EC Number   |
General Information |
Reference |
|---|
    2.4.1.122 | malfunction |
abrogation of the enzyme promotes membrane protein internalization. Disruption of core 1 O-glycosyltransferase activity induces endocytosis and faster accumulation of cell surface proteins in cytoplasmic vesicles and induces clathrin-mediated endocytosis. Enzyme-deficient human corneal keratinocytes display plasma membrane invaginations on the apical surface |
723563 |
| 2.4.1.122 | more |
C1GALT1 is overexpressed in various human malignancies |
759872 |
| 2.4.1.122 | malfunction |
C1GALT1 overexpression enhances HNSCC cell viability, migration, and invasion, which can be reversed by erlotinib. Silencing of C1GALT1 suppresses the malignant behavior both in vitro and in vivo. C1GALT1 knockdown decreases the EGFR signaling in SAS, OEC-M1, and FaDu cells. Decreased C1GALT1 causes accumulation of Tn antigens |
759356 |
| 2.4.1.122 | physiological function |
C1GalTA is required for nervous system morphogenesis, C1GalTA is required for laminin O-glycosylation |
703369 |
| 2.4.1.122 | malfunction |
C1GalTA null mutant is lethal, mutant animals exhibit a striking morphogenetic defect in which the ventral nerve cord is greatly elongated and the brain hemispheres are misshapen |
703369 |
| 2.4.1.122 | physiological function |
core 1 beta1,3-galactosyltransferase (C1GALT1) controls the crucial step of GalNAc-type O-glycosylation and is overexpressed in various human malignancies with a role in head and neck squamous cell carcinoma (HNSCC). Enzyme C1GALT1 seems to promote in vitro disease progression in ovarian cancer. C1GALT1 modifies O-glycans on epidermal growth factor receptor (EGFR). C1GALT1 regulates phosphorylation, EGF-binding affinity, and O-glycosylation of EGFR to enhance malignant phenotypes in HNSCC cells. C1GALT1 regulates EGF-binding affinity of EGFR in HNSCC cells. C1GALT1 transfers galactose to Tn antigen to form T antigen. C1GALT1 is overexpressed in head and neck squamous cell carcinoma (HNSCC) tumors and high C1GALT1 expression predicts poor prognosis |
759356 |
| 2.4.1.122 | physiological function |
core 1 beta1,3-galactosyltransferase (C1GALT1) controls the crucial step of GalNAc-type O-glycosylation. C1GALT1 regulates phosphorylation, EGF-binding affinity, and O-glycosylation of EGFR to enhance malignant phenotypes in HNSCC cells. Itraconazole blocks C1GALT1-mediated malignant phenotypes and EGFR activity, overview. C1GALT1 transfers galactose to Tn antigen to form T antigen |
759872 |
| 2.4.1.122 | malfunction |
core 1 beta1,3-galactosyltransferase (C1GALT1) expression is upregulated in HNSCC tumors and is associated with adverse clinicopathologic features. Moreover, high C1GALT1 expression predicts poor disease-free and overall survivals. C1GALT1 overexpression enhances HNSCC cell viability, migration, and invasion, which can be reversed by erlotinib. Silencing of C1GALT1 suppresses the malignant behavior both in vitro and in vivo. Blocking O-glycan elongation on epidermal growth factor receptor (EGFR) by C1GALT1 knockdown decreases EGF-EGFR binding affinity and inhibits EGFR signaling, thereby suppressing malignant phenotypes. C1GALT1 knockout also decreases the EGFR signaling in SAS cells as shown in two independent clones. C1GALT1 overexpression in SAS cells increases EGF-induced phosphorylation of EGFR at Y1068. By contrast, C1GALT1 knockdown decreases the EGFR signaling in OEC-M1 and FaDu cells. Decreased C1GALT1 causes accumulation of Tn antigens, which is detected by vicia villosa agglutinin (VVA) lectin |
759872 |
| 2.4.1.122 | physiological function |
core 1 O-glycosylation is required to maintain transcellular barrier function. Core 1 O-glycans contribute to maintenance of apical barrier function on exposed mucosal surfaces by preventing clathrin-mediated endocytosis |
723563 |
| 2.4.1.122 | malfunction |
dC1GalT1 loss in larvae leads to various defects, including a decreased number of circulating hemocytes, hyperdifferentiation of hematopoietic stem cells in lymph glands, malformation of the central nervous system, mislocalization of neuromuscular junction (NMJ) boutons, and ultrastructural abnormalities in NMJs and muscle cells. Mutant larvae show lower expression of glucuronylated T antigen on the muscles and at NMJs. Mislocalization of neuromuscular junction (NMJ) boutons and a partial loss of the basement membrane components collagen IV (Col IV) and nidogen (Ndg) at the muscle 6/7 boundary are observed. Those two phenotypes are correlated and identical to previously described phenotypes in dC1GalT1 mutant larvae |
759109 |
