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


ST6GALNAC2, ST6GalNAc II, hST6GalNAc II, SIATL1, sialyltransferase 7
ST6GALNAC2 belongs to a family of sialyltransferases that add sialic acids to the nonreducing ends of glycoconjugates. At the cell surface, these modifications have roles in cell-cell and cell-substrate interactions, bacterial adhesion, and protein targeting (Samyn-Petit et al., 2000 [PubMed 10742600]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: sialyltransferase, ACID, CAN, IgA, IgA1
Papers on ST6GALNAC2
Study of correlation between polymorphism of ST6GALNAC2 and susceptibility to IgA nephropathy.
Ma et al., Ürümqi, China. In Exp Ther Med, Jun 2015
UNASSIGNED: The aim of the present study was to explore the correlation between single nucleotide polymorphisms (SNPs) rs3840858 and rs2304921 in a specific α-2,6 sialyltransferase gene, ST6GALNAC2, and the susceptibility to immunoglobulin (IgA) nephropathy (IgAN).
N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.
Raska et al., Birmingham, United States. In Nephrol Dial Transplant, Feb 2015
Prior analyses of IgA1-producing cells had indicated that α2,6-sialyltransferase II (ST6GalNAc-II) is likely responsible for sialylation of GalNAc of galactose-deficient IgA1, but direct evidence is missing.
Phyllodes tumor of the breast: role of Axl and ST6GalNAcII in the development of mammary phyllodes tumors.
Zhao et al., Dalian, China. In Tumour Biol, 2014
The purpose of this study was to evaluate the implications of Axl and ST6GalNAcII in phyllodes tumors.
ST6GalNAcII mediates the invasive properties of breast carcinoma through PI3K/Akt/NF-κB signaling pathway.
Zhao et al., Dalian, China. In Iubmb Life, 2014
The objective of this study is to clarify the possible role and mechanism of ST6GalNAcII in the metastasis process of breast carcinoma.
An in vivo functional screen identifies ST6GalNAc2 sialyltransferase as a breast cancer metastasis suppressor.
Isacke et al., London, United Kingdom. In Cancer Discov, 2014
Using this approach, we identified the sialyltransferase ST6GalNAc2 as a novel breast cancer metastasis suppressor.
Cytokines alter IgA1 O-glycosylation by dysregulating C1GalT1 and ST6GalNAc-II enzymes.
Novak et al., Birmingham, United States. In J Biol Chem, 2014
These cytokines reduced galactosylation of the O-glycan substrate directly via decreased expression of the galactosyltransferase C1GalT1 and, indirectly, via increased expression of the sialyltransferase ST6GalNAc-II, which prevents galactosylation by C1GalT1.
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
However, ST8Sia-VI-based chimeric enzymes lost expression or activity when their sialylmotif L sequences were replaced with those of ST3Gal-I and ST6GalNAc-II, suggesting the existence of an ST8Sia family specific motif in the sialylmotif L. The ST8Sia-I- and ST8Sia-VI-based chimeric enzymes lost enzymatic activity when their sialylmotif S sequences were interchanged.
ST6GalNAc-I controls expression of sialyl-Tn antigen in gastrointestinal tissues.
Reis et al., Porto, Portugal. In Front Biosci (elite Ed), 2010
We have previously shown in vitro that ST6GalNAc-I and ST6GalNAc-II sialyltransferases can synthesize sialyl-Tn.
Glycomic and transcriptomic response of GSC11 glioblastoma stem cells to STAT3 phosphorylation inhibition and serum-induced differentiation.
Conrad et al., Tallahassee, United States. In J Proteome Res, 2010
In serum treated cells, an overall increase in glycosphingolipids may be due to increased expression of ST6GALNAC2, a sialyltransferase.
Interaction between variants of two glycosyltransferase genes in IgA nephropathy.
Wang et al., Beijing, China. In Kidney Int, 2009
potential genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1 O-glycosylation, disease predisposition, and disease severity, and may contribute to the polygenic nature of IgA nephropathy
Activity of alpha2,6-sialyltransferase and its gene expression in peripheral B lymphocytes in patients with IgA nephropathy.
Wang et al., Beijing, China. In Scand J Immunol, 2009
reduced sialylation of serum IgA1 may result from decreased expression of ST6GALNAC2.
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
A down-regulation of C2GnT1 mRNA and enzymatic activity was observed with a concurrent up-regulation of ST3Gal I and ST6GalNAc II mRNA resulting in a loss of the core 2 structures required for sLe(x) expression as a P-selectin ligand.
Variants of the ST6GALNAC2 promoter influence transcriptional activity and contribute to genetic susceptibility to IgA nephropathy.
Wang et al., Beijing, China. In Hum Mutat, 2007
the ADG haplotype in the ST6GALNAC2 gene is a functional regulatory variant that may contribute to the genetic susceptibility in a subset of patients in whom the desialylation of IgA1 molecules was the main causative pathogenesis of IgAN
Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells.
Novak et al., Birmingham, United States. In J Mol Biol, 2007
Expression of the ST6-GalNAcII gene and activity of the CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase were higher in immunoglobulinA1-producing cell lines.
The ST6GalNAc-I sialyltransferase localizes throughout the Golgi and is responsible for the synthesis of the tumor-associated sialyl-Tn O-glycan in human breast cancer.
Taylor-Papadimitriou et al., London, United Kingdom. In J Biol Chem, 2006
Endogenous or exogenous expression of hST6GalNAc-I (but not ST6GalNAc-II) always results in the expression of sialyl-Tn.
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