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Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2007 Mar 23; Vol. 282 (12), pp. 9127-42. Date of Electronic Publication: 2007 Jan 29. - Publication Year :
- 2007
-
Abstract
- The structural diversity of glycoprotein N-linked oligosaccharides is determined by the expression and regulation of glycosyltransferase activities and by the availability of the appropriate acceptor/donor substrates. Cells in different tissues and in different developmental stages utilize these control points to manifest unique glycan expression patterns in response to their surroundings. The activity of a Toll-like receptor, called Tollo/Toll-8, induces a pattern of incompletely defined, but neural specific, glycan expression in the Drosophila embryo. Understanding the full extent of the changes in glycan expression that result from altered Tollo/Toll-8 signaling requires characterization of the complete N-linked glycan profile of both wild-type and mutant embryos. N-Linked glycans harvested from wild-type or mutant embryos were subjected to direct structural analysis by analytic and preparative high pressure liquid chromatography, by multidimensional mass spectrometry, and by exoglycosidase digestion, revealing a predominance of high mannose and paucimannose glycans. Di-, mono-, and nonfucosylated forms of hybrid, complex biantennary, and triantennary glycans account for 12% of the total wild-type glycan profile. Two sialylated glycans bearing N-acetylneuraminic acid were detected, the first direct demonstration of this modification in Drosophila. Glycan profiles change during normal development consistent with increasing alpha-mannosidase II and core fucosyl-transferase enzyme activities, and with decreasing activity of the Fused lobes processing hexosaminidase. In tollo/toll-8 mutants, a dramatic, expected loss of difucosylated glycans is accompanied by unexpected decreases in monofucosylated and nonfucosylated hybrid glycans and increases in some nonfucosylated paucimannose and biantennary glycans. Therefore, tollo/toll-8 signaling influences flux through several processing steps that affect the maturation of N-linked glycans.
- Subjects :
- Animals
Animals, Genetically Modified
Drosophila melanogaster
Fucose chemistry
Mannose chemistry
Mass Spectrometry
Models, Biological
Models, Chemical
Mutation
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Time Factors
Toll-Like Receptor 8 genetics
Embryo, Nonmammalian
Gene Expression Regulation, Developmental
Polysaccharides chemistry
Toll-Like Receptor 8 physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 282
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 17264077
- Full Text :
- https://doi.org/10.1074/jbc.M606711200