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Buy GALNT3 elisa kit, Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3) ELISA Kit-NP_056551.2 (MBS9316705) product datasheet at MyBioSource, ELISA Kits

Human Polypeptide GalNAc transferase 10 ELISA Kit;Human GalNAc-T10 ELISA Kit;Human pp-GaNTase 10 ELISA Kit;Human Protein-UDP acetylgalactosaminyltransferase 10 ELISA Kit;Human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10 ELISA Kit;Human GALNACT10 ELISA Kit;Human PPGALNACT10 ELISA Kit;Human PPGANTASE10 ELISA Kit;Human polypeptide N-acetylgalactosaminyltransferase 10 ELISA Kit;Human GalNAc transferase 10 ELISA Kit;Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 10 (GalNAc-T10) ELISA Kit ...

Glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase (EC 2.4.1.174, N-acetylgalactosaminyltransferase I, glucuronylgalactosylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase I, UDP-N-acetyl-D-galactosamine:D-glucuronyl-1,3-beta-D-galactosyl-proteoglycan beta-1,4-N-acetylgalactosaminyltransferase) is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-(1->3)-D-galactosyl-proteoglycan ⇌ {\displaystyle \rightleftharpoons } UDP + N-acetyl-D-galactosaminyl-(1->4)-beta-D-glucuronyl-(1->3)-beta-D-galactosylproteoglycan This enzyme requires Mn2+. Rohrmann, K.; Niemann, R.; Buddecke, E. (1985). Two N-acetylgalactosaminyltransferases are involved in the biosynthesis of chondroitin sulfate. ...

This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin ...

Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3) (GALNT3), mRNA. (H00002591-R01) - Products - Abnova

In the field of biochemistry, O-linked glycosylation is the attachment of a sugar molecule to an oxygen atom in an amino acid residue in a protein. O-linked glycosylation is a form of glycosylation that occurs in the Golgi apparatus in eukaryotes. It also occurs in archaea and bacteria. O-linked glycosylation occurs at a later stage during protein processing, probably in the Golgi apparatus. This is the addition of N-acetyl-galactosamine to serine or threonine residues by the enzyme UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (EC number 2.4.1.41), followed by other carbohydrates (such as galactose and sialic acid). This process is important for certain types of proteins such as proteoglycans, which involves the addition of glycosaminoglycan chains to an initially unglycosylated proteoglycan core protein. These additions are usually serine O-linked glycoproteins, which seem to have one of two main functions. One function involves secretion to form components of ...

Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis. We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates. GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171. Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop. We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate. GalNAc-T3s structure further reveals ...

GALNT7 antibody [N1C2] (UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7)) for ICC/IF, IHC-P, WB. Anti-GALNT7 pAb (GTX106068) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.

Abstract: Protein O-glycosylation is controlled by polypeptide GalNAc-transferases (GalNAc-Ts) that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and catalysis remains unclear. Here we present the first crystal structures of complexes of GalNAc-T2 with glycopeptides that together with enhanced sampling molecular dynamics simulations demonstrate a cooperative mechanism by which the lectin domain enables free acceptor sites binding of glycopeptides into the catalytic domain. Atomic force microscopy and small-angle X-ray scattering experiments further reveal a dynamic conformational landscape of GalNAc-T2 and a prominent role of compact structures that are both required for efficient catalysis. Our model indicates that the activity profile of GalNAc-T2 is dictated by conformational heterogeneity and relies on a flexible linker located between the catalytic and the lectin domains. Our ...

Authors: Ju, Tongzhong , Aryal, Rajindra P. , Kudelka, Matthew R. , Wang, Yingchun , Cummings, Richard D. Article Type: Research Article Abstract: The Tn antigen is a tumor-associated carbohydrate antigen that is not normally expressed in peripheral tissues or blood cells. Expression of this antigen, which is found in a majority of human carcinomas of all types, arises from a blockage in the normal O-glycosylation pathway in which glycans are extended from the common precursor GalNAcα1-O-Ser/Thr (Tn antigen). This precursor is generated in the Golgi apparatus on newly synthesized glycoproteins by a family of polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs) and then extended to the common core 1 O-glycan Galβ1-3GalNAcα1-O-Ser/Thr (T antigen) by a single enzyme termed the T-synthase (core 1 β3-galactosyltransferase or C1GalT). Formation …of the active form of the T-synthase requires a unique molecular chaperone termed Cosmc, encoded by Cosmc on the X-chromosome (Xq24 in humans, ...

Genome-wide association studies have identified GALNT2 as a candidate gene in lipid metabolism, but it is not known how the encoded enzyme ppGalNAc-T2, which contributes to the initiation of mucin-type O-linked glycosylation, mediates this effect. In two probands with elevated plasma high-density lipoprotein cholesterol and reduced triglycerides, we identified a mutation in GALNT2. It is shown that carriers have improved postprandial triglyceride clearance, which is likely attributable to attenuated glycosylation of apolipoprotein (apo) C-III, as observed in their plasma. This protein inhibits lipoprotein lipase (LPL), which hydrolyses plasma triglycerides. We show that an apoC-III-based peptide is a substrate for ppGalNAc-T2 while its glycosylation by the mutant enzyme is impaired. In addition, neuraminidase treatment of apoC-III which removes the sialic acids from its glycan chain decreases its potential to inhibit LPL. Combined, these data suggest that ppGalNAc-T2 can affect lipid metabolism ...

Abnormal O-glycans expressed by cancer cells have functional importance in cell adhesion, invasion, and metastasis [15]. Alterations in mucin-type O-glycans has been associated with malignant transformation, resulting in the formation of less complex structures and leading to an increase of the simple short determinants. Protein O-glycosylation is deregulated in breast cancer cells, leading to the accumulation of simple mucin-type tumor-associated antigens [37]. The expression of GalNAc-T14 mRNA was analyzed in normal and malignant tissue from breast, skin, lung, pancreas, ovary, endometrium, bladder and lymphoid cancers. A subset of tumor samples, ranging from 10% in lobular breast cancer to 30% in lung cancer and diffuse large B-cell lymphoma, showed GalNAc-T14 mRNA overexpression [36]. Under thees circumstances, we hypothesize the expression of GalNAc-T14 may be a useful biomarker for breast cancer by immunohistochemistry.. It has been shown that several glycosyltransferases are useful tumor ...

Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.

Many studies have verified that posttranslational modification determines whether FGF23 polypeptide is secreted as an intact biologically active molecule or subjected to intracellular proteolysis (37). FGF23 is O-glycosylated at the residue T178 by the enzyme ppGalNAc-T3 (polypeptide N-acetylgalactosaminyltransferase 3), and this modification blocks its proteolysis and is required for the release of iFGF23 (38). Furthermore, a secretory kinase, FAM20C, phosphorylates FGF23 on S180 within the furin recognition motif R176XXR179/S180, and this phosphorylation blocks the O-glycosylation of FGF23 and renders it susceptible to proteolysis by furin (14, 39). It seems that these dynamic posttranslational processes including phosphorylation, glycosylation, and proteolysis play a critical role in the intracellular regulation of FGF23 homeostasis. In light of these findings, it is important to note that both tPA and uPA can cleave glycosylated FGF23, because glycosylated rhFGF23 was used in this study. ...

Predicted to have carbohydrate binding activity and transferase activity, transferring glycosyl groups. Predicted to be involved in protein glycosylation. Predicted to localize to Golgi apparatus. Human ortholog(s) of this gene implicated in colorectal cancer. Orthologous to human GALNT12 (polypeptide N-acetylgalactosaminyltransferase 12 ...

N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.149); Glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase (EC 2.4.1.122); fucose-specific β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.-); globotriosylceramide β-1,3-GalNAc transferase (EC 2.4.1.79); chondroitin synthase (β-1,3-GlcUA and β-1,4-GalNAc transferase (EC 2.4.1.175); chondroitin β-1,3-glucuronyltransferase (EC 2.4.1.226); chondroitin β-1,4-N-acetylgalactosaminyltransferase (EC 2.4.1.-); UDP-Gal: β-galactosylxylosylprotein β-1,3-galactosyltransferase (EC 2.4.1.134); UDP-GlcNAc: O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.222 ...

N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.149); Glycoprotein-N-acetylgalactosamine 3-β-galactosyltransferase (EC 2.4.1.122); fucose-specific β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.-); globotriosylceramide β-1,3-GalNAc transferase (EC 2.4.1.79); chondroitin synthase (β-1,3-GlcUA and β-1,4-GalNAc transferase (EC 2.4.1.175); chondroitin β-1,3-glucuronyltransferase (EC 2.4.1.226); chondroitin β-1,4-N-acetylgalactosaminyltransferase (EC 2.4.1.-); UDP-Gal: β-galactosylxylosylprotein β-1,3-galactosyltransferase (EC 2.4.1.134); UDP-GlcNAc: O-fucosylpeptide β-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.222 ...

Complete information for GALNT18 gene (Protein Coding), Polypeptide N-Acetylgalactosaminyltransferase 18, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

Complete information for GALNT18 gene (Protein Coding), Polypeptide N-Acetylgalactosaminyltransferase 18, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

Sigma-Aldrich offers abstracts and full-text articles by [Erandi Lira-Navarrete, Matilde de Las Rivas, Ismael Compañón, María Carmen Pallarés, Yun Kong, Javier Iglesias-Fernández, Gonçalo J L Bernardes, Jesús M Peregrina, Carme Rovira, Pau Bernadó, Pierpaolo Bruscolini, Henrik Clausen, Anabel Lostao, Francisco Corzana, Ramon Hurtado-Guerrero].

Glycosaminoglycans (GAGs) are linear polysaccharide chains consisting of repeating disaccharide units and form proteglycans by covalently attaching to their core proteins. Chondroitin sulfate (CS) is a glycosaminoglycan with the disaccharide unit GalNAc(b1-4)GlcA(b1-3), modified with ester-linked sulfate at certain positions. Dermatan sulfate (DS) is a modified form of CS, in which a portion of D-glucuronate residues is epimerized to L-iduronates. CS and DS are linked to serine residues in core proteins via a linkage tetrasaccharide formed by the transfer of xylose and three more residues [MD:M00057]. The assembly process of CS is initiated by the transfer of N-acetylgalactosamine to the linkage tetrasaccharide. The polymerization step is catalyzed by bifunctional enzymes (chondroitin synthases) that have both b1-3 glucuronosyltransferase and b1-4 N-acetylgalactosaminyltransferase activities [MD:M00058]. Chondroitin polymerization also requires the action of the chondroitin polymerizing factor. ...

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

B4GALNT2 catalyzes the last step in the biosynthesis of the human Sd(a) antigen through the addition of an N-acetylgalactosamine residue via a beta-1,4 linkage to a subterminal galactose residue substituted with an alpha-2,3-linked sialic acid. B4GALNT2 also catalyzes the last step in the biosynthesis of the Cad antigen (Montiel et al., 2003 [PubMed 12678917]).[supplied by OMIM, Mar 2008 ...

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B4galnt2 - B4galnt2 (untagged) - Mouse beta-1,4-N-acetyl-galactosaminyl transferase 2 (B4galnt2), (10ug) available for purchase from OriGene - Your Gene Company.

Purified Recombinant Human GALNT2 Protein, Myc/DDK-tagged, C13 and N15-labeled from Creative Biomart. Recombinant Human GALNT2 Protein, Myc/DDK-tagged, C13 and N15-labeled can be used for research.

Next-day shipping cDNA ORF clones derived from B4galnt1 beta-1,4-N-acetyl-galactosaminyl transferase 1 available at GenScript, starting from $99.00.

Human GALNT9 full-length ORF ( NP_068580.2, 1 a.a. - 237 a.a.) recombinant protein with GST-tag at N-terminal. (H00050614-P01) - Products - Abnova

Monoklonale und polyklonale GALNT13 Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für GALNT13 Antikörper. Hier bestellen.

A4GALT encodes a type II membrane glycosyltransferase and results in Pk and P1 antigens of the P Non-ABO blood group along with B3GALNT1. ...

MalaCards based summary : Hyperphosphatemic Familial Tumoral Calcinosis, Fgf23-Related An important gene associated with Hyperphosphatemic Familial Tumoral Calcinosis, Fgf23-Related is FGF23 (Fibroblast Growth Factor 23 ...

Mucin-type O-linked glycosylation is abundant in the extracellular matrix and is initiated in the Golgi by the UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase family of enzymes (pGalNAc-T in mammals and PGANT in Drosophila), which adds a GalNAc sugar to serines or threonines of secreted and membrane-bound proteins. In Drosophila, there are nine PGANTs (PGANT1-8, PGANT35A) and three putative PGANT isoforms. CG30463 is one putative PGANT isoform based on sequence conservation. Knockdown of CG30463 via RNA interference (RNAi) in vivo results in lethality, indicating that CG30463 is an essential gene. However, the catalytic activity of the enzyme encoded by CG30463 had not been identified previously. Here, we demonstrate that CG30463 encodes a functional O-glycosyltransferase, PGANT9. Purified PGANT9 protein transferred GalNAc onto both peptide and glycopeptide substrates in vitro. Additionally, over-expression of PGANT9 in cell culture increased HPA-reactive glycosylation in vivo. ...

A highly conserved threonine near the C terminus of gp120 of human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) was investigated for its contributions to envelope protein function and virion infectivity. When this highly conserved Thr residue was substituted with anything other than serine (the other amino acid that can accept O-glycosylation), the resulting virus was noninfectious. We found that this Thr was critical for the association of gp120 with the virion and that amino acid substitution increased the amount of dissociated gp120 in the cell culture supernatant. When HIV virions were generated in cells overexpressing polypeptide N-acetylgalactosaminyltransferase 1 (GalNAcT1), viral infectivity was increased 2.5-fold compared to that of virus produced in wild-type HEK293T cells; infectivity was increased 8-fold when the Thr499Ser mutant was used. These infectivity enhancements were not observed when GalNAcT3 was used. Using HEK293T knockout cell lines totally devoid ...

The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...

An incomplete elongation of O-glycan saccharide chains in mucins have been found in epithelial cancers, leading to the expression of shorter carbohydrate structures, such as the Tn antigen (GalNAc-O-Ser/Thr). This antigen is one of the most specific human cancer-associated structures and is capable of inducing effective immune responses against cancer cells. We aimed to investigate the causes of the expression of Tn antigen in the Tn-rich MCF-7 breast cancer cell line focusing on the first step of the O-glycosylation process. Interestingly, amino acid sequences derived from non-mammary apomucins (MUC5B and MUC6) were very good acceptor substrates for ppGalNAc-Ts, which are the enzymes catalyzing the Tn antigen synthesis. MUC6 peptide glycosylation with MCF-7 microsome extracts as source of ppGalNAc-T activity yielded 95% conversion of the peptide into MUC6-Tn. In addition, the MUC6-Tn glycopeptide was a poor acceptor substrate for core 1 beta3Gal-T, the next enzyme involved in the saccharide chain

Materials and Methods: A retrospective study of seven patients of tumoral calcinosis treated with complete surgical excision over a period of 1 year was done. Demographic details were compiled. Routine blood investigations were performed. All patients underwent radiographs and magnetic resonance imaging (MRI) scans of involved part. We did not perform computed tomography (CT) or bone scan in any of our patients. All seven patients underwent surgery and were followed up till 2 years ...

B4GALNT3 - B4GALNT3 (GFP-tagged) - Human beta-1,4-N-acetyl-galactosaminyl transferase 3 (B4GALNT3) available for purchase from OriGene - Your Gene Company.

Human blood group A and B antigens are produced by two closely related glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA) utilizes UDP-GalNAc to extend H antigen acceptors (Fuc alpha(1-2)Gal beta-OR) producing A antigens, whereas a galactosyltransferase (GTB) utilizes UDP-Gal as a donor to extend H structures producing B antigens. GTA and GTB have a characteristic (211)DVD(213) motif that coordinates to a Mn(2+) ion shown to be critical in donor binding and catalysis. Three GTB mutants, M214V, M214T, and M214R, with alterations adjacent to the (211)DVD(213) motif have been identified in blood banking laboratories. From serological phenotyping, individuals with the M214R mutation show the B(el) variant expressing very low levels of B antigens, whereas those with M214T and M214V mutations give rise to A(weak)B phenotypes. Kinetic analysis of recombinant mutant GTB enzymes revealed that M214R has a 1200-fold decrease in k(cat) compared with wild type GTB. The crystal structure ...

The GALNT3 gene provides instructions for making a protein called ppGalNacT3, which is found in many types of cells. Learn about this gene and related health conditions.

pfam06306 (PSSM ID: 114995): Conserved Protein Domain Family CgtA, This family consists of several beta-1,4-N-acetylgalactosaminyltransferase proteins from Campylobacter jejuni

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Expression of CHPF2 (ChSy-3, CSGlcA-T, KIAA1402) in cancer tissue. The cancer tissue page shows antibody staining of the protein in 20 different cancers.

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Hyperphosphatemic familial tumoral calcinosis (HFTC)/hyperostosis-hyperphosphatemia syndrome (HHS) is an autosomal recessive disorder of ectopic calcification due to deficiency of or resistance to intact fibroblast growth factor 23 (iFGF23). Inactivating mutations in FGF23, N-acetylgalactosaminyltransferase 3 (GALNT3), or KLOTHO (KL) have been reported as causing HFTC/HHS. We present what we believe is the first identified case of autoimmune hyperphosphatemic tumoral calcinosis in an 8-year-old boy. In addition to the classical clinical and biochemical features of hyperphosphatemic tumoral calcinosis, the patient exhibited markedly elevated intact and C-terminal FGF23 levels, suggestive of FGF23 resistance. However, no mutations in FGF23, KL, or FGF receptor 1 (FGFR1) were identified. He subsequently developed type 1 diabetes mellitus, which raised the possibility of an autoimmune cause for hyperphosphatemic tumoral calcinosis. Luciferase immunoprecipitation systems revealed markedly elevated ...

Hyperphosphatemic familial tumoral calcinosis (HFTC)/hyperostosis-hyperphosphatemia syndrome (HHS) is an autosomal recessive disorder of ectopic calcification due to deficiency of or resistance to intact fibroblast growth factor 23 (iFGF23). Inactivating mutations in FGF23, N-acetylgalactosaminyltransferase 3 (GALNT3), or KLOTHO (KL) have been reported as causing HFTC/HHS. We present what we believe is the first identified case of autoimmune hyperphosphatemic tumoral calcinosis in an 8-year-old boy. In addition to the classical clinical and biochemical features of hyperphosphatemic tumoral calcinosis, the patient exhibited markedly elevated intact and C-terminal FGF23 levels, suggestive of FGF23 resistance. However, no mutations in FGF23, KL, or FGF receptor 1 (FGFR1) were identified. He subsequently developed type 1 diabetes mellitus, which raised the possibility of an autoimmune cause for hyperphosphatemic tumoral calcinosis. Luciferase immunoprecipitation systems revealed markedly elevated ...

A novel gene participating in the polymerization of chondroitin chain is found out. A gene product thereof, which forms a complex with chondroitin synthase |i|in vivo|/i| and thus promotes polymerization of chondroitin, is named chondroitin polymerization factor (ChPF). This chondroitin polymerization factor is usable in artificially synthesizing sugar chain skeletons of sulfated glycosaminoglycans having useful physiological activities such as chondroitin sulfate and dermatan sulfate, which makes it industrially useful.

ST3Gal V (or GM3 synthase) is the sialyltransferase that catalyses the initial step in the biosynthesis of most complex gangliosides from lactosylceramide. ST3Gal V plays a key regulatory role in determining the cell surface ganglioside profile and, consequently, in modulating a large variety of ganglioside-dependent cellular events, such as cell proliferation and differentiation, adhesion, apoptosis, oncogenesis. In addition, a homozygous loss-of-function mutation in the hST3Gal V gene is cause of an autosomal recessive infantile-onset symptomatic epilepsy syndrome. Recently, we have identified a hST3Gal V mRNA variant containing an additional translation start codon, located upstream and in-frame with that considered unique translation initiation site in the human GM3 synthase gene, providing the first evidence of the existence of two differentially N-terminal extended isoforms of the protein [1]. The functional relevance of the longer isoform has to be defined yet, and a study to define its ...

Expression of B4GALNT3 (B4GalNac-T3, FLJ16224, FLJ40362) in urinary bladder tissue. Antibody staining with HPA011404 in immunohistochemistry.

Tumoral calcinosis is an uncommon condition characterized by the calcification of periarticular soft tissue. In uremic patients the disease is secondary to metabolic disturbances in predisposed patients. The authors report the case of a 73-year-old woman who presented with a new painful cervical mass while undergoing continuous ambulatory peritoneal dialysis for long-standing end-stage renal disease (ESRD). A CT scan of the neck showed a lobulated, calcified mass in the left paraspinal soft tissue at C2-3. This mass affected the facet joint and also extended into the neural foramen but did not cause any neurological compromise. Due to the patients significant medical comorbidities, resection was deferred and the patient was followed in the clinic. Subsequent repeat imaging has shown a significant decrease in the size of the mass. In the context of ESRD, a diagnosis of uremic tumoral calcinosis (UTC) was made. The authors conducted a search of the PubMed and EMBASE databases and identified 7 ...

The N-acetylgalactosamine-transferase11 (GALNT11) activation in leukemia and the role of cyclophosphamide and cytarabine in expression of this enzyme

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