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ST6 beta-galactosamide alpha-2,6-sialyltranferase 1

sialyltransferase, ST6Gal I
This gene encodes a member of glycosyltransferase family 29. The encoded protein is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The protein, which is normally found in the Golgi but can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CD75, and CD76. This gene has been incorrectly referred to as CD75. Three transcript variants encoding two different isoforms have been described. [provided by RefSeq, Aug 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, CD45, HAD, glycosyltransferase
Papers on sialyltransferase
Sialic acids in cancer biology and immunity.
Läubli et al., Basel, Switzerland. In Glycobiology, Feb 2016
These changes have been shown to be the result of altered sialyltransferase and sialidase expression.
Comparative analyses of the lipooligosaccharides from nontypeable Haemophilus influenzae and Haemophilus haemolyticus show differences in sialic acid and phosphorylcholine modifications.
Apicella et al., Novato, United States. In Infect Immun, Feb 2016
Genomic analyses of ten strains demonstrated that H. haemolyticus lacked the sialyltransferase genes lic3A and lic3B (9/10) and siaA (10/10) but all strains contained the sialic acid uptake genes siaP and siaT (10/10).
Sialyltransferase inhibition and recent advances.
Sun et al., Harbin, China. In Biochim Biophys Acta, Jan 2016
Elevated sialyltransferase activity leads to overexpression of cell surface sialic acids and contributes to many disease developments, such as cancer and inflammation.
Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer.
Reis et al., Porto, Portugal. In Biochim Biophys Acta, Jan 2016
METHODS: MKN45 gastric carcinoma cells transfected with the sialyltransferase ST3GAL4 were established as a model overexpressing sialylated terminal glycans.
Sialylation: an Avenue to Target Cancer Cells.
Patel et al., Ahmadābād, India. In Pathol Oncol Res, Jan 2016
The alterations in sialylation is accompanied by changes in sialic acid, sialidase activity, sialyltransferase (ST) activity or sialoproteins.
Computational characterisation of the interactions between human ST6Gal I and transition-state analogue inhibitors: insights for inhibitor design.
Yu et al., Wollongong, Australia. In J Mol Recognit, Jan 2016
UNASSIGNED: Human β-galactoside α-2,6-sialyltransferase I (hST6Gal I) catalyses the synthesis of sialylated glycoconjugates involved in cell-cell interactions.
Significance of β-Galactoside α2,6 Sialyltranferase 1 in Cancers.
Gu et al., Sendai, Japan. In Molecules, 2014
However, the increased α2,6 sialylation catalyzed by β-galactoside α2,6 sialyltranferase 1 (ST6Gal I) is frequently observed in many types of the cancers.
Sweet role of platelet endothelial cell adhesion molecule in understanding angiogenesis.
Taniguchi et al., Saitama, Japan. In Glycobiology, 2014
In endothelial cells that lack α2,6-sialic acid because of sialyltransferase ST6Gal I deficiency, impairment of the homophilic PECAM interaction and PECAM-dependent cell survival signaling is observed.
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.
High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension.
Barb et al., United States. In J Vis Exp, 2014
These proteins are the human FcγRIIIa and the rat α2-6 sialyltransferase, ST6GalI, both expressed with an N-terminal GFP fusion, as well as the unmodified human immunoglobulin G1 Fc.
Virus entry. Lassa virus entry requires a trigger-induced receptor switch.
Brummelkamp et al., Amsterdam, Netherlands. In Science, 2014
Iterative haploid screens revealed that the sialyltransferase ST3GAL4 was required for the interaction of the virus glycoprotein with LAMP1.
Anti-inflammatory IgG production requires functional P1 promoter in β-galactoside α2,6-sialyltransferase 1 (ST6Gal-1) gene.
Lau et al., Buffalo, United States. In J Biol Chem, 2012
Data indicate that the P1 promoter of the ST6Gal-1 gene is critical for Fc sialylation.
Disulphide linkage in mouse ST6Gal-I: determination of linkage positions and mutant analysis.
Tsuji et al., Hiratsuka, Japan. In J Biochem, 2012
the loci of disulphide linkages in ST6Gal-I differ from those in ST3Gal I, suggesting that the linkage specificity of sialyltransferase may results from significant structural differences, including the loci of disulphide linkages (ST6Gal-I)
Cleavage of ST6Gal I by radiation-induced BACE1 inhibits golgi-anchored ST6Gal I-mediated sialylation of integrin β1 and migration in colon cancer cells.
Lee et al., Seoul, South Korea. In Radiat Oncol, 2011
Our results suggest that soluble ST6Gal may participate in cancer progression and metastasis prior to being secreted from cancer cells
ST6Gal-I regulates macrophage apoptosis via α2-6 sialylation of the TNFR1 death receptor.
Bellis et al., Birmingham, United States. In J Biol Chem, 2011
ST6Gal-I regulates macrophage apoptosis via alpha2-6 sialylation of the TNFR1 death receptor.
Disease-free survival of colorectal cancer patients in relation to CDw75 antigen expression.
Fernández-Briera et al., Vigo, Spain. In Pathobiology, 2010
CDw75 expression in colorectal tumoural tissue was correlated with growth pattern (p = 0.044), Dukes stage (p = 0.002), TNM stage (p = 0.020) and distant metastasis (p = 0.005).
Genes that mediate breast cancer metastasis to the brain.
Massagué et al., New York City, United States. In Nature, 2009
Gene expression analysis of these cells and of clinical samples, coupled with functional analysis, identified the cyclooxygenase COX2 (also known as PTGS2), the epidermal growth factor receptor (EGFR) ligand HBEGF, and the alpha2,6-sialyltransferase ST6GALNAC5 as mediators of cancer cell passage through the blood-brain barrier.
Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling.
Paulson et al., Los Angeles, United States. In Nat Immunol, 2006
B cells deficient in the enzyme (ST6Gal I) that forms the CD22 ligand show suppressed BCR signaling.
Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-of-function mutation of GM3 synthase.
Crosby et al., London, United Kingdom. In Nat Genet, 2004
We sequenced genes in the region and identified a nonsense mutation in SIAT9, which is predicted to result in the premature termination of the GM3 synthase enzyme (also called lactosylceramide alpha-2,3 sialyltransferase).
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.
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