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additional information
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beta1,6-N-acetylglucosaminyltransferase V (GnT-V) is encoded by ets-1, a transcriptional factor which also regulates several enzymes associated with cell invasion and metastasis
malfunction
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associated with increase metastasis
malfunction
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Mgat5 knockout mice, change in depression-like behaviour, decrease in immobility time in the forced swim test and the tail suspension test, no response to antidepressant treatment, altered social behavior in males
malfunction
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N-acetylglucosaminyltransferase Va knockout mice, aberrant expression of several N-glycan structures, decrease in tumor progression
malfunction
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overexpressed in malignant tumors
malfunction
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decreased enzyme activity due to inflammatory cytokine induction in human monocytes results in enhancement of integrin alpha5beta1-dependent monocyte-vascular endothelium adhesion and transmigration
malfunction
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enzyme down-regulation inhibits the proliferation, migration and invasion of the Hep-G2 cells
malfunction
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GnT-V null brains lack N-linked, beta(1,6)-glycans but have normal levels of O-Manbeta(1,6)-branched structures
malfunction
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Mgat5-deficient mouse skin is resistant to 12-O-tetradecanoyl phorbol-13-acetate-induced epidermal thickening. Cell surface epidermal growth factor receptor expression is decreased in Mgat5-deficient mouse keratinocytes
malfunction
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N-acetylglucosaminyltransferase-V-deficient mice are born healthy and lack beta1,6GlcNAc branches on N-glycans, but develop immunological disorders due to T-cell dysfunction at 12-20 months of age
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
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
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
malfunction
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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
malfunction
Mgat5 overexpression increases p21-activated kinase 1 (PAK1) expression and upregulated beta-1-6-GlcNAc branched N-glycosylation. Mgat5 overexpression promotes anchorage-independent growth and inhibits anoikis in hepatoma cells. shRNA-mediated PAK1 knockdown and kinase inactivation with kinase dead mutant PAK1 K299R coexpression or allosteric inhibitor P21-activated kinase inhibitor III (IPA3) treatment reverses anoikis resistance in Mgat5-overexpressed hepatoma cells. Knockdown of Mgat5 reduces EGFR/PAK1-dependent anoikis resistance, which can be reversed by PAK1 T423E
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)
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
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
malfunction
overexpression of N-acetylglucosaminyltransferase V protects detached cancer cells from apoptotic death, and suppression or knockout of the gene sensitized cancer cells to the apoptotic death. The gene overexpression also stimulates anchorage-dependent as well as anchorage-independent colony formation of cancer cells following anoikis stress treatments
metabolism
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part of N-glycan pathway
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
metabolism
the enzyme is involved in the N-glycan-branching pathway, regulation of cellular metabolite levels by Mgat5, overview
metabolism
activation of the PI3K/Akt pathway is involved in the regulation of GnT-V expression and deletion of GnT-V-mediated N-glycosylation impairs the PI3K/Akt pathway
physiological function
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involved in the malignant potential of mucinous ovarian cancer
physiological function
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tumor progression
physiological function
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a high enzyme expression in keratinocytes contributes to heparin-binding epidermal growth factor-like growth factor-mediated epidermal hyperproliferation by inhibiting endocytosis of epidermal growth factor receptors bearing beta1,6 N-acetylglucosamine on their N-glycans. The enzyme plays a role in epidermal homoeostasis, particularly in hyperproliferative conditions
physiological function
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concomitant overexpression of tissue inhibitor of metalloproteinase-1 and N-acetylglucosaminyltransferase V directs accelerated tumor growth and cancer progression in vivo and in vitro. Cells with high enzyme expression show higher collagenolytic activity, compared with the mock cells. Membrane type-1-matrix metalloproteinase expression is induced by N-acetylglucosaminyltransferase V overexpression
physiological function
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enzyme overexpression of in cancer cells enhances the signaling of growth factors such as epidermal growth factor by increasing galectin-3 binding to polylactosamine structures on receptor N-glycans. Enzyme overexpression in Mv1Lu cells enhances the migration of these cells to scratch wounds. GnT-V maintains skin homeostasis by regulating the proliferation of keratinocytes through epidermal growth factor-R signaling
physiological function
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GnT-V is involved in synthesizing branched O-mannosyl glycans in brain
physiological function
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N-acetylglucosaminyltransferase V (GnT-V) regulates transforming growth factor-beta1 response in hepatic stellate cells and the progression of steatohepatitis through modulating lymphocyte and hepatic stellate cell functions. Excess expression of GnT-V enhances beta1-6GlcNAc branching of N-glycans in transgenic hepatic stellate cells. GnT-V enhances transforming growth factor-beta signaling but decreases collagen I expression in transgenic hepatic stellate cells
physiological function
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N-acetylglucosaminyltransferase V expression is closely associated with metastasis in vivo
physiological function
elevated expression and activity of N-acetylglucosaminyltransferase V in hepatocellular carcinoma is a common early event involved in tumor invasion during hepatocarcinogenesis. EGFR/PAK1 signaling dominates Mgat5-induced resistance of hepatoma cells to anoikis
physiological function
enzyme expression is involved in the development of various cancers and their progression, through altering N-glycan branching, associations between MGAT5 expression and clinicopathologic features, overview. Kaplan-Meier survival analysis indicates that the overall survival of gastric cancer patients with low intratumoral MGAT5 expression is significantly poorer than those patients with high MGAT5 intratumoral expression
physiological function
enzyme that catalyzes the formation of a beta1,6-N-acetylglucosamine side chain to a core mannosyl residue in N-linked glycoproteins. Besides its direct function of producing aberrant glycoproteins, it promotes cancer progression by its involvement in the stimulation of oncoproteins. Enzyme GnT-V guides the transcriptional activation of membrane-type matrix metalloproteinase-1 (MT1-MMP) in cancer cells. The activated MT1-MMP expression has dual effects on cancer progression. It not only promotes proteolytic activity for cancer cells per se, but also leads to the activation of MMP-2. Consequently, the activation of the two MMPs triggered by GnT-V intensifies the invasive potential. Cancer invasion is stimulated by GnT-V-induced activation of both MT1-MMP and MMP-2
physiological function
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expression of enzyme Gnt-V correlates with the N stage in patients with small cell lung cancer. Increased enzyme activity leads to the radiosensitivity and migration of small cell lung cancer cells by inducing epithelial-mesenchymal transition. Gnt-V regulates the expression of epithelial and mesenchymal markers in SCLC cells
physiological function
GnT-V promotes the destabilization of E-cadherin at the cell membrane leading to its mislocalization and unstable adherens-junctions with impairment of cellcell adhesion. Role pf the enzyme GnT-V in E-cadherin-mediated tumor invasion. GnT-V catalyzes the addition of ?1,6 GlcNAc branching N-glycans and is associated to increased metastasis. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures
physiological function
N-acetylglucosaminyltransferase V catalyzes the synthesis of the beta1-6 bond between the sugar residue of the donor and alpha1,6-linked mannose of the core of N-glycan. Subsequently, the beta1-6 branch is formed and antennae are initiated
physiological function
alterations in glycosylation patterns regulate cancer development and progression, serve as important biomarkers, and provide a set of specific targets for diagnosis and therapeutic intervention. The modifications most often associated with cancer include sialylation, beta1,6-GlcNAc-branched N-glycans, and core fucosylation. Increased GlcNAc-branched N-glycan levels result from increased activity of N-acetylglucosaminyltransferase V (GnT-V) encoded by the mannoside acetylglucosaminyltransferase 5 (MGAT5) gene and are closely associated with cancer metastasis. N-acetylglucosaminyltransferase V (GnT-V) regulates cancer processes and cancer cell migration. GnT-V-mediated N-glycosylation of CD147/basigin, a tumor-associated glycoprotein that carries beta1,6-N-acetylglucosamine (beta1,6-GlcNAc) glycans, is upregulated during TGF-beta1-induced epithelial-to-mesenchymal transition (EMT), which correlates with tumor metastasis in patients with hepatocellular carcinoma (HCC). The PI3K/Akt signaling pathway is involved in the regulation of GnT-V expression
physiological function
N-acetylglucosaminyltransferase V (GnT-V) catalyzes the formation of the N-linked beta-1-6 branching of oligosaccharides adding GlcNAc to beta-1,6-linked branches
physiological function
N-acetylglucosaminyltransferase V (GnT-V) is a Golgi-located enzyme that catalyzes the branching of the beta1,6-N-acetylglucosamine side chain to the core mannosyl residue of N-linked glycan. N-acetylglucosaminyltransferase V confers anoikis resistance to colon cancer cells during hematogenous metastasis. This resistance is abolished by the lectin from Sambucus sieboldiana, treatment with the lectin significantly sensitizes anoikis-induced cancer cell deaths in vitro as well as in vivo. Anoikis is a form of anchorage-dependent apoptosis, and cancer cells adopt anokis-resistance molecular machinery to conduct metastasis. The MGAT5 gene is a key modulator of anoikis resistance, MGAT5-stimulated anoikis resistance is validated in clinical specimens by correlating the MGAT5 mRNA levels to the cancer stage. MGAT5 potentiates anchorage-dependent and -independent growth following anoikis stress. Glycan profiling identifies unique N-glycan structural features involved in anoikis resistance