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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2

beta3GnT, beta3Gn-T1
This gene encodes a member of the beta-1,3-N-acetylglucosaminyltransferase family. This enzyme is a type II transmembrane protein. It prefers the substrate of lacto-N-neotetraose, and is involved in the biosynthesis of poly-N-acetyllactosamine chains. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, NAC, putative type-2 membrane protein, carboxypeptidase D, fucosyltransferase
Papers on beta3GnT
Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-acetyllactosamine chains in differentiated HL-60 cells.
Yamashita et al., Yokohama, Japan. In J Biol Chem, 2008
up-regulation of beta3Gn-T8 in differentiated cells increases poly-N-acetyllactosamine chains by activating intrinsic beta3Gn-T2.
Construction of a cysteine protease deficient Bombyx mori multiple nucleopolyhedrovirus bacmid and its application to improve expression of a fusion protein.
Park et al., Shizuoka, Japan. In J Virol Methods, 2007
By using this system, a GFP(uv)-beta1,3-N-acetylglucosaminyltransferase 2 (GFP(uv)-beta3GnT2) fusion protein was successfully expressed in silkworm larvae with less protein degradation and without larvae liquefaction; beta3GnT activity improved 30%.
Specific expression of GFPuv-beta1,3-N-acetylglucosaminyltransferase 2 fusion protein in fat body of Bombyx mori silkworm larvae using signal peptide.
Park et al., Shizuoka, Japan. In Biochem Biophys Res Commun, 2007
Ninety-four percent of total intracellular beta1,3-N-acetylglucosaminyltransferase (beta3GnT) activity was detected in cell precipitations following the 600, 8000, and 114,000g centrifugations.
Enhanced production of secretory beta1,3-N-acetylglucosaminyltransferase 2 fusion protein into hemolymph of Bombyx mori larvae using recombinant BmNPV bacmid integrated signal sequence.
Kato et al., Shizuoka, Japan. In J Biotechnol, 2007
When the BmNPV bacmid encoding the signal sequences from the silkworm B. mori bombyxin (bx) and B. mori prophenoloxidase-activating enzyme (ppae) was injected into silkworm larvae, 56.1 and 51.5mU/ml beta3GnT, respectively, were secreted into the hemolymph of silkworm larvae.
Application of a radial-flow bioreactor in the production of beta1,3-N-acetylglucosaminyltransferase-2 fused with GFPuv using stably transformed insect cell lines.
Park et al., Shizuoka, Japan. In Biotechnol Appl Biochem, 2005
An RFB (radial-flow bioreactor) with a reactor volume of 5 ml was applied to produce human beta3GnT (beta1,3-N-acetylglucosaminyltransferase) using two stably transformed insect cell lines.
The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
Park et al., Shizuoka, Japan. In Biochem Biophys Res Commun, 2005
The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
Improvement of the production of GFPuv-beta1,3-N-acetylglucosaminyltransferase 2 fusion protein using a molecular chaperone-assisted insect-cell-based expression system.
Park et al., Shizuoka, Japan. In Biotechnol Bioeng, 2005
On the other hand, the co-expression system produced an extracellular beta3GnT activity of 22-23 mU/mL, which was approximately 3.5- and 11-fold higher than those of the stable expression of the fusion gene without the chaperone and the conventional BES with the addition of protease, respectively.
Characterization of a cDNA encoding a protein with limited similarity to beta1, 3-N-acetylglucosaminyltransferase.
Mao et al., Shanghai, China. In Mol Biol Rep, 2004
beta1, 3-N-acetylglucosaminyltransferase is similar to a new protein, beta3-GnTL1
Comparative analysis of GFP(UV)-beta1,3-N-acetylglucosaminyltransferase 2 production in two insect-cell-based expression systems.
Park et al., Shizuoka, Japan. In Protein Expr Purif, 2004
The difference between the maximal beta3GnT activities of the isolates studied was considered to be due to the presence of a copy number of the fusion gene, as determined on the basis of the results of Southern blot analysis.
Suppression of beta 1,3galactosyltransferase beta 3Gal-T5 in cancer cells reduces sialyl-Lewis a and enhances poly N-acetyllactosamines and sialyl-Lewis x on O-glycans.
Trinchera et al., Varese, Italy. In Eur J Biochem, 2004
beta 3Gal-T5 plays a relevant role in gastrointestinal and pancreatic tissues counteracting the glycosylation pattern associated with malignancy
Association between expression levels of CA 19-9 and N-acetylglucosamine-beta;1,3-galactosyltransferase 5 gene in human pancreatic cancer tissue.
Monden et al., Ōsaka, Japan. In Pathobiology, 2003
beta3Gal-T5 is presumed to be responsible for the synthesis of CA 19-9 in pancreatic cancer tissue.
Different glycosyltransferases are differentially processed for secretion, dimerization, and autoglycosylation.
Fukuda et al., Marseille, France. In Glycobiology, 2003
To better understand these processes, six glycosyltransferases were selected on the basis of the donor sugars, including two N-acetylglucosaminyltransferases, core 1 beta1,3-N-acetylglucosaminyltransferase (C1-beta3GnT) and core 2 beta1,6-N-acetylglucosaminyltransferase (C2GnT-I); two fucosyltransferases, alpha1,2-fucosyltransferase-I (FucT-I) and alpha1,3-fucosyltransferase-VII (FucT-VII); and two sialyltransferases, alpha2,3-sialyltransferase-I (ST3Gal-I) and alpha2,6-sialyltransferase-I (ST6Gal-I).
Lewis type 1 antigen synthase (beta3Gal-T5) is transcriptionally regulated by homeoproteins.
Narimatsu et al., Hachiōji, Japan. In J Biol Chem, 2003
beta3Gal-T5, controlled by the intestinal homeoproteins, may play an important role in the specific function of intestinal cells by modifying the carbohydrate structure of glycoproteins
Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family.
Sasaki et al., Machida, Japan. In J Biol Chem, 2001
We have isolated three types of cDNAs encoding novel beta1,3-N-acetylglucosaminyltransferases (designated beta3Gn-T2, -T3, and -T4) from human gastric mucosa and the neuroblastoma cell line SK-N-MC.
Molecular cloning and expression analysis of a mouse UDP-GlcNAc:Gal(beta1-4)Glc(NAc)-R beta1,3-N-acetylglucosaminyltransferase homologous to Drosophila melanogaster Brainiac and the beta1,3-galactosyltransferase family.
Schachter et al., Toronto, Canada. In Glycoconj J, 2000
We have isolated a murine cDNA coding for a beta1,3-N-acetylglucosaminyltransferase enzyme ( beta3GnT).
A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to beta-1,3-galactosyltransferases.
Hennet et al., Zürich, Switzerland. In Proc Natl Acad Sci U S A, 1999
Human and mouse cDNAs encoding a new beta-1, 3-N-acetylglucosaminyltransferase (beta3GnT) have been isolated from fetal and newborn brain libraries.
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