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ST3 beta-galactoside alpha-2,3-sialyltransferase 2

ST3Gal II, hST3Gal II, siat4b
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: sialyltransferase, ACID, HAD, CAN, POLYMERASE
Papers on ST3Gal II
A systematic analysis of acceptor specificity and reaction kinetics of five human α(2,3)sialyltransferases: Product inhibition studies illustrate reaction mechanism for ST3Gal-I.
Neelamegham et al., Buffalo, United States. In Biochem Biophys Res Commun, Feb 2016
The KM for ST3Gal-I and ST3Gal-II was 100 and 30-fold lower, respectively, for Type-III compared to Type-I acceptors.
Critical role of evolutionarily conserved glycosylation at Asn211 in the intracellular trafficking and activity of sialyltransferase ST3Gal-II.
Daniotti et al., Córdoba, Argentina. In Biochem J, Aug 2015
ST3Gal-II, a type II transmembrane protein, is the main mammalian sialyltransferase responsible for GD1a and GT1b ganglioside biosynthesis in brain.
Intrinsically de-sialylated CD103(+) CD8 T cells mediate beneficial anti-glioma immune responses.
Wheeler et al., Los Angeles, United States. In Cancer Immunol Immunother, 2014
Modulation of CD8 T cell sialic acid with neuraminidase and ST3Gal-II revealed de-sialylation was necessary and sufficient for promiscuous binding to and stimulation by tumor pMHC I.
Biosynthesis of the major brain gangliosides GD1a and GT1b.
Schnaar et al., Baltimore, United States. In Glycobiology, 2012
We conclude that the St3gal2 and St3gal3 gene products (ST3Gal-II and ST3Gal-III sialyltransferases) are largely responsible for ganglioside terminal α2-3 sialylation in the brain, synthesizing the major brain gangliosides GD1a and GT1b.
Characterization of cancer associated mucin type O-glycans using the exchange sialylation properties of mammalian sialyltransferase ST3Gal-II.
Matta et al., Buffalo, United States. In J Proteome Res, 2012
To this end, the present study demonstrates that the exchange sialylation property of mammalian ST3Gal-II can facilitate the labeling of mucin glycoproteins in cancer cells, tumor specimens, and glycoproteins in cancer sera.
Androgen-regulated transcriptional control of sialyltransferases in prostate cancer cells.
Kaneda et al., Ōsaka, Japan. In Plos One, 2011
The expression of ST3Gal II was constitutively activated in castration-resistant prostate cancer cell lines, PC3 and DU145, because of the hypomethylation of CpG island in its promoter.
Mammalian sialyltransferase ST3Gal-II: its exchange sialylation catalytic properties allow labeling of sialyl residues in mucin-type sialylated glycoproteins and specific gangliosides.
Matta et al., Buffalo, United States. In Biochemistry, 2011
Recently, we found that mammalian sialyltransferase ST3Gal-II can catalyze the formation of CMP-NeuAc from 5'-CMP in the presence of a donor containing the NeuAcα2,3Galβ1,3GalNAc unit [Chandrasekaran, E. V., et al. (2008) Biochemistry 47, 320-330].
Expression of gangliosides, GD1a, and sialyl paragloboside is regulated by NF-κB-dependent transcriptional control of α2,3-sialyltransferase I, II, and VI in human castration-resistant prostate cancer cells.
Kaneda et al., Ōsaka, Japan. In Int J Cancer, 2011
GD1a is synthesized from GM1 by α2,3 sialyltransferase (ST3Gal) I and mainly by ST3Gal II.
Inhibition of ganglioside GD1a synthesis suppresses the differentiation of human mesenchymal stem cells into osteoblasts.
Choo et al., Iksan, South Korea. In Dev Growth Differ, 2011
In this study, we investigated the regulatory role of ganglioside GD1a in the differentiation of osteoblasts from human mesenchymal stem cells (hMSCs) by using lentivirus-containing short hairpin (sh)RNA to knockdown ST3 β-galactoside α-2, 3-sialyltransferase 2 (ST3Gal II) mRNA expression.
Adult onset cardiac dilatation in a transgenic mouse line with Galβ1,3GalNAc α2,3-sialyltransferase II (ST3Gal-II) transgenes: a new model for dilated cardiomyopathy.
Matsuda et al., Ibaraki, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2010
Here, we report an adult onset cardiac dilatation in a transgenic mouse line with Galβ1,3GalNAc α2,3-sialyltransferase II (ST3Gal-II) transgenes.
Interferon-inducible factor 16 is a novel modulator of glucocorticoid action.
Donn et al., Manchester, United Kingdom. In Faseb J, 2010
Interferon-inducible protein 16 (IFI16), bone morphogenetic protein receptor type II (BMPRII), and regulator of G-protein signaling 14 (RGS14) increased Gc transactivation, whereas sialyltransferase 4B (SIAT4B) had a negative effect.
Chromosomal regions underlying noncoagulation of milk in Finnish Ayrshire cows.
Ojala et al., Helsinki, Finland. In Genetics, 2008
By scanning gene databases, we found two potential candidate genes: LOC538897, a nonspecific serine/threonine kinase on chromosome 2, and SIAT4B, a sialyltransferase catalyzing the last step of glycosylation of kappa-casein on chromosome 18.
The evolution of galactose alpha2,3-sialyltransferase: Ciona intestinalis ST3GAL I/II and Takifugu rubripes ST3GAL II sialylate Galbeta1,3GalNAc structures on glycoproteins but not glycolipids.
Tiralongo et al., Gold Coast, Australia. In Glycoconj J, 2008
We also report for the first time the characterization of a ST3Gal II gene from the bony fish Takifugu rubripes.
Promoter structure and transcriptional regulation of human beta-galactoside alpha2, 3-sialyltransferase genes.
Taniguchi, Tsukuba, Japan. In Curr Drug Targets, 2008
Multiple mRNA forms differing only in the 5'-untranslated regions have been identified in hST3Gal II, hST3Gal III, hST3Gal IV, hST3Gal V, and hST3Gal VI.
Reversible sialylation: synthesis of cytidine 5'-monophospho-N-acetylneuraminic acid from cytidine 5'-monophosphate with alpha2,3-sialyl O-glycan-, glycolipid-, and macromolecule-based donors yields diverse sialylated products.
Neelamegham et al., Buffalo, United States. In Biochemistry, 2008
Here we report another type of sialylation, termed reverse sialylation, catalyzed by mammalian sialyltransferase ST3Gal-II.
Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase.
Miyagi et al., Sendai, Japan. In J Biol Chem, 2003
ST3Gal II is a MSGb5 (stage-specific embryonic antigen-4) synthase and its increased expression level is closely related to renal carcinogenesis
Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene.
Matsumoto et al., Tsukuba, Japan. In Biochem Biophys Res Commun, 2003
Genomic structure, expression, and transcriptional regulation of ST3GALII.
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