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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.


N-acetylglucosaminyltransferase III, GnT-III, MGAT2, Mgat3
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: glycosyltransferase, CD45, ACID, CAN, HAD
Papers on N-acetylglucosaminyltransferase III
CSF N-glycoproteomics for early diagnosis in Alzheimer's disease.
Garozzo et al., Catania, Italy. In J Proteomics, Feb 2016
Previous studies specifically focused on the key role of glycosyltransferase GnT-III on AD-pathogenesis, addressing the patho-mechanism to specific sugar modification of BACE-1 glycoprotein with bisecting GlcNAc.
Bisecting GlcNAc modification stabilizes BACE1 protein under oxidative stress conditions.
Taniguchi et al., Wako, Japan. In Biochem J, Feb 2016
We have recently found that BACE1 is modified with bisecting N-acetylglucosamine (GlcNAc) by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene) and that GnT-III deficiency reduces Aβ-plaque formation in the brain by accelerating lysosomal degradation of BACE1.
Development of Highly Potent GAT1 Inhibitors: Synthesis of Nipecotic Acid Derivatives by Suzuki-Miyaura Cross-Coupling Reactions.
Wanner et al., Genova, Italy. In Chemmedchem, Jan 2016
Biological evaluation revealed several compounds that possess binding affinities and inhibitory potencies toward mGAT1, together with subtype selectivities against mGAT2-mGAT4 that were similar to or even higher than those for tiagabine.
Structural Changes in N-Glycans on Induced Pluripotent Stem Cells Differentiating Toward Cardiomyocytes.
Sawa et al., Suita, Japan. In Stem Cells Transl Med, Nov 2015
Expression of MGAT3, a glycosyltransferase-encoding gene that produces the bisecting GlcNAc structures, was higher in iPSCs and iPSC-CMs than in hCMCs.
Discovery of Selective Small Molecule Inhibitors of Monoacylglycerol Acyltransferase 3.
Ahn et al., Cambridge, United States. In J Med Chem, Oct 2015
Because the gene encoding MGAT3 (MOGAT3) is found only in higher mammals and humans, but not in rodents, a transgenic mouse model expressing the complete human MOGAT3 was used to characterize the effects of 6f in vivo.
Identification of 2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide (29) as an orally available MGAT2 inhibitor.
Sato et al., Saitama, Japan. In Bioorg Med Chem, Oct 2015
MGAT2 (monoacylglycerol acyltransferase 2) is expected to be an attractive target for the drug treatment of obesity, diabetes, and other disease.
Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics.
Kizuka et al., Wako, Japan. In Adv Cancer Res, 2014
These structures are enzymatic products of glycosyltransferases, GnT-V, GnT-III, and Fut8, respectively.
GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain.
Stanley et al., New York City, United States. In Elife, 2014
GnT1IP-L did not generate a FRET signal with MGAT2, MGAT3, MGAT4B or MGAT5 medial Golgi GlcNAc-tranferases.
RNA-seq analysis of glycosylation related gene expression in STZ-induced diabetic rat kidney inner medulla.
Chen et al., Atlanta, United States. In Front Physiol, 2014
In contrast, although highly expressed in kidney IM, the glycosyltransferase genes Mgat1, Mgat2, and fucosyltransferase Fut8, did not show any changes.
The bisecting GlcNAc in cell growth control and tumor progression.
Stanley et al., New York City, United States. In Glycoconj J, 2012
The bisecting GlcNAc is transferred to the core mannose residue of complex or hybrid N-glycans on glycoproteins by the β1,4-N-acetylglucosaminyltransferase III (GlcNAcT-III) or MGAT3.
Glycerolipid acyltransferases in triglyceride metabolism and energy homeostasis-potential as drug targets.
Hammond et al., Indianapolis, United States. In Endocr Metab Immune Disord Drug Targets, 2012
Monoacylglycerol and diacylglycerol acyltransferases (MGAT2 and DGAT1) are important enzymes involved in intestinal triglyceride absorption, and studies in recent years from knockout mice have revealed their important role in whole body energy metabolism through changes in intestinal TAG absorption kinetics.
Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor β1 (TGF-β1) in epithelial cell lines.
Gu et al., Sendai, Japan. In J Biol Chem, 2012
Roles of N-acetylglucosaminyltransferase III in epithelial-to-mesenchymal transition induced by transforming growth factor beta1 (TGF-beta1) in epithelial cell lines
Carbohydrate antigens.
Fukuzawa et al., Ōsaka, Japan. In Curr Opin Organ Transplant, 2012
To modify other carbohydrate antigen apart from α-Gal, only the overexpression of GnT-III appears to have an effect on the suppression of the N-linked sugar of non-Gal antigen.
The betaine-GABA transporter (BGT1, slc6a12) is predominantly expressed in the liver and at lower levels in the kidneys and at the brain surface.
Danbolt et al., Oslo, Norway. In Am J Physiol Renal Physiol, 2012
This study suggests that BGT1 plays its main role in the liver, thereby complementing other betaine-transporting carrier proteins (e.g., slc6a20) that are predominantly expressed in the small intestine or kidney rather than the liver.
Loss and recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation is a mechanism involved in epithelial-mesenchymal-epithelial transitions.
Oliveira et al., Porto, Portugal. In Plos One, 2011
Mgat3 glycogene expression and GnT-III-mediated glycosylation, specifically on E-cadherin, is a novel and major component of the Epithelial-Mesenchymal-Transition and the reverted process, Mesenchymal-Epithelial-Transition mechanism.
MGAT2 deficiency ameliorates high-fat diet-induced obesity and insulin resistance by inhibiting intestinal fat absorption in mice.
Oku et al., Toda, Japan. In Lipids Health Dis, 2011
The results suggest that MGAT2 has a pivotal role in lipid metabolism in the small intestine, and the inhibition of MGAT2 activity may be a promising strategy for the treatment of obesity-related metabolic disorders.
Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics.
Korekane et al., Nehe, China. In Bmb Rep, 2011
This mini-review describes some of our recent studies on a functional glycomics approach to the study of branched N-glycans produced by N-acetylglucosaminyltransferases III, IV, V and IX (Vb) (GnT-III, GnT-IV, V and IX (Vb)) and fucosyltransferase 8 (Fut8) and their patho-physiological significance, with emphasis on the importance of a systems glycobiology approach as a future perspective for glycobiology.
Deletion of the betaine-GABA transporter (BGT1; slc6a12) gene does not affect seizure thresholds of adult mice.
Danbolt et al., Oslo, Norway. In Epilepsy Res, 2011
Mice lacking exons 3-5 of the BGT1 gene have normal development & show seizure susceptibility indistinguishable from wild-type in a variety of seizure threshold models. This does not support a role for BGT1 in the control of seizure susceptibility.
Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.
Farese et al., San Francisco, United States. In Nat Med, 2009
Mogat2 is a key determinant of energy metabolism in response to dietary fat and suggest that inhibition or deletion of this enzyme may prove to be a useful strategy for treating obesity.
Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity.
Bailey et al., Zürich, Switzerland. In Nat Biotechnol, 1999
The glycosylation pattern of chCE7, an antineuroblastoma chimeric IgG1, was engineered in Chinese hamster ovary cells with tetracycline-regulated expression of beta(1,4)-N-acetylglucosaminyltransferase III (GnTIII), a glycosyltransferase catalyzing formation of bisected oligosaccharides that have been implicated in antibody-dependent cellular cytotoxicity (ADCC).
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