Glycobiology Advance Access published online on May 25, 2005
Glycobiology, doi:10.1093/glycob/cwi081
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Department of Experimental Medicine and Center of Excellence for Biomedical Research, University of Genova, Viale Benedetto XV, 1, 16132, Genova, Italy
* To whom correspondence should be addressed. LAD II/CDG IIc is a genetic disease characterized by a decreased expression of fucose in glycoconjugates, resulting in leukocyte adhesion deficiency and severe morphological and neurological abnormalities. The biochemical defect is a reduced transport of GDP-L-fucose from cytosol into the Golgi compartment, which reduces its availability as substrate for fucosyltransferases. The aim of the present study was to determine the effects of a limited supply of GDP-L-fucose inside the Golgi on core fucosylation (
Received December 28, 2004
Revised May 17, 2005
Accepted May 19, 2005
Article
Core fucosylation of N-linked glycans in Leukocyte Adhesion Deficiency/Congenital Disorder of Glycosylation IIc (LAD II/CDG IIc) fibroblasts
2 Department of Biochemistry, the 21st COE program, Osaka University, Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan
3 Department of Internal Medicine, University of Genova, Viale Benedetto XV, 6, 16132, Genova, Italy
Michela Tonetti, E-mail: tonetti{at}unige.it
Abstract 
1,6-fucose linked to core N-acetylglucosamine) of N-linked glycans in LAD II fibroblasts. The results showed that, although [3H]fucose incorporation was generally reduced in LAD II cells, core fucosylation was affected to a greater extent compared to other types of fucosylation of N-linked oligosaccharides. In particular, core fucosylation was found to be nearly absent in biantennary negatively charged oligosaccharides, while other types of structures, in particular triantennary neutral species, were less affected by the reduction. Expression and activity of 1,6-fucosyltransferase in control and LAD II fibroblasts were comparable, thus excluding the possibility of a decreased activity of the transferase. The data obtained confirm that the concentration of GDP-L-fucose inside the Golgi can differentially affect the various types of fucosylation in vivo and also indicate that core fucosylation is not dependent only on the availability of GDP-L-fucose, but it is significantly influenced by the type of oligosaccharide structure. The relevant reduction in core fucosylation observed in some species of oligosaccharides could also provide clues for the identification of glycans involved in the severe developmental abnormalities observed in LAD II.1,6-fucosyltransferase/fibroblasts.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  Y. Zhao, S. Itoh, X. Wang, T. Isaji, E. Miyoshi, Y. Kariya, K. Miyazaki, N. Kawasaki, N. Taniguchi, and J. Gu Deletion of Core Fucosylation on {alpha}3beta1 Integrin Down-regulates Its Functions J. Biol. Chem., December 15, 2006; 281(50): 38343 - 38350. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Ma, J. L. Simala-Grant, and D. E. Taylor Fucosylation in prokaryotes and eukaryotes Glycobiology, December 1, 2006; 16(12): 158R - 184R. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Luo, K. Koles, W. Vorndam, R. S. Haltiwanger, and V. M. Panin Protein O-Fucosyltransferase 2 Adds O-Fucose to Thrombospondin Type 1 Repeats J. Biol. Chem., April 7, 2006; 281(14): 9393 - 9399. [Abstract] [Full Text] [PDF]
|
|