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

Xylosyltransferase II

XT-II, XT2, XYLT2, xylosyltransferase II, SLC6A18, XYLT-II
The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, STEP, HAD, fibrillin-1
Papers on XT-II
Xylan-degrading enzymes from Aspergillus terreus: Physicochemical features and functional studies on hydrolysis of cellulose pulp.
New
Ferreira Filho et al., Brasília, Brazil. In Carbohydr Polym, Jan 2016
Two endo-β-1,4-xylanases named XylT1 and XylT2, previously purified from Aspergillus terreus, were structurally investigated by fluorescence quenching and characterized with respect to their binding properties with phenolic compounds.
UV irradiation-induced production of monoglycosylated biglycan through downregulation of xylosyltransferase 1 in cultured human dermal fibroblasts.
New
Chung et al., Seoul, South Korea. In J Dermatol Sci, Jul 2015
UV-mediated reduction of XYLT1 expression was much stronger than that of XYLT2.
Homozygosity for frameshift mutations in XYLT2 result in a spondylo-ocular syndrome with bone fragility, cataracts, and hearing defects.
New
Hinsdale et al., Westmead, Australia. In Am J Hum Genet, Jul 2015
Whole exome sequence analyses showed that both individuals had a homozygous c.692dup mutation (GenBank: NM_022167.3) in the xylosyltransferase II locus (XYLT2) (MIM: 608125), causing reduced XYLT2 mRNA and low circulating xylosyltransferase (XylT) activity.
Xylosyltransferase II is the predominant isoenzyme which is responsible for the steady-state level of xylosyltransferase activity in human serum.
New
Hendig et al., Bad Oeynhausen, Germany. In Biochem Biophys Res Commun, May 2015
Both xylosyltransferases I and II (XT-I and XT-II) catalyze the transfer of xylose from UDP-xylose to select serine residues in the proteoglycan core protein.
Identification and characterization of human xylosyltransferase II promoter single nucleotide variants.
New
Hendig et al., Bad Oeynhausen, Germany. In Biochem Biophys Res Commun, Apr 2015
The human isoenzymes xylosyltransferase-I and -II (XT-I, XT-II) catalyze the rate-limiting step in proteoglycan biosynthesis.
Blood cells transcriptomics as source of potential biomarkers of articular health improvement: effects of oral intake of a rooster combs extract rich in hyaluronic acid.
Palou et al., Palma, Spain. In Genes Nutr, 2014
Among them, a reduced gene expression of glucuronidase-beta (GUSB), matrix metallopeptidase 23B (MMP23B), xylosyltransferase II (XYLT2), and heparan sulfate 6-O-sulfotransferase 1 (HS6ST1) was found in the supplemented group.
Effects of sesamin on the biosynthesis of chondroitin sulfate proteoglycans in human articular chondrocytes in primary culture.
Kongtawelert et al., Chiang Mai, Thailand. In Glycoconj J, 2014
Real-time-quantitative PCR showed that sesamin promoted the expression of the genes encoding the core protein (ACAN) of the major CS-PG aggrecan and the biosynthetic enzymes (XYLT1, XYLT2, CHSY1 and CHPF) required for the synthesis of CS-GAG side chains.
The missing "link": an autosomal recessive short stature syndrome caused by a hypofunctional XYLT1 mutation.
Ozkinay et al., Köln, Germany. In Hum Genet, 2014
Defects in the enzymes catalyzing steps two to four of the linker chain synthesis have been shown to cause autosomal recessive human phenotypes while no mutation has yet been reported in humans for the xylosyltransferases 1 and 2 (XT1 and XT2), the initiating enzymes in the linker chain formation.
Novel candidate genes putatively involved in stress fracture predisposition detected by whole-exome sequencing.
Atzmon et al., Israel. In Genet Res (camb), 2013
Of these, three missense mutations (rs7426114, rs4073918, rs3752135 in the NEB, SLC6A18 and SIGLEC12 genes, respectively) and three synonymous mutations (rs2071856, rs2515941, rs716745 in the ELFN2, GRK4, LRRC55 genes) displayed significant different rates in SF cases compared with controls.
A genomewide association study of smoking relapse in four European population-based samples.
Grabe et al., Verona, Italy. In Psychiatr Genet, 2013
A single-nucleotide polymorphism rs1008509, within the Xylosyltransferase II (XYLT2) gene, was suggestively associated with smoking relapse in the discovery phase (β=-0.504;
Human xylosyltransferase-I - a new marker for myofibroblast differentiation in skin fibrosis.
Hendig et al., Bad Oeynhausen, Germany. In Biochem Biophys Res Commun, 2013
In contrast, XYLT2 expression was only marginally affected by TGF-β1 as well as ALK5 inhibition.
Sensory quality of selected raw ripened meat products.
Barwińska et al., Kraków, Poland. In Acta Sci Pol Technol Aliment, 2013
The analysis was conducted in compliance with Polish Standards, and the cutting strength was measured with the use of the TA-XT2 texture-meter.
Association study: SLC6A18 gene and myocardial infarction.
GeneRIF
Aoi et al., Tokyo, Japan. In Clin Biochem, 2011
These results suggest that SLC6A18 or neighboring genes are associated with increased susceptibility to myocardial infarction.
Xylosyltransferase II is a significant contributor of circulating xylosyltransferase levels and platelets constitute an important source of xylosyltransferase in serum.
GeneRIF
Hinsdale et al., Stillwater, United States. In Glycobiology, 2009
the data from Xylt2 knock-out mice and mice with liver neoplasia show that liver is a significant source of serum XylT2 activity.
Orphan transporter SLC6A18 is renal neutral amino acid transporter B0AT3.
GeneRIF
Verrey et al., Zürich, Switzerland. In J Biol Chem, 2009
In contrast to its association with ACE2 observed in Xenopus oocytes, experiments with ace2 and collectrin null mice demonstrate that in vivo it is Collectrin, a smaller homologue of ACE2, that is required for functional expression of XT2 in kidney.
Analysis of xylosyltransferase II binding to the anticoagulant heparin.
GeneRIF
Götting et al., Bad Oeynhausen, Germany. In Biochem Biophys Res Commun, 2009
A protein sequence alignment and polarity plot of XylT-I and XylT-II revealed several Cardin-Weintraub motifs and charged surface clusters, which might be involved in electrostatic-mediated heparin-binding.
Kidney amino acid transport.
Review
Camargo et al., Zürich, Switzerland. In Pflugers Arch, 2009
A new finding is that the luminal Na(+)-dependent neutral amino acid transporters of the SLC6 family require an associated protein for their surface expression as shown for the Hartnup transporter B(0)AT1 (SLC6A19) and suggested for the L: -proline transporter SIT1 (IMINO(B), SLC6A20) and for B(0)AT3 (XT2, SLC6A18).
Xylosyltransferase gene variants and their role in essential hypertension.
GeneRIF
Götting et al., Bad Oeynhausen, Germany. In Am J Hypertens, 2009
The deviation from Hardy-Weinberg equilibrium of two XYLT2 variants might be due to gene-phenotype associations which remain to be explored, as well as the possibility of gene-gene interactions.
Human xylosyltransferases in health and disease.
Review
Kleesiek et al., Bad Oeynhausen, Germany. In Cell Mol Life Sci, 2007
The xylosyltransferases I and II (XT-I, XT-II, EC 2.4.2.26) catalyze the transfer of xylose from UDP-xylose to selected serine residues in the proteoglycan core protein, which is the initial and ratelimiting step in glycosaminoglycan biosynthesis.
The never-ending story of peptide O-xylosyltransferase.
Review
Wilson, Vienna, Austria. In Cell Mol Life Sci, 2004
In a journey lasting 40 years from the first reports on its activity in the 1960s to its purification and the cloning of relevant complementary DNAs, peptide O-xylosyltransferase has finally arrived at the same point as many other enzymes.
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