Disease relevance of MGAT3

• Expression of bisecting N-acetylglucosaminyltransferase-III in human hepatocarcinoma tissues, fetal liver tissues, and hepatoma cell lines of Hep3B and HepG2 [1].
• Selective suppression of N-acetylglucosaminyltransferase III activity in a human hepatoblastoma cell line transfected with hepatitis B virus [2].
• N-Acetylglucosaminyltransferase III (GnT-III) catalyzes the formation of a bisecting GlcNAc structure in N-glycans, resulting in the suppression of metastasis [3].
• Cell cycle-dependent regulation of N-acetylglucosaminyltransferase-III in a human colon cancer cell line, Colo201 [4].
• Changes in N-acetylglucosaminyltransferase III, IV and V in renal cell carcinoma [5].

High impact information on MGAT3

• This change is consistent with a decrease in the activity of N-acetylglucosaminyltransferase III (GnTIII) toward PrP(C) in cells where PrP(Sc) is formed and argues that, in at least some cells forming PrP(Sc), the glycosylation machinery has been perturbed [6].
• The galactosyltransferase and N-acetylglucosaminyltransferase III activities of the bone marrow myeloma cells from 5 MM cases were found to have a low enzyme activity ratio of galactosyltransferase to N-acetylglucosaminyltransferase III which reflects the hypogalactosylation [7].
• N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on {alpha}3beta1 Integrin-mediated Cell Migration [3].
• Acyl-CoA:monoacylglycerol acyltransferase-2 (MGAT2) catalyzes the synthesis of diacylglycerol and differs from the MGAT1 and MGAT3 in tissue distribution at the mRNA level [8].
• The hepatitis B virus X protein inhibits secretion of apolipoprotein B by enhancing the expression of N-acetylglucosaminyltransferase III [9].

Chemical compound and disease context of MGAT3

• An N-acetylglucosaminyltransferase III which catalyzes the addition of N-acetylglucosamine through a beta 1-4 linkage (bisecting N-acetylglucosamine) to the beta-linked mannose of the trimannosyl core structure of N-linked oligosaccharides of glycoproteins was measured in human serum, and liver and hepatoma tissues [10].
• The activity of GlcNAc-T III was determined in Triton X-100 extracts of four human Epstein-Barr virus (EBV)-infected B-cell lines, in four T-cell lines originally established from lymphocytes of patients with acute lymphatic leukemia, and in human tonsillar B and T lymphocytes [11].

Biological context of MGAT3

• We have isolated and characterized the immediate (1651 bP) 5'-flanking region of the gene (GnT-III) encoding N-acetylglucosaminyltransferase III (GnT-III) from a human placental genomic library [12].
• The kinetic basis of the donor substrate specificity of beta1, 4-N-acetylglucosaminyltransferase III (GnT-III) was investigated using a purified recombinant enzyme [13].
• Transfection of N-acetylglucosaminyltransferase III gene suppresses expression of hepatitis B virus in a human hepatoma cell line, HB611 [14].
• Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by up-regulation of the internalization rate of the receptors [15].
• The increase of GlcNAc T-III activity and bis-GlcNAc content in N-glycans may be related to cell adhesion observed in monocytic differentiation [16].

Anatomical context of MGAT3

• N-acetylglucosaminyltransferase III (GlcNAc-TIII), a product of the human MGAT3 gene, was discovered as a glycosyltransferase activity in hen oviduct [17].
• In this paper, uridine diphosphate (UDP)-N-acetylglucosamine/beta-D-mannoside beta-1,4 N-acetylglucosaminyltransferase III (GlcNAc-transferase-III C 2.4.1.144) activity was determined in human hepatoma cell lines of Hep3B and HepG2, and also compared with those of normal liver tissues and primary hepatocytes [1].
• Changes in the expression of N-acetylglucosaminyltransferase III, IV, V associated with the differentiation of HL-60 cells [18].
• Beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase III activity in human B and T lymphocyte lines and in tonsillar B and T lymphocytes [11].
• The four EBV-transformed B-cell lines showed appreciable GlcNAc-T III activities (ranging from 3.4 to 19.0 nmol.h-1.mg protein-1), while the tonsillar resting B lymphocytes had much less activity (0.68 nmol.h-1.mg protein-1) [11].

Associations of MGAT3 with chemical compounds

• N-acetylglucosaminyltransferase III (GnT-III) is a key enzyme that inhibits the extension of N-glycans by introducing a bisecting N-acetylglucosamine residue [19].
• We suggest that the completely bisected nature of the light-chain oligosaccharides comes from a high level of activity of GlcNAc-T-III (the enzyme responsible for the attachment of the bisecting GlcNAc) in the cells producing the IgG [20].
• BACKGROUND AND AIM: UDP-N-acetylglucosamine: alpha-D-mannoside beta-1,4 N-acetylglucosaminyltransferase III (GnT-III) is a key enzyme in N-glycan biosynthesis [21].
• N-Acetylglucosaminyltransferase III (GnT III) catalyses the addition of N-acetylglucosamine through a beta 1-4 linkage to the mannose of the trimannosyl core, resulting in conversion of the concanavalin A (Con A)-reactive glycan into a non-reactive state [22].
• N-Acetylglucosaminyltransferase III activity of 21 patients with HCC was significantly reduced after treatment such as transcatheter arterial chemoembolization and/or percutaneous ethanol infection therapy, (123 +/- 77 to 100 +/- 60 pmol/mL per h) [22].

Regulatory relationships of MGAT3

• Caveolin-1 appears to regulate the localization of N-acetylglucosaminyltransferase III (GnT-III) in the intra-Golgi subcompartment [23].

Other interactions of MGAT3

• Caveolin-1 regulates the functional localization of N-acetylglucosaminyltransferase III within the golgi apparatus [23].
• In this study we examined the consequences of overexpression of the bisecting structure on the EGF receptor by gene transfection of U373 MG cells with the N-acetylglucosaminyltransferase III (GnT-III) [24].
• Simultaneously, the activities of alpha 1-6 fucosyltransferase (alpha 1-6FT) and N-acetylglucosaminyltransferase III (GnT-III), IV (GnT-IV) and V (GnT-V) were assayed in these cell lines [25].
• Competitive glycosylation has largely targeted replacement of Gal by insertion of a gene for a fucosyltransferase or a sialyltransferase, or by insertions of the gene for N-acetylglucosaminyltransferase III to reduce cell-surface expression of several oligosaccharides [26].
• Serum N-acetylglucosaminyltransferase III activities in hepatocellular carcinoma [22].

Analytical, diagnostic and therapeutic context of MGAT3

• Sequence analysis of the 5'-flanking region of the gene encoding human N-acetylglucosaminyltransferase III [12].
• The nodules had significant GlcNAc-T III activity (1.2-2.2 nmol/h/mg), whereas the surrounding liver, regenerating liver 24 h after partial hepatectomy and control liver from normal rats had negligible activity (0.02-0.03 nmol/h/mg) [27].
• N-Acetylglucosaminyltransferase III activity was determined by high performance liquid chromatography [22].
• BACKGROUND: Our previous study reported that cynomolgus monkey did not hyperacutely reject a skin xenograft from a N-acetylglucosaminyltransferase III (GnT-III) transgenic pig [28].

References