly-N-acetyllactosamine was
incubated with a mixture of
4Gal-TI and i-extension
1,3-N-acetylglucosaminyltransferase, the major product
was the oligosaccharide with one N-acetyllactosamine extension on the linear Gal
1
4GlcNAc
1
3 side chain. Only a
minor product contained galactosylated I-branch without
N-acetyllactosamine extension. This finding was explained
by the fact that
4Gal-TI adds a galactose poorly to
1,6-GlcNAc
attached to linear poly-N-acetyllactosamines, while
1,3-N-acetylglucosaminyltransferase and
4Gal-TI
efficiently add N-acetyllactosamine to linear
poly-N-acetyllactosamines. Together, these results strongly
suggest that galactosylation of I-branch is a rate-limiting step in
I-branched poly-N-acetyllactosamine synthesis, allowing
poly-N-acetyllactosamine extension mostly along the linear
poly-N-acetyllactosamine side chain. These findings are
entirely consistent with previous findings that
poly-N-acetyllactosamines in human erythrocytes, PA-1
embryonic carcinoma cells, and rabbit erythrocytes contain multiple,
short I-branches.
This article has been cited by other articles:
![]() |
H. Korekane, T. Taguchi, Y. Sakamoto, K. Honke, N. Dohmae, H. Salminen, S. Toivonen, J. Helin, K. Takio, O. Renkonen, et al. Purification and cDNA cloning of UDP-GlcNAc:GlcNAc{beta}1-3Gal{beta}1-4Glc(NAc)-R [GlcNAc to Gal]{beta}1,6N-acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine Glycobiology, May 1, 2003; 13(5): 387 - 400. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Seko, N. Dohmae, K. Takio, and K. Yamashita beta 1,4-Galactosyltransferase (beta 4GalT)-IV Is Specific for GlcNAc 6-O-Sulfate. beta 4GalT-IV ACTS ON KERATAN SULFATE-RELATED GLYCANS AND A PRECURSOR GLYCAN OF 6-SULFOSIALYL-LEWIS X J. Biol. Chem., March 7, 2003; 278(11): 9150 - 9158. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Grabenhorst and H. S. Conradt The Cytoplasmic, Transmembrane, and Stem Regions of Glycosyltransferases Specify Their in Vivo Functional Sublocalization and Stability in the Golgi J. Biol. Chem., December 17, 1999; 274(51): 36107 - 36116. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Nakayama, J.-C. Yeh, A. K. Misra, S. Ito, T. Katsuyama, and M. Fukuda Expression cloning of a human alpha 1,4-N-acetylglucosaminyltransferase that forms GlcNAcalpha 1right-arrow4Galbeta right-arrowR, a glycan specifically expressed in the gastric gland mucous cell-type mucin PNAS, August 3, 1999; 96(16): 8991 - 8996. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Ujita, J. McAuliffe, O. Hindsgaul, K. Sasaki, M. N. Fukuda, and M. Fukuda Poly-N-acetyllactosamine Synthesis in Branched N-Glycans Is Controlled by Complemental Branch Specificity of i-Extension Enzyme and beta 1,4-Galactosyltransferase I J. Biol. Chem., June 11, 1999; 274(24): 16717 - 16726. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Ujita, A. K. Misra, J. McAuliffe, O. Hindsgaul, and M. Fukuda 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 J. Biol. Chem., May 19, 2000; 275(21): 15868 - 15875. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Shiraishi, A. Natsume, A. Togayachi, T. Endo, T. Akashima, Y. Yamada, N. Imai, S. Nakagawa, S. Koizumi, S. Sekine, et al. Identification and Characterization of Three Novel beta 1,3-N-Acetylglucosaminyltransferases Structurally Related to the beta 1,3-Galactosyltransferase Family J. Biol. Chem., January 26, 2001; 276(5): 3498 - 3507. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Lee, S. Sundaram, N. L. Shaper, T. S. Raju, and P. Stanley Chinese Hamster Ovary (CHO) Cells May Express Six beta 4-Galactosyltransferases (beta 4GalTs). CONSEQUENCES OF THE LOSS OF FUNCTIONAL beta 4GalT-1, beta 4GalT-6, OR BOTH IN CHO GLYCOSYLATION MUTANTS J. Biol. Chem., April 20, 2001; 276(17): 13924 - 13934. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |