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 | 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 | 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 | 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 | 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 | more |
GnT-III overexpression does not affect cell morphology |
721738 |
| 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 |
