EC Number   |
General Information |
Reference |
|---|
   2.4.1.155 | malfunction |
absense of the enzyme is due to a base insertion at nucleotide 822 of the Magt5 gene that shifts the open reading frame. A 155 amino acid truncated GlcNAcT-V (instead of a full length 740 amino acid enzyme) may be synthesized, which consists of the cytosolic and transmembrane domains and a short piece of the stem region, the truncated enzyme is degenerated. Lack of the enzyme protein causes a reduction in Golgi volume density in Lec4A cells, this can be reversed by stable transfection of Lec4A cells with a cDNA encoding Mgat5. No effect on Golgi volume density is observed in CHO Lec1 cells that contain enzymatically active GlcNAcT-V, but cannot synthesize beta1,6-branched glycans due to an inactive GlcNAcT-I in their Golgi apparatus. The structure of the Golgi apparatus in cells stably transfected and therefore overexpressing different glycosyltransferases appears normal |
736218 |
| 2.4.1.155 | malfunction |
associated with increase metastasis |
703956 |
| 2.4.1.155 | malfunction |
decreased enzyme activity due to inflammatory cytokine induction in human monocytes results in enhancement of integrin alpha5beta1-dependent monocyte-vascular endothelium adhesion and transmigration |
722417 |
| 2.4.1.155 | malfunction |
enzyme down-regulation inhibits the proliferation, migration and invasion of the Hep-G2 cells |
722200 |
| 2.4.1.155 | malfunction |
GnT-V null brains lack N-linked, beta(1,6)-glycans but have normal levels of O-Manbeta(1,6)-branched structures |
722771 |
| 2.4.1.155 | malfunction |
GnT-V overexpression greatly promotes cell migration in the transfectants by using wound healing assay. But the induction in the cell migration is significantly suppressed by an addition of chitosan oligosaccharides (COS) |
758997 |
| 2.4.1.155 | malfunction |
GnT-V overexpression induces an aberrant E-cadherin cellular localization and alters cell morphology, fibroblastoid cells exhibit a remarkable decrease of E-cadherin membranar expression with punctual E-cadherin staining in focal areas of cell-cell contacts |
721738 |
| 2.4.1.155 | malfunction |
inhibition of enzyme Gnt-V increases the radiosensitivity of cancer cells. Increased enzyme activity leads to the radiosensitivity and migration of small cell lung cancer cells by inducing epithelial-mesenchymal transition. Overexpression of Gnt-V leads to a further increase in the relative viable cell number and survival fraction with a decrease in apoptosis rate and Bax/Bcl-2 ratio, when the cells are treated with irradiation. Downregulation of Gnt-V increased E-cadherin but suppressed ZEB2, vimentin and N-cadherin expression, while upregulation of enzyme levels leads to the downregulation of E-cadherin and upregulation of ZEB2, vimentin and N-cadherin at both the protein and mRNA levels |
736094 |
| 2.4.1.155 | malfunction |
inhibition of N-acetylglucosaminyltransferase V enhances the cetuximab-induced radiosensitivity of nasopharyngeal carcinoma (NPC) cells likely through EGFR N-glycan alterations. Cetuximab is an epidermal growth factor receptor (EGFR) inhibitor used as a radiosensitizer in the treatment of NPC. The half-maximal inhibitory concentration (IC50) of cetuximab in CNE-1 and CNE-2 cells is 0.717 and 1.244 mg/ml, respectively |
759306 |
| 2.4.1.155 | malfunction |
interruption of beta1,6-GlcNAc glycan modification of CD147/basigin decreases matrix metalloproteinase (MMP) expression in HCC cell lines and affects the interaction of CD147/basigin with integrin beta1, mechanism modeling, overview. Real-time PCR shows that MMP-1, MMP-2, and MMP-9 are reduced in cells treated with mutant CD147/basigin (defective beta1,6-branched N-glycosylation) compared with cells treated with wild-type, suggesting that GnT-V-mediated glycosylation increases CD147/basigin-mediated HCC cell invasion. Overexpression of GnT-V increases the level of CD147/basigin-beta1,6-branching and the induction of MMPs |
759648 |
