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    MGAT3 beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase [ Homo sapiens (human) ]

    Gene ID: 4248, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Suppression of MGAT3 expression and the epithelial-mesenchymal transition of lung cancer cells by miR-188-5p.

    Suppression of MGAT3 expression and the epithelial-mesenchymal transition of lung cancer cells by miR-188-5p.
    Niu H, Qu A, Guan C., Free PMC Article

    03/12/2022
    Associations between genetic variants of KIF5B, FMN1, and MGAT3 in the cadherin pathway and pancreatic cancer risk.

    Associations between genetic variants of KIF5B, FMN1, and MGAT3 in the cadherin pathway and pancreatic cancer risk.
    Zhao L, Liu H, Luo S, Moorman PG, Walsh KM, Li W, Wei Q., Free PMC Article

    08/7/2021
    Study found that N-Acetylglucosaminyltransferase III (GnT-III) is expressed in trophoblasts during normal human pregnancy and is involved in regulating trophoblast function.

    Expression of N-Acetylglucosaminyltransferase III Promotes Trophoblast Invasion and Migration in Early Human Placenta.
    Deng Q, Liu X, Yang Z, Xie L.

    05/23/2020
    The expression of GnT-III in placenta suggests a role for GnT-III in the regulation of tropho- blast behavior. And decreased expression of GnT-III is associated with oxidative stress in preeclamptic pla- centas and, thus, may be involved in the pathogenesis of preeclampsia.

    Downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition.
    Deng Q, Yin N, Chen Y, Shan N, Liu X, Qi H.

    10/19/2019
    Results strongly indicate that the MGAT3 and BACH2 genes play an important role in IBD pathogenesis and suggest a possible disease pathway mediated by the pro-inflammatory properties of IgG antibodies acquired by alterations in Fc glycosylation.

    Promoter methylation of the MGAT3 and BACH2 genes correlates with the composition of the immunoglobulin G glycome in inflammatory bowel disease.
    Klasić M, Markulin D, Vojta A, Samaržija I, Biruš I, Dobrinić P, Ventham NT, Trbojević-Akmačić I, Šimurina M, Štambuk J, Razdorov G, Kennedy NA, Satsangi J, Dias AM, Pinho S, Annese V, Latiano A, D'Inca R, IBD consortium, Lauc G, Zoldoš V., Free PMC Article

    05/25/2019
    Novel insights into the epigenetic regulation of MGAT3/bisecting GlcNAc and demonstrate the importance of N-glycosylation in cancer progression.

    Epigenetic activation of MGAT3 and corresponding bisecting GlcNAc shortens the survival of cancer patients.
    Kohler RS, Anugraham M, López MN, Xiao C, Schoetzau A, Hettich T, Schlotterbeck G, Fedier A, Jacob F, Heinzelmann-Schwarz V., Free PMC Article

    02/10/2018
    Data suggest that GNT-III expression regulates levels/activation of the heavily glycosylated Notch receptor involved in normal and malignant cell development; suppression of GNT-III in epithelial ovarian carcinoma cell lines results in down-regulation of Notch signaling that is more potent than pharmacologic blockage of Notch activation.

    The glycosyltransferase GnT-III activates Notch signaling and drives stem cell expansion to promote the growth and invasion of ovarian cancer.
    Allam H, Johnson BP, Zhang M, Lu Z, Cannon MJ, Abbott KL., Free PMC Article

    10/21/2017
    MGAT3 expressed in cells stimulates lipid droplet growth. These findings provide additional evidence that MGAT3 likely functions as a triacylglycerol synthase in cells.

    Biochemical characterization of human acyl coenzyme A: 2-monoacylglycerol acyltransferase-3 (MGAT3).
    Brandt C, McFie PJ, Stone SJ.

    05/13/2017
    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

    DNA hypomethylation upregulates expression of the MGAT3 gene in HepG2 cells and leads to changes in N-glycosylation of secreted glycoproteins.
    Klasić M, Krištić J, Korać P, Horvat T, Markulin D, Vojta A, Reiding KR, Wuhrer M, Lauc G, Zoldoš V., Free PMC Article

    04/8/2017
    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.

    Expression of N-Acetylglucosaminyltransferase III Suppresses α2,3-Sialylation, and Its Distinctive Functions in Cell Migration Are Attributed to α2,6-Sialylation Levels.
    Lu J, Isaji T, Im S, Fukuda T, Kameyama A, Gu J., Free PMC Article

    08/6/2016
    Mgat3 plays an important role in early spontaneous miscarriage in humans.

    Altered β1,6-GlcNAc and bisecting GlcNAc-branched N-glycan on integrin β1 are associated with early spontaneous miscarriage in humans.
    Zhang M, Wang M, Gao R, Liu X, Chen X, Geng Y, Ding Y, Wang Y, He J.

    06/28/2016
    MGAT3 protein and gene expression in in uveal and cutaneous melanoma cells

    Diverse expression of N-acetylglucosaminyltransferase V and complex-type β1,6-branched N-glycans in uveal and cutaneous melanoma cells.
    Pocheć E, Rydlewska M, Przybyło M, Lityńska A.

    04/30/2016
    HS5 cells had significantly enhanced levels of bisecting N-glycans (catalyzed by MGAT3 whereas HS27a cells had enhanced levels of Galbeta1,4GlcNAc.

    Quantitative analysis of glycans, related genes, and proteins in two human bone marrow stromal cell lines using an integrated strategy.
    Li X, Li D, Pang X, Yang G, Deeg HJ, Guan F., Free PMC Article

    11/21/2015
    functional characterization of N-acetylglucosaminyltransferases III and V in human melanoma cells

    Overexpression of N-acetylglucosaminyltransferases III and V in human melanoma cells. Implications for MCAM N-glycosylation.
    Bubka M, Link-Lenczowski P, Janik M, Pocheć E, Lityńska A.

    02/7/2015
    GnT-III determines E-cadherin-mediated tumor suppression, and GnT-V regulates E-cadherin-mediated tumor invasion.

    E-cadherin and adherens-junctions stability in gastric carcinoma: functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V.
    Pinho SS, Figueiredo J, Cabral J, Carvalho S, Dourado J, Magalhães A, Gärtner F, Mendonfa AM, Isaji T, Gu J, Carneiro F, Seruca R, Taniguchi N, Reis CA.

    06/22/2013
    Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines

    Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines.
    Xu Q, Isaji T, Lu Y, Gu W, Kondo M, Fukuda T, Du Y, Gu J., Free PMC Article

    07/14/2012
    MGAT3 mRNA biomarker may characterize subgroups of Alzheimer's disease patients with different disease progression.

    MGAT3 mRNA: a biomarker for prognosis and therapy of Alzheimer's disease by vitamin D and curcuminoids.
    Fiala M, Mahanian M, Rosenthal M, Mizwicki MT, Tse E, Cho T, Sayre J, Weitzman R, Porter V.

    06/9/2012
    the modulation of glycosyltransferases MGAT3 and MGAT5 by synthetic N-acetyl-D-glucosamine-calix[4]arene correlated with the improvement of NK cell effector functions and the augmentation of tumor cells sensitivity to NK cell-mediated cytotoxicity.

    Glycosylation regulates NK cell-mediated effector function through PI3K pathway.
    Benson V, Grobarova V, Richter J, Fiserova A.

    06/28/2010
    upregulation of GnT-III in AD brains may represent an adaptive response to protect them from additional beta-amyloid production

    Protective effect of N-glycan bisecting GlcNAc residues on beta-amyloid production in Alzheimer's disease.
    Akasaka-Manya K, Manya H, Sakurai Y, Wojczyk BS, Kozutsumi Y, Saito Y, Taniguchi N, Murayama S, Spitalnik SL, Endo T.

    03/15/2010
    MGAT3 and MGAT5 competitively modified E-cadherin N-glycans.

    The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin.
    Pinho SS, Reis CA, Paredes J, Magalhães AM, Ferreira AC, Figueiredo J, Xiaogang W, Carneiro F, Gärtner F, Seruca R.

    01/21/2010
    An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.

    An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.
    Sato Y, Isaji T, Tajiri M, Yoshida-Yamamoto S, Yoshinaka T, Somehara T, Fukuda T, Wada Y, Gu J., Free PMC Article

    01/21/2010
    beta1,4-N-acetylglucosaminyltransferase III inhibits the function of alpha5beta1 integrin

    Introduction of bisecting GlcNAc into integrin alpha5beta1 reduces ligand binding and down-regulates cell adhesion and cell migration.
    Isaji T, Gu J, Nishiuchi R, Zhao Y, Takahashi M, Miyoshi E, Honke K, Sekiguchi K, Taniguchi N.

    01/21/2010
    down-regulation of hydrogen peroxide-induced PKC delta activation in cells transfected with this enzyme

    Down-regulation of hydrogen peroxide-induced PKC delta activation in N-acetylglucosaminyltransferase III-transfected HeLaS3 cells.
    Shibukawa Y, Takahashi M, Laffont I, Honke K, Taniguchi N.

    01/21/2010
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