Differential regulation of glycoprotein sulfation and fucosylation during growth of Dictyostelium discoideum

Tschursin, Elizabeth; Riley, George F.; Henderson, Ellen J.

doi:10.1111/j.1432-0436.1989.tb00807.x

Cited by 6 publications

(7 citation statements)

References 36 publications

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“…Previous radiolabeling data suggested that sulphation can occur on fucosylated glycans or on phosphorylated glycans in a mutually exclusive manner . This, however, is not in accordance with our new data; indeed, sulfate is present not only on PNGase F-released glycans, but also on fucosylated ones released by PNGase A.…”

Section: Discussioncontrasting

confidence: 94%

“…37 This, however, is not in accordance with our new data; indeed, sulfate is present not only on PNGase F-released glycans, but also on fucosylated ones released by PNGase A. Due to the use of the latter enzyme rather than endoglycosidase H, we also reveal, for the first time, that methylphosphorylated glycans can also carry core α1,3-fucose.…”

Section: Discussioncontrasting

confidence: 89%

“…We also found glycans with both sulfate and methylphosphate possessing maximally three acidic groups in HL241 Previous radiolabeling data suggested that sulphation can occur on fucosylated glycans or on phosphorylated glycans in a mutually exclusive manner. 37 This, however, is not in accordance with our new data; indeed, sulfate is present not only on PNGase F-released glycans, but also on fucosylated ones released by PNGase A. Due to the use of the latter enzyme rather than endoglycosidase H, we also reveal, for the first time, that methylphosphorylated glycans can also carry core α1,3-fucose.…”

Section: Anionic Modifications Of Dictyostelium N-glycanscontrasting

confidence: 89%

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Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL

et al. 2013

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The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.

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Section: Discussioncontrasting

confidence: 94%

Section: Discussioncontrasting

confidence: 89%

Section: Anionic Modifications Of Dictyostelium N-glycanscontrasting

confidence: 89%

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Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL

et al. 2013

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“…The first report of intersecting GlcNAc residues (Couso et al, 1987) was with phosphorylated glycans of vegetative axenic cells, and our results establish that it is also present on apparently unphosphorylated (Prem Das and Henderson, 1986) species during early development. It will be interesting to look for this modification in bacterially grown cells, since axenic culture causes precocious expression of aggregation stage fuco-sylation of N-linked oligosaccharides (Tschursin et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…It will be interesting to look for this modification in bacterially grown cells, since axenic culture causes precocious expression of aggregation stage fuco-sylation of N-linked oligosaccharides (Tschursin et al, 1989).…”

Section: Caps On H E X L L Glycansmentioning

confidence: 99%

Processing of neutral N‐linked oligosaccharides during early Dictyostelium discoideum development

1990

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We have used metabolic radiolabeling with oligosaccharide precursors, coupled with subcellular fractionation, to examine the distribution o f several classes o f asparagine-linked oligosaccharides during early development. In Dictyosteliurn, we have observed endoglycosidase H (endo H)-sensitive structures with sizes corresponding to 10 (HexlO) and 11 ( H e x l l ) hexose residues on the chitobiose core. Only Hexl 1 was detected as the major structure on fucosylated endo H-resistant species. All Hexl 1 species cofractionated with plasma membrane and secreted glycoproteins, whereas Hexl 0 appeared to be confined to intracellular membrane and soluble glycoproteins. Sulfated species correlated with lysosomal and secreted fractions, and glucose residues were markedly depressed in H e x l l of secreted glycoproteins. Outer branch structural studies have revealed several components of the endo H-sensitive species. Using a-mannosidase and p-hexosaminidase as diagnostic tools, species elucidated thus far are: a structure with 10 mannoses, a structure with nine mannoses and an intersecting N-acetylglucosamine, structures with three glucoses and seven or eight mannoses and several larger species with multiple blocks to digestion.

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Characterization of a cytosolic fucosylation pathway in Dictyostelium.

Gonzalez-Yanes

Cicero

Brown

et al. 1992

Journal of Biological Chemistry

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Differential regulation of glycoprotein sulfation and fucosylation during growth of Dictyostelium discoideum

Cited by 6 publications

References 36 publications

Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL

Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL

Processing of neutral N‐linked oligosaccharides during early Dictyostelium discoideum development

Characterization of a cytosolic fucosylation pathway in Dictyostelium.

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