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There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. Zusätzlich bieten wir Ihnen MGAT3 Antikörper (69) und MGAT3 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
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The MGAT3 and bisected complex N-glycans retard mouse mammary tumor progression; identification of key galectins that promote mammary tumor progression in mice is not straightforward because the galectin genes are expressed; and high levels of MGAT3.
data suggest that Fut8 (zeige FUT8 Proteine)(-/-) mice adapted to oxidative stress, both ex vivo and in vivo, by inducing various genes including GnT-III, which may compensate for the loss of core fucose functions
Mgat3 glycogene expression and GnT-III-mediated glycosylation, specifically on E-cadherin (zeige CDH1 Proteine), is a novel and major component of the Epithelial-Mesenchymal-Transition and the reverted process, Mesenchymal-Epithelial-Transition mechanism.
Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1 (zeige TGFB1 Proteine)) in epithelial cell lines
GnT-III expression may be precisely regulated by the interplay of E-cadherin (zeige CDH1 Proteine)-catenin complex-mediated cell-cell adhesion and Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) signaling
upregulation of GnT-III in AD brains may represent an adaptive response to protect them from additional beta-amyloid production
mice homozygous for the Mgat3T37 mutation that express truncated GlcNAc-TIII from two mutant alleles suffer neurological and other consequences
beta1,4-N-acetylglucosaminyltransferase III inhibits the function of alpha5beta1 integrin
An E-cadherin (zeige CDH1 Proteine)-dependent pathway plays a critical role in regulation of GnT-III expression; changes in GnT-III expression presumably contribute to intracellular signaling transduction during tissue development and homeostasis.
Novel insights into the epigenetic regulation of MGAT3/bisecting GlcNAc and demonstrate the importance of N-glycosylation in cancer progression.
Data suggest that GNT-III expression regulates levels/activation of the heavily glycosylated Notch (zeige NOTCH1 Proteine) receptor involved in normal and malignant cell development; suppression of GNT-III in epithelial ovarian carcinoma cell lines results in down-regulation of Notch (zeige NOTCH1 Proteine) signaling that is more potent than pharmacologic blockage of Notch (zeige NOTCH1 Proteine) activation.
MGAT3 expressed in cells stimulates lipid droplet growth. These findings provide additional evidence that MGAT3 likely functions as a triacylglycerol synthase in cells.
Core-fucosylated tetra-antennary structures were decreased in quantity likely as a result of hypomethylated MGAT3 gene promoter followed by increased expression of this gene
High expression of alpha2,6-sialylation on the cell surface could affect the anti-migratory role of GnT-III, which provides an insight into the mechanistic roles of GnT-III in tumor metastasis.
Mgat3 plays an important role in early spontaneous miscarriage in humans.
MGAT3 protein and gene expression in in uveal and cutaneous melanoma cells
HS5 cells had significantly enhanced levels of bisecting N-glycans (catalyzed by MGAT3 whereas HS27a cells had enhanced levels of Galbeta1,4GlcNAc.
GnT-III determines E-cadherin (zeige CDH1 Proteine)-mediated tumor suppression, and GnT-V (zeige MGAT5 Proteine) regulates E-cadherin (zeige CDH1 Proteine)-mediated tumor invasion.
There are believed to be over 100 different glycosyltransferases involved in the synthesis of protein-bound and lipid-bound oligosaccharides. The enzyme encoded by this gene transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc. Multiple alternatively spliced variants, encoding the same protein, have been identified.
, mannosyl (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
, beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like
, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
, glcNAc-T III
, GlcNAc-T III
, N-acetylglucosaminyltransferase III
, mannoside acetyl glucosaminyltransferase 3