2.4.1.144	malfunction	detailed glycomic analysis of the effect of GnT-III overexpression in WM266-4-GnT-III metastatic melanoma cells, overview. Overexpression of GnT-III in melanoma leads to modification of a broad range of N-glycan types by the introduction of the bisecting GlcNAc residue with highly branched complex structures among them. The presence of these unusual complex N-glycans results in stronger interactions of cellular glycoproteins with the PHA-L. Elevated activity of GnT-III in cancer cells does not necessarily lead to a total abrogation of the formation of highly branched glycans. The modification of pre-existing N-glycans by the introduction of bisecting GlcNAc can modulate their capacity to interact with carbohydrate-binding proteins such as plant lectins	759316	
2.4.1.144	malfunction	downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition. Excessive oxidative stress can decrease GnT-III expression in trophoblast and the decreased expression of GnT-III may be involved in the development of preeclampsia. Clinical characteristics of preeclampsia group comparedwith normal pregnancy group, overview	759591	
2.4.1.144	malfunction	knockdown of GnT-III by siRNA causes no alteration in expression levels of E-cadherin mRNA and protein, but induces alterations on E-cadherin cellular localization in MCF-7/AZ cells. GnT-III knockdown cells reveal a membrane de-localization of E-cadherin leading to its cytoplasmic accumulation and cause modifications of E-cadherin N-glycans catalyzed by GnT-III and GnT-V	703956	
2.4.1.144	malfunction	suppression of GnT-III in epithelial ovarian carcinoma (EOC) cell lines and primary tumor-derived cells results in an inhibition of Notch signaling that is more potent than pharmacologic blockage of Notch activation via gamma-secretase inhibition. The inhibition results from the redirection of the Notch receptor to the lysosome, a distinct mechanism	759483	
2.4.1.144	metabolism	existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview	721738	
2.4.1.144	metabolism	GnT-III is considered to be a key glycosyltransferase in the N-glycan biosynthetic pathway because the introduction of the bisecting GlcNAc residue suppresses further processing and elongation of the N-glycans catalyzed by GnT-V. So, in the tumor context, GnT-III and GnT-V have generally a dual role where GnT-III acts as metastases suppressors whereas GnT-V is associated with increased malignancy and metastasis	759591	
2.4.1.144	metabolism	interplay between GnT-III and sialyltransferases in the expression of their enzymatic products and also their functions in tumor metastasis. Interplay between GnT-III and ST6GAL1 in regulating cell migration	736507	
2.4.1.144	metabolism	N-acetylglucosaminyltransferase-III-mediated glycosylation, specifically on E-cadherin, is a major component of the Epithelial-Mesenchymal-Transition /Mesenchymal-Epithelial-Transition mechanism signature	723551	
2.4.1.144	additional information	GnT-III overexpression does not affect cell morphology	721738	
2.4.1.144	additional information	usage of MALDI-TOF and ESIion-trap-MS/MS together with HILIC-HPLC of 2-AA labeled N-glycans to study the N-glycome of membrane-attached and secreted proteins. Characterization of N-glycan epitopes on membrane and secreted proteins using plant lectins, several plant lectins are used in lectin blot assay, overview	759316	
2.4.1.144	physiological function	all subunits of laminin-332 are modified by GnT-III, introduction of GnT-III inhibits GnT-V products	704446	
2.4.1.144	physiological function	glycosyltransferase GnT-III activates Notch signaling and drives stem cell expansion to promote the growth and invasion of ovarian cancer. Glycosylation mediated by GnT-III increases Notch receptor levels and activity. GnT-III expression controls the expansion of side-population cells, also known as cancer stem cells, GnT-III expression regulates the levels and activation of the heavily glycosylated Notch receptor involved in normal and malignant development. The gene Mgat3 encoding the glycosyltransferase GnT-III is elevated in epithelial ovarian carcinomas (EOCs) and leads to the production of abnormal truncated N-linked glycan structures instead of the typical bisected forms, role for bisecting glycosylation in the control of Notch transport, overview. GnT-III expression maintains the side-population and promotes spheroid formation in ovarian cancer cells	759483	
2.4.1.144	physiological function	GnT-III induced a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. Role of GnT-III on E-cadherin-mediated tumor suppression. GnT-III catalyzes the formation of a bisecting GlcNAc structure in N-glycans and is a metastases suppressor. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures	721738	
2.4.1.144	physiological function	GnT-III is an antagonistic of GnT-V, thereby contributing to the suppression of cancer metastasis. Modification of the alpha3 subunit by GnT-III supersedes modification by GnT-V. Overexpression of GnT-III in highly metastatic melanoma cells reduces beta1,6 GlcNAc branching in cell-surface N-glycans and increases bisected N-glycans, which results in an enhancement of cell-cell adhesion due to prolonged turnover of E-cadherin on the cell surface. Overexpression of GnT-III significantly reduces the ability of epithelial growth factor receptor to bind to its receptor, reduces epithelial growth factor receptor autophosphorylation, and subsequently blocks epithelial growth factor receptor-mediated Erk phosphorylation in U373 MG glioma cells and in PC12 cells. GnT-III also inhibits the formation of the alpha-Gal epitope, which is a major xenotransplantation antigen that is problematic in swine-to-human organ transplantation. GnT-III affects antibody-dependent cellular cytotoxicity activity. Transgenic mice, in which GnT-III is expressed specifically in the liver by use of a serum amyloid P component gene promoter, exhibits fatty liver. Ectopic expression of GnT-III disrupts the function of apolipoprotein B, resulting in abnormal lipid accumulation	705381	
2.4.1.144	physiological function	GnT-III-deficient mice are viable and reproduce normally, thus GnT-III and the bisected N-glycans may not be essential for normal development	705381	
2.4.1.144	physiological function	integrins are modified by GnT-III, which inhibits cell migration and cancer metastasis. Overexpression of GnT-III results in an inhibition of alpha5beta1 integrin-mediated cell spreading and migration, and the phosphorylation of the focal adhesion kinase. Overexpression of GnT-III in highly metastatic melanoma cells reduces beta1, six branching in cell-surface N-glycans and increases bisected N-glycans. GnT-III is an antagonistic of GnT-V, contributing to the suppression of cancer metastasis, overexpression of GnT-III inhibits GnT-V-induced cell migration. Overexpression of GnT-III slows E-cadherin turnover, resulting in increased E-cadherin expression on the surface of B16 melanoma cells	703093	
2.4.1.144	physiological function	introduction of GnT-III suppresses additional processing and branching formation of N-glycans catalyzed by other endogenous glycosyltransferases, such as GnT-V and GnT-IV. Cell adhesion on fibronectin is down-regulated in GnT-III transfectants compared with mock and GnT-V transfectants. Overexpression of GnT-III significantly inhibits cell migration on fibronectin. GnT-III significantly down-regulates cell spreading on fibronectin in wild-type transfectants, whereas the deletion of site-4 abolishes the suppression of cell spread induced by GnT-III in D-4 transfectants	704468	
2.4.1.144	physiological function	levels of fucosylation (79%, median value 80%, q1, 78%, q3, 82%) and xylosylation (94, median value 94%, q1, 93%, q3, 95%) are not significantly reduced in cells expressing GnTIII under the control of the CaMV 35S promoter compared to the levels observed in wild-type cells. Expression of GnTIII under the control of the UAS123mas promoter reduces fucosylation, but not xylosylation	704773	
2.4.1.144	physiological function	metastasis suppressor	703956	
2.4.1.144	physiological function	N-acetylglucosaminyltransferase III (GnT-III) is known to catalyze N-glycan bisection and thereby modulate the formation of highly branched complex structures within the Golgi apparatus. While active, it inhibits the action of other GlcNAc transferases such as GnT-IVand GnT-V. Moreover, GnT-III is considered an inhibitor of the metastatic potential of cancer cells both in vitro and in vivo	759316	
2.4.1.144	physiological function	N-acetylglucosaminyltransferase III catalyzes the addition of the bisecting GlcNAc branch on N-glycans, and is a metastasis suppressor with an important role of GnT-III in N-glycan biosynthesis and tumor cell behaviours. Increased expression of GnT-III in human hepatomas, glioma, and ovarian cancers. Overexpression of GnT-III significantly inhibits alpha2,3-sialylation but not alpha2,6-sialylation via post-transcriptional mechanisms. GnT-III plays an anti-migratory role in tumor cells without or with a low level of alpha2,6-linked sialic acids but not in those alpha2,6-hypersialylated	736507	
2.4.1.144	physiological function	N-acetylglucosaminyltransferase III is a glycosyltransferase which produces bisected N-glycans by transferring GlcNAc to the 4-position of core mannose. Bisected N-glycans are involved in physiological and pathological processes through the functional regulation of their carrier proteins	735761	
2.4.1.144	physiological function	N-acetylglucosaminyltransferase III is involved in formation of beta1,4 linkage between GlcNAc and beta-mannose residue within the core of oligosaccharide. The resulting bisected N-glycan acquires a characteristic conformation that renders inaccessibility to many other enzymes participating in biosynthetic pathways of hybrid and complex multiantennary N-glycans as well as to lectins	735724	
2.4.1.144	physiological function	N-acetylglucosaminyltransferases III (GnT-III) is one of the most important N-glycosyltransferases encoded by the MGAT3 gene. GnT-III catalyzes the addition of GlcNAc via b1-4 linkage to the b-mannose of the mannosyl core of N-glycans. N-acetylglucosaminyltransferase III (GnT-III) is correlated with tumor invasion and metastasis. GnT-III is an important regulator at the maternal-fetal interface during early pregnancy	759591	
2.4.1.144	physiological function	overexpression of GnT-III downregulates alpha5beta1 integrin-mediated cell spreading and migration, and the phosphorylation of the focal adhesion kinase. Overexpression of GnT-III slows E-cadherin turnover, resulting in increased E-cadherin expression on the surface of B16 melanoma cells. GnT-III inhibits GnT-V-induced cell migration. Overexpression of GnT-III inhibits cancer metastasis by at least two mechanisms: an enhancement in cell-cell adhesion and a downregulation of cell-ECM adhesion	702516	
2.4.1.144	physiological function	the enzyme induces a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. The enzyme plays a role on E-cadherin-mediated tumor suppression	721738	
2.4.1.144	physiological function	the enzyme plays an important role in the suppression of cancer metastasis. The enzyme influences epithelial-to-mesenchymal transition-like changes through not only prolongation of E-cadherin turnover but also suppression of beta-catenin-p-Smad complex formation. The enzyme plays important roles in transforming growth factor-beta-induced epithelial-to-mesenchymal transition-like changes. The enzyme does not significantly affect the expression of E-cadherin mRNA	722755