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Chemical Compound Review:

HMDB00304 [3-acetamido-4,5-dihydroxy- 6...

Synonyms: KST-1A8088, AC1L1AVK, AR-1A8573, AC1Q6SL3, L000907, ...

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Disease relevance of uridine diphosphate N-acetylglucosamine

WbpO, a UDP-N-acetyl-D-galactosamine dehydrogenase from Pseudomonas aeruginosa serotype O6 [1].
Microsomal preparations from chondroitin 6-sulfate-producing chick embryo epiphyseal cartilage, and from chondroitin 4-sulfate-producing mouse mastocytoma cells, were incubated with UDP-[14C]glucuronic acid and UDP-N-acetylgalactosamine to form non-sulfated proteo[14C]chondroitin [2].
Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells [3].
Animal studies suggest that overactivity of the hexosamine pathway, resulting in increased UDP-hexosamines [UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc)] is an important mechanism by which hyperglycemia causes insulin resistance [4].
The UDP N-acetylgalactosamine 4-epimerase gene is essential for mesophilic Aeromonas hydrophila serotype O34 virulence [5].

High impact information on uridine diphosphate N-acetylglucosamine

Vesicles containing a deletion mutant of the C03H5.2 protein transport UDP-N-acetylglucosamine at rates comparable with that of wild-type transporter, whereas transport of UDP-N-acetylgalactosamine was decreased by 85-90%, resulting in an asymmetrical loss of substrate transport [6].
We have characterized a transporter of UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine encoded by the Caenorhabditis elegans gene C03H5 [6].
The specific activity of the V94M-hGALE protein expressed in yeast was severely reduced with regard to UDP-galactose and partially reduced with regard to UDP-N-acetylgalactosamine [7].
Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland [8].
The mutant line, genotype LDLD, cannot synthesize UDP-N-acetylgalactosamine under normal culture conditions and, therefore, cannot add mucin-type O-linked oligosaccharides to proteins [9].

Chemical compound and disease context of uridine diphosphate N-acetylglucosamine

1H NMR spectra revealed the presence of elevated levels of UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine in glioblastoma extracts and the glioblastoma cell line U-87, in comparison with normal brain tissue and primary cell cultures of neurons and astrocytes [10].

Biological context of uridine diphosphate N-acetylglucosamine

Molecular basis of the globoside-deficient P(k) blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene [11].
In the present report, five oligopeptides [PTTTPITTTT(K), ITTTTTVTPT(K), TVTPTPTPTG(K), PTPTGTQTPT(K) and TQTPTTTPIT(K)] corresponding to portions of the MUC2 tandem repeat domain were synthesized, and incubated with UDP-N-acetyl-D-galactosamine (UDP-GalNAc) and detergent-soluble microsomes, prepared from the human colon carcinoma cell line LS174T [12].
The major UDP-hexose species were found to be UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine (ca 2:1 ratio), which have been proposed in the literature to be markers of cell differentiation status [13].
The UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-T) family enzymes regulate the initial steps of mucin O-glycosylation and could be responsible for the altered glycosylation observed in cancer [14].
The formation of radioactive UDP-N-acetylgalactosamine from UDP-N-acetyl[U-14C]-glucosamine was demonstrated by radioautography, after hydrolysis of UDP-derivatives and separation of the hexosamines by paper chromatography [15].

Anatomical context of uridine diphosphate N-acetylglucosamine

An alpha-3-N-acetylgalactosaminyltransferase that transfers N-acetylgalactosamine from UDP-N-acetylgalactosamine to H-active structures to form A determinants was purified to homogeneity from human gut mucosal tissue of blood-group-A subjects [16].
A microsomal preparation from the fibroblasts was incubated with UDP-D-[5-3H]glucuronic acid, UDP-D-[14C]glucuronic acid, UDP-N-acetyl-D-galactosamine and 3'-phospho-5'-adenylyl sulphate [17].
We also measured the enzymatic activities of UDP-N-acetylgalactosamine: GM3, N-acetylgalactosaminyl transferase (EC 2.4.1.92) and of CMP-N-acetylneuraminic acid: GM3 sialyl transferase (EC 2.4.99.8) in neuroblastoma cells cultured under these conditions [18].
Simultaneous, quantitative analysis of UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine, UDP-glucose and UDP-galactose in human peripheral blood cells, muscle biopsies and cultured mesangial cells by capillary zone electrophoresis [19].
Expression of UDP-N-acetylgalactosamine: beta-galactose beta 1,4-N-acetylgalactosaminyltransferase in functionally defined T-cell clones [20].

Associations of uridine diphosphate N-acetylglucosamine with other chemical compounds

Moreover, using both UDP-glucuronic acid (GlcUA) and UDP-N-acetylgalactosamine (GalNAc) as sugar donors, chondroitin polymerization was demonstrated on the so-called glycosaminoglycan-protein linkage region tetrasaccharide sequence of alpha-thrombomodulin [21].
Wild-type mice and knockout mice with a disrupted gene for GM2/GD2 synthase (UDP-N-acetyl-D-galactosamine : GM3/GD3 N-acetyl-D-glactosaminyltransferase) were immunized with GD1a conjugated to keyhole limpet hemocyanin [22].
The Km for UDP-N-acetylgalactosamine was 110 microM and that for an octapeptide acceptor (VTPRTPPP) was 3.0 mM at 37 degrees C. Using a range of synthetic peptides of known structure related to TPPP it was established that L-threonine residues were specifically O-glycosylated probably in the alpha-configuration [23].
A single mutation in the gene that codes for UDP N-acetylgalactosamine 4-epimerase (gne) confers the O(-) phenotype (LPS without O-antigen molecules) on a strain in serotypes O18 and O34, but not in serotypes O1 and O2 [5].
Formation of two species of [14C]proteochondroitin sulfate has previously been demonstrated with UDP-D-[14C]glucuronic acid and UDP-N-acetylgalactosamine as substrates with a microsomal preparation from chick-embryo epiphyseal cartilage [24].

Gene context of uridine diphosphate N-acetylglucosamine

Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family [25].
The activities of UDP-N-acetylgalactosamine (GalNAc):polypeptide GalNAc transferase and UDP-galactose (Gal):asialo bovine submaxillary mucin (BSM) Gal transferase were found to be elevated [26].
Purification and characterization of UDP-N-acetylgalactosamine GM3/GD3 N-acetylgalactosaminyltransferase from mouse liver [27].
Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen [28].
The effects of O-glycosylation on the synthesis and secretion of apolipoprotein E (apoE, a glycoprotein with O- but not N-linked sugars) were studied with a UDP-galactose/UDP-N-acetylgalactosamine 4-epimerase-deficient cell mutant (ldlD cells) which expresses a reversible defect in protein O-glycosylation [29].

References

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Sulfation of chondroitin. Specificity, degree of sulfation, and detergent effects with 4-sulfating and 6-sulfating microsomal systems. Sugumaran, G., Silbert, J.E. J. Biol. Chem. (1988) [Pubmed]
Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells. Elhammer, A., Kornfeld, S. J. Biol. Chem. (1986) [Pubmed]
Muscle uridine diphosphate-hexosamines do not decrease despite correction of hyperglycemia-induced insulin resistance in type 2 diabetes. Pouwels, M.J., Span, P.N., Tack, C.J., Olthaar, A.J., Sweep, C.G., van Engelen, B.G., de Jong, J.G., Lutterman, J.A., Hermus, A.R. J. Clin. Endocrinol. Metab. (2002) [Pubmed]
The UDP N-acetylgalactosamine 4-epimerase gene is essential for mesophilic Aeromonas hydrophila serotype O34 virulence. Canals, R., Jiménez, N., Vilches, S., Regué, M., Merino, S., Tomás, J.M. Infect. Immun. (2006) [Pubmed]
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Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia. Wohlers, T.M., Christacos, N.C., Harreman, M.T., Fridovich-Keil, J.L. Am. J. Hum. Genet. (1999) [Pubmed]
Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Roth, J., Wang, Y., Eckhardt, A.E., Hill, R.L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
Use of a mutant cell line to study the kinetics and function of O-linked glycosylation of low density lipoprotein receptors. Kozarsky, K., Kingsley, D., Krieger, M. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
UDP-N-acetylhexosamines and hypotaurine in human glioblastoma, normal brain tissue and cell cultures: 1H/NMR spectroscopy study. Sonnewald, U., Isern, E., Gribbestad, I.S., Unsgård, G. Anticancer Res. (1994) [Pubmed]
Molecular basis of the globoside-deficient P(k) blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene. Hellberg, A., Poole, J., Olsson, M.L. J. Biol. Chem. (2002) [Pubmed]
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The influence of medium formulation on phosphomonoester and UDP-hexose levels in cultured human colon tumor cells as observed by 31P NMR spectroscopy. Shedd, S.F., Lutz, N.W., Hull, W.E. NMR in biomedicine. (1993) [Pubmed]
UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 as a new immunohistochemical breast cancer marker. Berois, N., Mazal, D., Ubillos, L., Trajtenberg, F., Nicolas, A., Sastre-Garau, X., Magdelenat, H., Osinaga, E. J. Histochem. Cytochem. (2006) [Pubmed]
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Purification, properties and partial amino acid sequence of the blood-group-A-gene-associated alpha-3-N-acetylgalactosaminyltransferase from human gut mucosal tissue. Navaratnam, N., Findlay, J.B., Keen, J.N., Watkins, W.M. Biochem. J. (1990) [Pubmed]
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Simultaneous, quantitative analysis of UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine, UDP-glucose and UDP-galactose in human peripheral blood cells, muscle biopsies and cultured mesangial cells by capillary zone electrophoresis. Lehmann, R., Huber, M., Beck, A., Schindera, T., Rinkler, T., Houdali, B., Weigert, C., Häring, H.U., Voelter, W., Schleicher, E.D. Electrophoresis (2000) [Pubmed]
Expression of UDP-N-acetylgalactosamine: beta-galactose beta 1,4-N-acetylgalactosaminyltransferase in functionally defined T-cell clones. Conzelmann, A., Bron, C. Biochem. J. (1987) [Pubmed]
Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. Kitagawa, H., Izumikawa, T., Uyama, T., Sugahara, K. J. Biol. Chem. (2003) [Pubmed]
High-affinity anti-ganglioside IgG antibodies raised in complex ganglioside knockout mice: reexamination of GD1a immunolocalization. Lunn, M.P., Johnson, L.A., Fromholt, S.E., Itonori, S., Huang, J., Vyas, A.A., Hildreth, J.E., Griffin, J.W., Schnaar, R.L., Sheikh, K.A. J. Neurochem. (2000) [Pubmed]
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Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family. Bennett, E.P., Weghuis, D.O., Merkx, G., van Kessel, A.G., Eiberg, H., Clausen, H. Glycobiology (1998) [Pubmed]
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Purification and characterization of UDP-N-acetylgalactosamine: globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase, a synthase of human blood group P antigen, from canine spleen. Taniguchi, N., Makita, A. J. Biol. Chem. (1984) [Pubmed]
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