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UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 4

GalNAc-T4, GALNT4, ppGaNTase-T4
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. In vitro, the encoded protein can complement other GalNAc-Ts in the complete O-glycosylation of the mucin-1 tandem repeat and can O-glycosylate the P-selectin glycoprotein ligand-1 molecule. The coding region of this gene is contained within a single exon. Fusion transcripts, which combine part of this gene with the 5' exons of the neighboring POC1B (POC1 centriolar protein homolog B) gene, also exist. [provided by RefSeq, Dec 2010] (from NCBI)
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Top mentioned proteins: GalNAc-T, MUC1, STEP, fibrillin-1, CD45
Papers on GalNAc-T4
GalNAc-T4 putatively modulates the estrogen regulatory network through FOXA1 glycosylation in human breast cancer cells.
New
Zhang et al., Dalian, China. In Mol Cell Biochem, Dec 2015
UNASSIGNED: GALNT4 belongs to a family of N-acetylgalactosaminyltransferases, which catalyze the transfer of GalNAc to Serine or Threonine residues in the initial step of mucin-type O-linked protein glycosylation.
GALNT4 predicts clinical outcome in patients with clear cell renal cell carcinoma.
Gu et al., Shanghai, China. In J Urol, 2014
PURPOSE: We investigated the clinical significance of GALNT4 expression in patients with clear cell renal cell carcinoma.
Identification of CAD candidate genes in GWAS loci and their expression in vascular cells.
Lusis et al., Los Angeles, United States. In J Lipid Res, 2013
By integrating human and mouse results, we predict that PPAP2B, GALNT4, MAPKAPK5, TCTN1, SRR, SNF8, and ICAM1 play a causal role in the susceptibility to atherosclerosis through a role in the vasculature.
Engineering mammalian mucin-type O-glycosylation in plants.
Petersen et al., Slagelse, Denmark. In J Biol Chem, 2012
A chimeric YFP construct containing a 3.5 tandem repeat sequence of MUC1 was glycosylated with up to three and five GalNAc residues when co-expressed with GalNAc-T2 and a combination of GalNAc-T2 and GalNAc-T4, respectively, as determined by mass spectrometry.
Genetic polymorphisms in platelet-related proteins and coronary artery disease: investigation of candidate genes, including N-acetylgalactosaminyltransferase 4 (GALNT4) and sulphotransferase 1A1/2 (SULT1A1/2).
GeneRIF
Shields et al., Dublin, Ireland. In J Thromb Thrombolysis, 2009
GALNT4 identified as a risk gene for cardiovascular disease, whose effects may be on either platelet or endothelial function through modifications of PSGL1 or other important glycosylated proteins.
Estrogen regulates vesicle trafficking gene expression in EFF-3, EFM-19 and MCF-7 breast cancer cells.
Westley et al., Newcastle upon Tyne, United Kingdom. In Int J Clin Exp Pathol, 2008
We focused on five genes (SYTL5, RAB27B, SNX24, GALNT4 and SLC12A2/NKCC1/BSC2) and confirmed their estrogen-regulation using quantitative real-time PCR (qPCR).
Differential gene expression profiles of normal human parotid and submandibular glands.
Wang et al., Beijing, China. In Oral Dis, 2008
Ninety-eight transcripts were upregulated at least twofold in the submandibular gland compared with the parotid gland, including the chloride channel CFTR and mucin-associated genes that belong to the starch and sucrose metabolism pathway (GalNAc-T4, GalNAc-T7 and GalNAc-T13).
The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.
Clausen et al., Copenhagen, Denmark. In Glycobiology, 2007
We have previously shown that the lectin domain of GalNAc-T4 modulates its substrate specificity to enable unique GalNAc-glycopeptide specificities and that this effect is selectively inhibitable by GalNAc; however, direct evidence of carbohydrate binding of GalNAc-transferase lectins has not been previously presented.
Identification of Tgf beta1i4 as a downstream target of Foxc1.
Kidson et al., Cape Town, South Africa. In Dev Growth Differ, 2006
Absence of Foxc1 led to downregulation of Stat1 and Galnt4, and upregulation of Tgf beta1i4 at embryonic day 13.5 in the developing head mesenchyme.
A MUC1 tandem repeat reporter protein produced in CHO-K1 cells has sialylated core 1 O-glycans and becomes more densely glycosylated if coexpressed with polypeptide-GalNAc-T4 transferase.
Hansson et al., Göteborg, Sweden. In Glycobiology, 2005
The reporter protein, MUC1(1.7TR)-IgG2a, was produced in CHO-K1 cells to study the glycosylation of the MUC1 TR and the in vivo role of polypeptide-GalNAc-T4 glycosyltransferase.
Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines.
Reis et al., Porto, Portugal. In J Histochem Cytochem, 2003
Our results showed that GalNAc-T1, -T2, and -T3 have an ubiquitous expression in all gastric cell lines, whereas GalNAc-T4, -T6, and -T11 show a restricted expression pattern.
The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization.
Gipson et al., Boston, United States. In Invest Ophthalmol Vis Sci, 2003
The GalNAc-T4 isoenzyme was found in the apical cell layers, whereas GalNAc-T2 was found in the supranuclear region of the basal cell layers of both cornea and conjunctiva.
O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines. Distinct specificity of GalNAc-transferase isoforms.
Irimura et al., Tokyo, Japan. In Eur J Biochem, 2002
The first and the third Thr residues act as the peptide's initial glycosylation sites for pp-GalNAc-T4, which were different from the sites for pp-GalNAc-T1 and T2 (the first Thr residue) or T3 (the third Thr residue) shown in our previous report.
The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities.
Clausen et al., Copenhagen, Denmark. In J Biol Chem, 2001
O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4.
Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat.
Clausen et al., Copenhagen, Denmark. In J Biol Chem, 1998
A fourth human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated GalNAc-T4, was cloned and expressed.
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