ISSN:
0192-253X
Keywords:
N-glycosylation
;
glycoprotein sorting
;
oligosaccharide processing
;
Life and Medical Sciences
;
Genetics
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Notes:
We have used metabolic radiolabeling with oligosaccharide precursors, coupled with subcellular fractionation, to examine the distribution of several classes of asparagine-linked oligosaccharides during early development. In Dictyostelium, we have observed endoglycosidase H (endo H)-sensitive structures with sizes corresponding to 10 (Hex10) and 11 (Hex11) hexose residues on the chitobiose core. Only Hex11 was detected as the major structure on fucosylated endo H-resistant species. All Hex11 species cofractionated with plasma membrane and secreted glycoproteins, whereas Hex10 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 Hex11 of secreted glycoproteins. Outer branch structural studies have revealed several components of the endo H-sensitive species. Usingα-mannosidase and β-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.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/dvg.1020110524
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