Cloned (Comment) | Organism |
---|---|
expressed in transgenic mice | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-D-glucose + (N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3)-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R | - |
Homo sapiens | UDP + N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6)-(beta-D-glucosyl-1,4)-beta-D-mannosyl-1,4-N-acetyl-beta-D-glucosaminyl-R | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GnT-III | - |
Mus musculus |
GnT-III | - |
Homo sapiens |
N-acetylglucosaminyltransferase III | - |
Mus musculus |
N-acetylglucosaminyltransferase III | - |
Homo sapiens |
Organism | Comment | Expression |
---|---|---|
Homo sapiens | downregulation of GnT-III expression in MDA-MB-231 cells, an E-cadherin-deficient cell line, the MDCK cell, in which GnTIII expression is undetectable, and fibroblasts, which lack E-cadherin | down |
Homo sapiens | significant up-regulation of GnT-III expression in epithelial cells that express basal levels of E-cadherin and GnT-III. Expression levels of GnT-III and its products, the bisected N-glycans, are up-regulated by cell-cell interaction via the E-cadherin-catenin-actin complex. GnT-III expression is significantly up-regulated in cells cultured under dense conditions. Modest increase in GnT-III expression under dense culture conditions in alpha-catenin-deficient DLD-1 cells as well as in E-cadherin-deficient MDA-MB-231 cells. Mutual regulation of GnT-III expression and E-cadherin-mediated cell-cell interaction exists as a positive-feedback loop | up |
General Information | Comment | Organism |
---|---|---|
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 | Homo sapiens |
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 | Mus musculus |