Aspartylglucosaminidase is a lysosomal hydrolase that cleaves the bond between asparagine (Asn) and GlcNAc and is involved in the degradation of glycoproteins within lysosomes.
Mucolipidosis (ML) types II and III are caused by a deficiency of GlcNAc phosphotransferase (GNPT), which creates the mannose-6-phosphate lysosomal targeting signal, and is associated with multiple lysosomal hydrolase deficiencies.
Effects of GlcNAc
on Larval Settlement on OSE Paper and on the Inhibiting Activity of WGA
When the scientists blocked the addition of GlcNAc
to a particular protein in mice, tumor-cell growth was impaired.
Since there were ~26 mM GlcNAc
sites in the HA, a ~5 mM "saturation" in [Cu(II)] might indicate a ~20% GlcNAc
-binding by Cu(II) for a maximal effect.
In contrast to COG7- and ATP6V0A2-CDG glycomes, the percentage of triantennary glycans was not decreased, and there was no increase in ions with terminal GlcNAc
or oligomannosidic glycans.
a]; HPA, Helix pomatia agglutinin; UEA 1, Ulex europaeus I; GlcNAcT-V, UDP-GlcNAc:N-glycan GlcNAc
transferase V; MMP, matrix metalloproteinase; ADAM, a disintegrin and metalloproteinase; ECM, extracellular matrix; EGF, epidermal growth factor; EGFR, EGF receptor; T[beta]R, transforming growth factor [beta] receptor; LC-MS/MS, liquid chromatography-tandem mass spectrometry; PNGase, peptide N-glycosidase; AAL, Aleuria aurantia lectin; LCA, Lens culinaris agglutinin; LEL, Lycopersiconesulentum lectin; MRM, multiple reaction monitoring; SISCAPA, stable isotope standards and capture by antipeptide (or anticarbohydrate) antibodies; MUC1, mucin-1.
GAGs are long, unbranched polysaccharides containing a disaccharide repeat that consists of either a GalNAc or GlcNAc
residue combined with a glucuronic acid (GlcA) or a Gal residue.
432] modified by an asialocarbohydrate composed of 2 GlcNAc
and 5 Man (Table 2).
Studies on linkage analysis and allele segregation showed that there was no linkage between congenital dyserythropoietic anemia type II phenotype and the chromosomal regions containing the candidate genes that code for GlcNAc
transferase II and a-mannosidase II.
97 (a) HexA, D-hexuronic acid; GlcNAc
2]) at one glycosylation site and a single GlcNAc
at the other, one of which is fucosylated.