Disease relevance of FLJ21865

• The effect of a bacteriolytic enzyme, the endo-beta-N-acetylglucosaminidase excreted by Staphylococcus aureus (SaG) on the response of human lymphocytes to mitogens and on the immune response in mice has been studied [1].
• Enhanced transglycosylation activity of Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase in media containing organic solvents [2].
• Possibly, accumulation of glycopeptides in fucosidosis urine is caused by the inability of human endo-beta-N-acetylglucosaminidase to cleave the asparagine-linked sugar chains, which have a fucose at the innermost N-acetylglucosamine residue [3].
• The influenza virus hemagglutinin is glycosylated with endo-beta-N-acetylglucosaminidase H-resistant, but not complex, oligosaccharides [4].
• The half time of acquisition of resistance to endo-beta-N-acetylglucosaminidase H was approximately 3 h for the recombinant feline infectious peritonitis virus S protein [5].

High impact information on FLJ21865

• We studied the glycosylation of the protein using endo-beta-N-acetylglucosaminidase H and peptide-N4-(N-acetyl-beta-glucosaminyl)-asparagine amidase digestion of oligosaccharide side chains of the two forms of sucrase-isomaltase [6].
• Staphylococcal endo-beta-N-acetylglucosaminidase inhibits response of human lymphocytes to mitogens and interferes with production of antibodies in mice [1].
• Only the early Mr 127,000 aminooligopeptidase was sensitive to endo-beta-N-acetylglucosaminidase H, suggesting that the larger form results from trimming of high-mannose cores and adding terminal sugars in the Golgi complex [7].
• In vivo, myeloperoxidase was labeled initially as a 85-K glycosylated polypeptide (75 K after treatment with endo-beta-N-acetylglucosaminidase H) [8].
• In HL-60 cells [32P]phosphate was incorporated into endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharides [8].

Chemical compound and disease context of FLJ21865

• Synthesis of neoglycoconjugates by transglycosylation with Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase. Demonstration of a macro-cluster effect for mannose-binding proteins [9].
• Endo-beta-N-acetylglucosaminidase H digestion of double-shelled virions identified the 41-kDa polypeptide as a glycoprotein [10].
• Digestion of asparagine-linked oligosaccharides by endo-beta-N-acetylglucosaminidase in the human skin fibroblasts obtained from fucosidosis patients [11].
• Starting from the derivatives with one complex-type carbohydrate and one GlcNAc, a high-mannose-type oligosaccharide was successfully transferred to the remaining GlcNAc using another endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae [12].
• Transfer of Man9GlcNAc to L-fucose by endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae [13].

Biological context of FLJ21865

• The purified enzyme was susceptible to hydrolysis by endo-beta-N-acetylglucosaminidase H, which resulted in at least two new forms, reduced in apparent molecular weight by approximately 4,000-6,000 [14].
• Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3) [15].
• Degradation of these apoB proteins is likely to be in the endoplasmic reticulum or ER-related compartment, as shown by sensitivity to endo beta-N-acetylglucosaminidase, by lack of an effect on the degradation kinetics by brefeldin A treatment, and by ImmunoGold EM [16].
• Mutations of endo-beta-N-acetylglucosaminidase H active site residueAs sp130 anG glu132: activities and conformations [17].
• A search of the C. elegans genome database revealed the existence of a gene exhibiting 34% identity to Mucor hiemalis (a fungus) endo-beta-N-acetylglucosaminidase (Endo-M) [18].

Anatomical context of FLJ21865

• Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol [19].
• A significant portion of the enzyme molecules synthesized was shown to be segregated into the microsomal vesicles and protected against digestion by endo-beta-N-acetylglucosaminidase, indicating that both proteolytic processing and glycosylation of the precursor polypeptide chains take place in the microsomes [20].
• These are approximately equal to 2,000 greater than the Mrs of precursor chains synthesized by intact fibroblasts and deglycosylated with endo-beta-N-acetylglucosaminidase H suggesting the presence of a signal sequence [21].
• The sensitivity of TPO2 to endo-beta-N-acetylglucosaminidase H indicated that the protein is processed through the endoplasmic reticulum and bears high mannose-type structures [22].
• These molecules were targeted to lysosomes, and their carbohydrate was trimmed to an endo-beta-N-acetylglucosaminidase H-resistant form [23].

Associations of FLJ21865 with chemical compounds

• The intracellular transport to the Golgi complex of the membrane protein VSV-G was not affected by primaquine as it acquires resistance to endo-beta-N-acetylglucosaminidase H at the same rate as in control cells [24].
• In human fibroblasts, the recognition of lysosomal enzymes by cell surface receptors is mediated by mannose 6-phosphate residues located on oligosaccharides that can be cleaved by endo-beta-N-acetylglucosaminidase H [25].
• The two allelic forms of the arylsulfatase A polypeptides were converted into a 57-kDa form by endo-beta-N-acetylglucosaminidase H, an enzyme specifically removing asparagine-linked oligosaccharides of the high-mannose (and hybrid) type [26].
• The most noticeable difference between the labeled glycopeptides from the tumor and CCL 239 cells was the presence in the former of an endo-beta-N-acetylglucosaminidase H-resistant high molecular weight glycopeptide fraction which was eluted in the void volume of Bio-Gel P-6 [27].
• This glycoprotein was resistant to endo-beta-N-acetylglucosaminidase H treatment suggesting a complex-type carbohydrate structure [28].

Other interactions of FLJ21865

• At this time, MUC2 immunoprecipitated by anti-MUC2 was completely oligomerized and was endo-beta-N-acetylglucosaminidase-resistant, indicating that the mucin had reached the Golgi region [29].
• Controlled deglycosylation using peptide : N-glycosidase F and endo-beta-N-acetylglucosaminidase F3 resulted in the formation of crystals of both hIL-10 : shIL-10R1 and vIL-10 : shIL-10R1 complexes, indicating that the difficulty in the crystal formation was largely due to the presence of complex carbohydrate side chains [30].
• Treatment of the active high mannose receptor with endo-beta-N-acetylglucosaminidase H generates a fully active aglycoreceptor polypeptide, indicating that core oligosaccharide addition is a prerequisite for activation but that oligosaccharide chains are not intrinsically required for EGF binding [31].
• The findings are consistent with the results obtained by endo-beta-N-acetylglucosaminidase F treatment of h-lamp-1 and h-lamp-2 precursors, described in the preceding paper (Carlsson, S. R., Roth, J., Piller, F., and Fukuda, M. (1988) J. Biol. Chem. 263, 18911-18919) [32].
• On the other hand, oligosaccharides containing mannosyl, xylosyl, rhamnosyl, and ribosyl units were liberated from endo-beta-N-acetylglucosaminidase-resistant glycopeptides upon treatment with N-glycanase [33].

Analytical, diagnostic and therapeutic context of FLJ21865

• The cells incorporate [3H]mannose into the enzyme; after release with endo-beta-N-acetylglucosaminidase H, most of the radioactivity comigrates with Glc1-Man9-GlcNAc on a gel filtration column [34].
• Oligosaccharides that migrated on paper chromatography as Man6-30GlcNAc standards were obtained upon treatment of delipidated proteins with a protease and endo-beta-N-acetylglucosaminidase H [35].
• Through the use of the specific glycosidases neuraminidase and endo-beta-N-acetylglucosaminidase H and affinity chromatography on lectin-Sepharose gels, we show here that the receptor is an N-glycosyl protein that contains complex carbohydrate chains [36].
• The glycopeptides tightly bound to the lectin were treated by endo-beta-N-acetylglucosaminidase H and oligosaccharides separated by HPLC [37].
• Sensitivities to the glycosidases peptide N-glycosidase F and endo-beta-N-acetylglucosaminidase H on both western blots and silver-stained gels suggested that the glutamate receptors were at least major constituents of the glycoprotein bands [38].

References