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ST3 beta-galactoside alpha-2,3-sialyltransferase 1

ST3Gal I
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. Correct glycosylation of the encoded protein may be critical to its sialyltransferase activity. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4B. Two transcript variants encoding the same protein have been found for this gene. Other transcript variants may exist, but have not been fully characterized yet. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: sialyltransferase, ACID, CAN, HAD, POLYMERASE
Papers using ST3Gal I antibodies
Delineation of the minimal catalytic domain of human Galbeta1-3GalNAc alpha2, 3-sialyltransferase (hST3Gal I)
Burchell Joy et al., In Glycobiology, 2000
... A 2.5-kb Sal I-Sca I fragment containing the MUC1 promoter fused to ST3Gal-I was purified (Qiagen kit) and dissolved in ...
Papers on ST3Gal I
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 results demonstrate human ST3Gal-I catalysis towards Type-III and Core-2 acceptors with KM = 5-50 μM and high VMax values.
Integrative view of α2,3-sialyltransferases (ST3Gal) molecular and functional evolution in deuterostomes: significance of lineage-specific losses.
Harduin-Lepers et al., Limoges, France. In Mol Biol Evol, Apr 2015
In this work, we reconstructed the evolutionary history of the metazoan α2,3-sialyltransferases family (ST3Gal), a subset of sialyltransferases encompassing six subfamilies (ST3Gal I-ST3Gal VI) functionally characterized in mammals.
Expression of ST3Gal, ST6Gal, ST6GalNAc and ST8Sia in human hepatic carcinoma cell lines, HepG-2 and SMMC-7721 and normal hepatic cell line, L-02.
He et al., Shenyang, China. In Glycoconj J, Feb 2015
ST3Gal-IV and ST6Gal I were overexpressed and ST3Gal-I, ST3Gal-V, ST3Gal-VI, ST6GalNAcII and ST6GalNAcVI were downregulated in HepG-2 and SMMC-7721 cell Lines, compared with control cell line.
Development of Monoclonal Antibodies against CMP-N-Acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (ST3Gal-I) Recombinant Protein Expressed in E. coli.
Chugh et al., Mumbai, India. In Biochem Res Int, 2014
ST3Gal-I, a sialyltransferase, is known to play a crucial role in sialylation of T antigen in bladder cancer and it has reported elevated expression in breast carcinogenesis with increased tumor progression stages.
α2-3 Sialic acid glycoconjugate loss and its effect on infection with Toxoplasma parasites.
Ikehara et al., Obihiro, Japan. In Exp Parasitol, 2013
Sialyltransferase ST3Gal-I deficient mice (ST3Gal-I(-/-) mice) lost α2-3 sialic acid linkages in macrophages and spleen cells.
Effects of amino acid substitutions in the sialylmotifs on molecular expression and enzymatic activities of α2,8-sialyltransferases ST8Sia-I and ST8Sia-VI.
Tsuji et al., Wako, Japan. In Glycobiology, 2013
Mouse sialyltransferases are grouped into four families according to the type of carbohydrate linkage they synthesize: β-galactoside α2,3-sialyltransferases (ST3Gal-I-VI), β-galactoside α2,6-sialyltransferases (ST6Gal-I and ST6Gal-II), N-acetylgalactosamine α2,6-sialyltransferases (ST6GalNAc-I-VI) and α2,8-sialyltransferases (ST8Sia-I-VI).
Structure-based mutagenic analysis of mechanism and substrate specificity in mammalian glycosyltransferases: porcine ST3Gal-I.
Withers et al., Vancouver, Canada. In Glycobiology, 2013
Kinetic analyses of mutants of ST3Gal-I, in conjunction with structural studies, have confirmed the mechanistic roles of His302 and His319 as general acid and base catalysts, respectively, and have quantitated other interactions with the cytosine monophosphate-N-acetyl β-neuraminic acid donor substrate.
Cyclooxygenase-2 enzyme induces the expression of the α-2,3-sialyltransferase-3 (ST3Gal-I) in breast cancer.
Burchell et al., London, United Kingdom. In J Biol Chem, 2013
Using the breast cancer cell line T47D, we have shown that PGE2, one of the final products of the cyclooxygenase-2 (COX-2) pathway, can induce the mRNA expression of the sialyltransferase α-2,3-sialyltransferase-3 (ST3Gal-I), resulting in increased sialyltransferase activity, demonstrated by a reduction in PNA lectin staining.
Expression patterns of α2,3-sialyltransferase I and α2,6-sialyltransferase I in human cutaneous epithelial lesions.
Beltrão et al., Recife, Brazil. In Eur J Histochem, 2012
In this study, it was evaluated the expression of ST3Gal I and ST6Gal I in cutaneous epithelial lesions that include actinic keratosis (n=15), keratoacanthoma (n=9), squamous cell carcinoma (n=22) and basal cell carcinoma (n=28) in order to evaluate if sialyltransferases expression is different in premalignant and in malignant tumors.
MUC1 in human and murine mammary carcinoma cells decreases the expression of core 2 β1,6-N-acetylglucosaminyltransferase and β-galactoside α2,3-sialyltransferase.
Ugorski et al., Wrocław, Poland. In Glycobiology, 2012
As the observed changes in O-glycan synthesis can be associated with changes in the expression of specific glycosyltransferases, core 1 β1,3-galactosyltransferase, core 2 β1,6-N-acetylglucosaminyltransferase (C2GnT1) and β-galactoside α2,3-sialyltransferase (ST3Gal I), we studied their expression in parental, vector-transfected and MUC1-transfected MDA-MB-231 and 4T1 cells as well as T47D cells transduced with small hairpin RNA targeted MUC1 mRNA.
Androgen-regulated transcriptional control of sialyltransferases in prostate cancer cells.
Kaneda et al., Ōsaka, Japan. In Plos One, 2011
We previously demonstrated that GD1a production was high in castration-resistant prostate cancer cell lines, PC3 and DU145, mainly due to their high expression of β-galactoside α2,3-sialyltransferase (ST3Gal) II (not ST3Gal I), and the expression of both ST3Gals was regulated by NF-κB, mainly by RelB.
Over-expression of ST3Gal-I promotes mammary tumorigenesis.
Burchell et al., Canada. In Glycobiology, 2010
Over-expression of ST3Gal-I promotes mammary tumorigenesis.
Mutational analysis for enzyme activity of mouse Galbeta1,3GalNAc alpha2,3-sialyltransferase (mST3Gal I).
Lee et al., Pusan, South Korea. In Indian J Biochem Biophys, 2010
tryptophan and cysteine residues conserved in ST3Gal I are critical for its activity
ST3Gal.I sialyltransferase relevance in bladder cancer tissues and cell lines.
Dall'Olio et al., Lisbon, Portugal. In Bmc Cancer, 2008
ST3Gal.I plays the major role in the sialylation of the T antigen in bladder cancer.
Characterization of mouse sialyltransferase genes: their evolution and diversity.
Takashima, Wako, Japan. In Biosci Biotechnol Biochem, 2008
These sialyltransferases are grouped into four families according to the carbohydrate linkages they synthesize: beta-galactoside alpha2,3-sialyltransferases (ST3Gal I-VI), beta-galactoside alpha2,6-sialyltransferases (ST6Gal I and II), GalNAc alpha2,6-sialyltransferases (ST6GalNAc I-VI), and alpha2,8-sialyltransferases (ST8Sia I-VI).
Family-based association study of lithium-related and other candidate genes in bipolar disorder.
Sklar et al., Boston, United States. In Arch Gen Psychiatry, 2008
evidence of the association of bipolar disorder with SIAT4A was seen
Sialyl-Lewis(x) on P-selectin glycoprotein ligand-1 is regulated during differentiation and maturation of dendritic cells: a mechanism involving the glycosyltransferases C2GnT1 and ST3Gal I.
Burchell et al., London, United Kingdom. In J Immunol, 2007
regulation of O-glycosylation controls sLe(x) expression, and also suggest that O-glycans may have a function in dendritic cells migration
Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
Reinherz et al., Boston, United States. In Cell, 2001
We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase.
Inhibition of the glycosylation and alteration in the intracellular trafficking of mucins and other glycoproteins by GalNAcalpha-O-bn in mucosal cell lines: an effect mediated through the intracellular synthesis of complex GalNAcalpha-O-bn oligosaccharides.
Huet et al., Lille, France. In Front Biosci, 2001
The metabolic alterations are very important in HT-29 cell line, leading to a massive accumulation of GalNAcalpha-O-bn oligosaccharide derivatives and to a strong inhibition of the terminal elongation of O-glycans by alpha2,3 sialyltransferase ST3Gal I. GalNAcalpha-O-bn treatment also induced alterations at the cellular level, exhibiting a large scale in HT-29 cells, i.e. 1) an inhibition of mucin secretion, 2) a blockade in the targeting of some membrane glycoproteins (brush border glycoproteins such as dipeptidylpeptidase IV, carcinoembryonic antigen and the mucin-like glycoprotein MUC1, and the basolateral cell adhesion molecule CD44), 3) an inhibition in the processing of lysosomal enzymes.
The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis.
Marth et al., San Diego, United States. In Immunity, 2000
St3gal-1 functions to protect CD8 T cells from apoptosis
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