Glycobiology, 2002, Vol. 12, No. 6 361-368
© 2002 Oxford University Press
Fuc-TIX: a versatile 
1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile
2 Institute of Biotechnology and Department of Biosciences, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland; 3 Division of Cell Biology, Institute of Life Science, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan; 4 Laboratory of Gene Function Analysis, Institute of Molecular and Cell Biology (IMCB), National Institutes of Advanced Industrial Science and Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan; and 5 Biomedicum and Haartman Institute, Department of Bacteriology and Immunology, University of Helsinki, P.O. Box 63, 00014 Helsinki, Finland
1,3-Fucosyltransferases (Fuc-Ts) convert N-acetyllactosamine (LN, Galß1-4GlcNAc) to Galß1-4(Fuc1-3)GlcNAc, the Lewis x (CD15, SSEA-1) epitope, which is involved in various recognition phenomena. We describe details of the acceptor specificity of 1,3-fucosyltransferase IX (Fuc-TIX). The unconjugated N- and O-glycan analogs LNß1-2Man, LNß1-6Man1-OMe, LNß1-2Man1-3(LNß1-2Man1-6)Manß1-4GlcNAc, and Galß1-3(LNß1-6)GalNAc reacted well in vitro with Fuc-TIX present in lysates of appropriately transfected Namalwa cells. Fuc-TIX reacted well with the reducing end LN of GlcNAcß1-3'LN (underscored site reacted) and GlcNAcß1-3'LNß1-3'LN (both LNs reacted), but very poorly with the reducing end LN of LNß1-3'LN. However, Fuc-TIX reacted significantly better with the non-reducing end LN as compared to the other LN units in the glycans LNß1-3'LN and LNß1-3'LNß1-3'LNß1-3'LN, confirming our previous data on LNß1-3'LNß1-OR. In contrast, the sialylated glycan Neu5Ac2-3'LNß1-3'LNß1-3'LNß1-3'LN was fucosylated preferentially at the two most reducing end LN units. We conclude that Fuc-TIX is a versatile 1,3-Fuc-T, that (1) generates distal Lewis x epitopes from many different acceptors, (2) possesses inherent ability for the biosynthesis of internal Lewis x epitopes on growing polylactosamine backbones, and (3) fucosylates the remote internal LN units of 2,3-sialylated i-type polylactosamines.
1 To whom correspondence should be addressed; E-mail: risto.renkonen{at}helsinki.fi
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  V. Bogoevska, A. Horst, B. Klampe, L. Lucka, C. Wagener, and P. Nollau CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues Glycobiology, March 1, 2006; 16(3): 197 - 209. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. S. Kawar, S. M. Haslam, H. R. Morris, A. Dell, and R. D. Cummings Novel Poly-GalNAc{beta}1-4GlcNAc (LacdiNAc) and Fucosylated Poly-LacdiNAc N-Glycans from Mammalian Cells Expressing {beta}1,4-N-Acetylgalactosaminyltransferase and {alpha}1,3-Fucosyltransferase J. Biol. Chem., April 1, 2005; 280(13): 12810 - 12819. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. K. Patnaik, B. Potvin, and P. Stanley LEC12 and LEC29 Gain-of-Function Chinese Hamster Ovary Mutants Reveal Mechanisms for Regulating VIM-2 Antigen Synthesis and E-selectin Binding J. Biol. Chem., November 26, 2004; 279(48): 49716 - 49726. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Kudo, M. Kaneko, H. Iwasaki, A. Togayachi, S. Nishihara, K. Abe, and H. Narimatsu Normal Embryonic and Germ Cell Development in Mice Lacking {alpha}1,3-Fucosyltransferase IX (Fut9) Which Show Disappearance of Stage-Specific Embryonic Antigen 1 Mol. Cell. Biol., May 15, 2004; 24(10): 4221 - 4228. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Maki and R. Renkonen Biosynthesis of 6-deoxyhexose glycans in bacteria Glycobiology, March 1, 2004; 14(3): 1R - 15R. [Abstract] [Full Text] [PDF]
|
|