EC Number   |
General Information |
Reference |
|---|
   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 |
