Disease relevance of NGLY1

• Restriction endonuclease maps of PNG-1 proviral DNA differed from that of a prototype strain of HTLV-I (MT-2), but, as verified by polymerase chain reaction, PNG-1 was definitely HTLV-I, not HTLV-II [1].
• A 36-kDa binding protein (BP), not digestible with N-glycanase, is increased in patients with extrapancreatic tumor hypoglycemia and during IGF I administration in healthy adults [2].
• The specific activity of purified MB1004 from E. coli was compared against the equivalent recombinant material purified from mammalian cells that was naturally glycosylated (MB1004G) or deglycosylated after treatment with N-glycanase (MB1004N) [3].
• To determine whether or not the glycan moieties in hTPO play a role in the disease-associated epitopes in Hashimoto's thyroiditis, radiolabeled recombinant hTPO was immunoprecipitated after digestion with N-glycanase [4].
• A commercially available endoglycosidase (N-glycanase, Genzyme, Boston, Mass.) purified from Flavobacterium meningosepticum with a specificity for cleaving asparagine-linked carbohydrate moieties in glycoproteins was tested on several pituitary and chorionic gonadotropins as substrates [5].

High impact information on NGLY1

• Partial sequence analysis and digestion with N-glycanase indicate that these are glycosylation forms of a single protein [6].
• A single messenger RNA transcript was found in all positive RNA samples, and N-glycanase treatment showed the form found in COS cells was identical to the form present on peripheral blood mononuclear cells (PBMCs) [7].
• Rhesus erythrocytes, treated with N-glycanase, bound specifically to P. vivax region II [8].
• Endo F N-glycanase mixture, which acts on all glycan species, including triantennary chains, led to complete deglycosylation of gp120/160 and of CD4 [9].
• Comparison of kinetic characteristics obtained with a yeast-derived hyperglycosylated form of BSF-1 (Mr 60,000) and N-glycanase-treated, sugar-free BSF-1 (Mr 15,000) showed no significant differences [10].

Chemical compound and disease context of NGLY1

• Antigenic characterization of this variant, designated PNG-1, by immunofluorescence, indicated no expression of gag-encoded proteins p19 and p24 (even after incubation with 5-bromo-2'-deoxyuridine), using monoclonal and polyclonal antibodies against HTLV-I gag gene products [1].

Biological context of NGLY1

• N-glycanase digestion increased I566T mutant FVIII activity and increased its IC50 for the peptide (1,400 mumol/L) [11].
• PCA reactivity with the 60-90-kDa antigen was abolished when the gastric membranes were (a) digested with Pronase, (b) reduced with 100 mM dithiothreitol, (c) treated with sodium periodate, or (d) digested with N-glycanase [12].
• An active process was involved since both pTHP gel formation and attenuation of cell adhesion were abolished by boiling or oligosaccharide removal with N-glycanase digestion [13].
• A combination of physiological parameters, chemotaxonomic characteristics, distinguishing 16S rRNA gene sequences, and phylogenetic analysis based on 16S rRNA genes provided strong evidence for the two new genera (represented by strains of the PNG1 clade and strain UMM518) within the family Micromonosporaceae [14].
• Treatment of crude cellular membrane fractions with N-glycanase, endoglycosidase H or neuraminidase showed that the altered migration of MRP on SDS-PAGE is due to a post-translational modification [15].

Anatomical context of NGLY1

• In comparison, in endothelial cells dimeric VAP-1 is larger, no trimeric forms are found, and VAP-1 does not have N-glycanase-sensitive oligosaccharides [16].
• Processing of a class I-restricted epitope from tyrosinase requires Peptide N-glycanase and the cooperative action of endoplasmic reticulum aminopeptidase 1 and cytosolic proteases [17].
• The glycosylation and polypeptide chain length of the p150,95, Mac-1, and lymphocyte function associated antigen (LFA-1) alpha and beta subunits were compared by immunoprecipitation with subunit specific MAb and antisera, and by digestion with Endo H and N-glycanase [18].
• Because some reports indicate that digestion of Fc gamma RIII on NK cells (Fc gamma RIIINK) with N-glycanase also results in two bands on SDS-PAGE, we investigated Fc gamma RIIINK to explore the possibility of a corresponding allelic polymorphism in this receptor [19].
• Analysis of immunoprecipitated E-selectin from human umbilical vein endothelial cells (HUVEC) by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate showed that E-selectin was completely resistant to endoglycosidase H, but sensitive to peptide N-glycanase F digestion [20].

Associations of NGLY1 with chemical compounds

• The oligosaccharides were released from the glycoprotein by N-glycanase digestion, coupled to a 2-aminopyridyl residue, and subjected to two-dimensional sugar mapping technique [21].
• Monosaccharides including mannose, fucose, glucose, galactose, GlcNAc, and GalNAc reversibly dissociated the intact form of the Hb, but the removal of carbohydrate with N-glycanase resulted in irreversible dissociation [22].
• In contrast, treatment with trypsin, endoglycosidase-F, O-Glycanase, N-Glycanase, lipase, various phospholipases, boiling, 2-mercaptoethanol at 37 degrees C, or periodate did not reduce the antigenicity of the larval surface to antibody NEB-D1E5 [23].
• All mutant FVIII proteins were susceptible to thrombin cleavage, and the A2-domain fragment from the I566T mutant had a reduced mobility because of use of an introduced potential N-linked glycosylation site that was confirmed by N-glycanase digestion [11].
• This variation was mainly the consequence of a modification of the glycosylation pattern of the molecule since deglycosylation by N-glycanase or biosynthesis in the presence of tunicamycin always produced a single molecular weight form, whether or not the source of tissue was normal or cancerous [24].

Physical interactions of NGLY1

• Enzymatic removal of carbohydrate chains from glycosylated gp120 by endoglycosidase H or an endoglycosidase F/N glycanase mixture had no effect on the ability of gp120 to bind CD4 [25].
• N-Glycanase deglycosylation of purified 44 kDa chymotryptic collagen-binding domain from human plasma fibronectin does not significantly modify its behavior on gelatin affinity chromatography [26].

Regulatory relationships of NGLY1

• The E2 protein expressed in both insect and mammalian cells was a glycoprotein of 60 kDa (gp60) and removal of the sugar residues by N-glycanase yielded 38- and 40-kDa proteins [27].
• The differences observed in apparent molecular masses of fibronectin receptors from uninduced and induced U-937 or THP-1 cells are removed by treatment of purified integrins with endoglycosidase F or N-glycanase [28].

Other interactions of NGLY1

• On the basis of their sensitivities to reducing agents and to sialidase, O-sialoglycoprotease, and N-glycanase treatments, we have characterized CD164 epitopes and grouped them into three classes by analogy with CD34 epitope classification [29].
• However, endoglycosidase digestion (using N-glycanase and endoglycosidase H) and peptide mapping (using V8 protease and N-chlorosuccinimide) strongly suggested that CD22 and CD21 are distinct gene products [30].
• After selective deglycosylation with either neuraminidase or N-glycanase, rLCAT and plasma LCAT had identical molecular weights [31].
• Glycosylated forms of CFTR were present as confirmed by treatment with N-glycanase [32].
• N-glycanase digestion suggested the presence of a 50 kDa core protein for the CVEC-FGFR [33].

Analytical, diagnostic and therapeutic context of NGLY1

• After SDS-PAGE of N-glycanase-treated FcR III under nonreducing conditions, the apparent Mr of each structural type was decreased, suggesting the presence of intramolecular disulfide bonds [34].
• N-glycanase digestion of 125I-labeled antigens purified by immunoprecipitation and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis collapsed the 60-90-kDa antigen to a sharp 34-kDa band; the 100-120-kDa component was unaffected [12].
• Treatment with N-glycanase caused a reduction in mass of 3571 +/- 219 Da, but there was no loss of mass after treatment with O-glycanase or neuraminidase [35].
• Treatment of placental cytosolic preparations with N-Glycanase prior to immunoblotting resulted in the identification of only an Mr 25,000 species [36].
• Lectin affinity high-performance liquid chromatography. Interactions of N-glycanase-released oligosaccharides with Ricinus communis agglutinin I and Ricinus communis agglutinin II [37].

References