EC Number   |
General Information |
Reference |
|---|
   2.4.1.145 | malfunction |
aberrant glycosylation of the cell surface is associated with the malignant transformation of normal cells. Tumor-cell-surface glycans are closely associated with tumor-cell migration, adhesion, and metastasis4, profiling of specific cell surface N-glycans in hepatocellular carcinoma with clinical tissues (88 tumor and adjacent normal tissues) and the corresponding serum samples of hepatocellular carcinoma patients, overview. The level of core-alpha-1,6-fucosylated triantennary glycan (NA3Fb) increases both on the cell surface and in the serum samples of hepatocellular carcinoma patients, and mRNA and protein expression of N-acetylglucosaminyltransferase IVa (GnT-IVa), which is related to the synthesis of the NA3Fb, is substantially increased in hepatocellular carcinoma tissues. Knockdown of GnT-IVa leads to a decreased level of NA3Fb and decreased ability of invasion and migration in HCC cells. The high expression of GnT-IVa is the cause of the abnormal increase of NA3Fb on the HCC cell surface, which regulates cell migration |
737252 |
| 2.4.1.145 | malfunction |
GnT-IVa overexpression increases cell adhesion, migration and invasion abilities of Jar cells. GnT-IVa overexpression increases cellular interaction with ECM as demonstrated by the relative adhesion rates of mock cells and Jar-GnT4a cells on fibronectin, collagen type I and collagen type IV. GnT-IVa knockdown in choriocarcinoma cells suppresses migration and invasion and decreases cellular adhesion to extracellular matrix |
759880 |
| 2.4.1.145 | malfunction |
isozyme GnT-IVb deficiency shows mild phenotypic alterations in hematopoietic cell populations and hemostasis, GnT-IVa/-IVb double deficiency completely abolishes GnT-IV activity that results in the disappearance of the GlcNAcbeta1-4 branch on the Manalpha1-3 arm |
703913 |
| 2.4.1.145 | metabolism |
N-acetylglucosaminyltransferase-IV synthesizes the GlcNAcbeta(1-4) branch structure on the Manalpha(1-3) arm of N-glycan core, and is essential for the production of multiantennary N-glycans cooperatively with N-acetylglucosaminyltransferase-V |
723792 |
| 2.4.1.145 | physiological function |
N-acetylglucosaminyltransferase IV (GnT-IV) is a glycosyltransferase which catalyses the formation of beta1,4GlcNAc branches on the mannose core of N-glycans. beta1,4GlcNAc branches on human chorionic gonadotropin (hCG) are detected in GTN but not in normal pregnancy or hydatidiform mole. N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma. Identification of target proteins for GnT-IVa glycosylation which contribute to the malignancy of choriocarcinoma, overview. GnT-IVa overexpression increases highly branched N-glycans on integrin beta1. Highly branched N-glycans resulting from the action of GnT-IVa are strongly detected in invasive mole and choriocarcinoma, in proportion to the GnT-IVa protein expression. GnT-IVa may play an important role in accelerating the malignancy of choriocarcinoma through addition of beta1,4GlcNAc branches to the N-glycans on some proteins |
759880 |
| 2.4.1.145 | physiological function |
the enzyme acts in migration and metastasis of mouse hepatocarcinoma cells through altering the glycosylation of CD147 |
722374 |
| 2.4.1.145 | physiological function |
the enzyme is involved in synthesis of tetra-antennary N-linked glycans. Cell surface glycans play an important role in intercellular and intracellular processes, including cell adhesion and development, cell recognition, and cancer development and metastasis. Changes in cell surface glycosylation modulate cellular activity |
737252 |
