Sökning: onr:"swepub:oai:gup.ub.gu.se/328396" >
N-glycan antennal m...
N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase
-
Paschinger, K. (författare)
-
Wols, F. (författare)
-
Yan, S. (författare)
-
visa fler...
-
- Jin, Chunsheng (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi,Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
-
Vanbeselaere, J. (författare)
-
Dutkiewicz, Z. (författare)
-
Arcalis, E. (författare)
-
Malzl, D. (författare)
-
Wilson, I. B. H. (författare)
-
visa färre...
-
(creator_code:org_t)
- Elsevier BV, 2023
- 2023
- Engelska.
-
Ingår i: Journal of Biological Chemistry. - : Elsevier BV. - 0021-9258. ; 299:4
- Relaterad länk:
-
https://gup.ub.gu.se...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Simple organisms are often considered to have simple gly-comes, but plentiful paucimannosidic and oligomannosidic glycans overshadow the less abundant N-glycans with highly variable core and antennal modifications; Caenorhabditis ele-gans is no exception. By use of optimized fractionation and assessing wildtype in comparison to mutant strains lacking either the HEX-4 or HEX-5 beta-N-acetylgalactosaminidases, we conclude that the model nematode has a total N-glycomic po-tential of 300 verified isomers. Three pools of glycans were analyzed for each strain: either PNGase F released and eluted from a reversed-phase C18 resin with either water or 15% methanol or PNGase Ar released. While the water-eluted frac-tions were dominated by typical paucimannosidic and oligo-mannosidic glycans and the PNGase Ar-released pools by glycans with various core modifications, the methanol-eluted fractions contained a huge range of phosphorylcholine-modified structures with up to three antennae, sometimes with four N-acetylhexosamine residues in series. There were no major differences between the C. elegans wildtype and hex-5 mutant strains, but the hex-4 mutant strains displayed altered sets of methanol-eluted and PNGase Ar-released pools. In keeping with the specificity of HEX-4, there were more glycans capped with N-acetylgalactosamine in the hex-4 mutants, as compared with isomeric chito-oligomer motifs in the wildtype. Considering that fluorescence microscopy showed that a HEX-4::enhanced GFP fusion protein colocalizes with a Golgi tracker, we conclude that HEX-4 plays a significant role in late-stage Golgi processing of N-glycans in C. elegans. Furthermore, finding more "parasite-like" structures in the model worm may facilitate discovery of glycan-processing enzymes occurring in other nematodes.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- linked oligosaccharides
- molecular-cloning
- o-glycans
- wild-type
- core
- identification
- protein
- alpha
- cells
- acid
- Biochemistry & Molecular Biology
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas