Modification of Epidermal Growth Factor-like Repeats withO-Fucose

Wang, Yang; Shao, Li; Shi, Shaolin; Harris, Reed J.; Spellman, Michael W.; Stanley, Pamela; Haltiwanger, Robert S.

doi:10.1074/jbc.m107849200

Cited by 220 publications

(95 citation statements)

References 34 publications

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“…2 Since total levels of the disaccharide Glc-␤1,3-Fuc-O(S/T), which is characteristic of TSRs (10,29) A potential explanation for the difference between addition of terminal fucose and O-fucosylation could rely in a different affinity for GDP-L-fucose, the protein fucosyltransferases having a lower K m for the nucleotide-sugar compared with the other fucosyltransferases that add fucose as terminal modification of the oligosaccharide chains. For instance, O-FucT-1, which modify EGF repeats, has a K m for GDP-L-fucose of ϳ5 M, while several fucosyltransferases involved in terminal fucosylation of N-glycans have nearly 10-fold higher K m values (43)(44). A similar phenomenon has been described in a mutant line of MDCK cells, which is severely defective for UDP-galactose transport into the lumen of Golgi vesicles (45).…”

Section: Fig 3 Elution Profiles From Sephadex G-50 Column Obtained mentioning

confidence: 51%

“…O-FucT-1, which modifies EGF repeats, has been cloned and characterized (43)(44); conversely, nothing is as yet known about the enzyme(s) responsible for fucosylation of TSRs. However, preliminary observations suggest that O-FucT-1 will not modify TSRs and that a separate enzymatic activity exists.…”

Section: Fig 3 Elution Profiles From Sephadex G-50 Column Obtained mentioning

confidence: 99%

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Differential Terminal Fucosylation of N-Linked Glycans Versus Protein O-Fucosylation in Leukocyte Adhesion Deficiency Type II (CDG IIc)

Sturla

Rampal

Haltiwanger

et al. 2003

Journal of Biological Chemistry

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LAD II/CDG IIc is a rare autosomal recessive disease characterized by a decreased expression of fucosylated antigens on cell surfaces that results in leukocyte adhesion deficiency and severe neurological and developmental abnormalities. Its molecular basis has been identified as a defect in the transporter of GDP-L-fucose into the Golgi lumen, which reduces the availability of the substrate for fucosyltransferases. During metabolic radiolabeling experiments using [ 3 H]fucose, LAD II fibroblasts incorporated significantly less radiolabel compared with control cells. However, fractionation and analysis of the different classes of glycans indicated that the decrease in [ 3 H]fucose incorporation is not generalized and is mainly confined to terminal fucosylation of N-linked oligosaccharides. In contrast, the total levels of protein O-fucosylation, including that observed in Notch protein, were unaffected. This finding demonstrates that the decrease in GDP-L-fucose levels in the fibroblast Golgi caused by the LAD II defect does not impair bulk protein O-fucosylation, but severely affects the bulk addition of fucose as a terminal modification of N-linked glycans. These data suggest that the severe clinical abnormalities including neurological and developmental ones observed in at least some of the LAD II patients may be related to alteration in recognition systems involving terminal fucose modifications of N-glycans and not be due to a defective O-fucosylation of proteins such as Notch.

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Section: Fig 3 Elution Profiles From Sephadex G-50 Column Obtained mentioning

confidence: 51%

Section: Fig 3 Elution Profiles From Sephadex G-50 Column Obtained mentioning

confidence: 99%

Differential Terminal Fucosylation of N-Linked Glycans Versus Protein O-Fucosylation in Leukocyte Adhesion Deficiency Type II (CDG IIc)

Sturla

Rampal

Haltiwanger

et al. 2003

Journal of Biological Chemistry

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“…Using this technique, we were able to find unique oligosaccharides such as poly-␤-galactose epitope which can bind to a galectin. Recent advances in the determination of rare oligosaccharide structures and in the discovery of glycosyltransferases that synthesize those rare glycans began to reveal various unique carbohydrate structures that play crucial roles in cellular communication during nonself pathogen recognition or other cellular activities (6,(73)(74)(75). Therefore, employment of FAC analysis would broaden the horizons to find such specific lectin ligands easily in the future with limited amounts of novel oligosaccharides.…”

Section: Discussionmentioning

confidence: 99%

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

Pelletier

Hashidate

Urashima

et al. 2003

Journal of Biological Chemistry

102

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Leishmania parasites are the causative agents of leishmaniasis, manifesting itself in a species-specific manner. The glycan epitopes on the parasite are suggested to be involved in the Leishmania pathogenesis. One of such established species-unique glycan structures is the poly-␤-galactosyl epitope (Gal␤1-3) n found on L. major, which can develop cutaneous infections with strong inflammatory responses. Interestingly, the polygalactosyl epitope is also suggested to be involved in the development of the parasites in its host vector, sand fly. Thus, the recognition of the galactosyl epitope by lectins expressed in host or sand fly should be implicated in the species-specific manifestations of leishmaniasis and in the parasite life cycle, respectively. We recently reported that one host ␤-galactoside-binding protein, galectin-3, can distinguish L. major from the other species through its binding to the poly-␤-galactosyl epitope, proposing a role for galectin-3 as an immunomodulator that could influence the L. major-specific immune responses in leishmaniasis. Here we report that galectin-9 can also recognize L. major by binding to the L. major-specific polygalactosyl epitope. Frontal affinity analysis with different lengths of poly-␤-galactosyllactose revealed that the galectin-9 affinity for polygalactose was enhanced in proportion to the number of Gal␤1-3 units present. Even though both galectins have comparable affinities toward the polygalactosyl epitopes, only galectin-9 can promote the interaction between L. major and macrophages, suggesting distinctive roles for the galectins in the L. major-specific development of leishmaniasis in the host.

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“…11 and 12). O-Fucosylation of EGF domains is catalyzed by the enzyme O-fucosyltransferase-1 (13,14). Loss of O-fucosyltransferase-1 activity by RNA interference with or mutation of the Drosophila Ofut1 gene (15)(16)(17) or by targeted mutation of the mouse Pofut1 gene (18) results in phenotypes that resemble those observed in the complete absence of Notch signaling.…”

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confidence: 99%

Regions of Drosophila Notch That Contribute to Ligand Binding and the Modulatory Influence of Fringe

Lei²,

Irvine

2005

Journal of Biological Chemistry

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Modification of Epidermal Growth Factor-like Repeats withO-Fucose

Cited by 220 publications

References 34 publications

Differential Terminal Fucosylation of N-Linked Glycans Versus Protein O-Fucosylation in Leukocyte Adhesion Deficiency Type II (CDG IIc)

Differential Terminal Fucosylation of N-Linked Glycans Versus Protein O-Fucosylation in Leukocyte Adhesion Deficiency Type II (CDG IIc)

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

Regions of Drosophila Notch That Contribute to Ligand Binding and the Modulatory Influence of Fringe

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