The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

N-Acetyl-D-galactosamine     N-[(3R,4R,5S,6R)-2,4,5- trihydroxy-6...

Synonyms: Aflexa, GlcNAc, NAcGlc, Maxi GS, CID899, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of N-acetyl-D-glucosamine

  • Chorea monoclonal antibodies showed specificity for mammalian lysoganglioside and N-acetyl-beta-D-glucosamine (GlcNAc), the dominant epitope of the group A streptococcal (GAS) carbohydrate [1].
  • For further characterization of the relationship between Asn-linked carbohydrate structures, cell adhesion, NK cell sensitivity, and metastasis, mutants of MDW4 were selected for resistance to the GlcNAc-binding lectin from Bandeiraea simplicifolia seeds (BSII) [2].
  • Anti-streptococcal antibodies cross-reactive with N-acetyl-betaD-glucosamine (GlcNAc) and myosin are present in the sera of patients with rheumatic fever (RF) [3].
  • BACKGROUND & AIMS: Clostridium difficile toxin A causes secretion and intestinal inflammation in rodents by binding to a specific trisaccharide Gal alpha 1-3Gal beta 1-4 GlcNAc on enterocyte receptors [4].
  • Increased levels of the alpha2,3 SAT (O) and decreased levels of the core-2 beta1,6 GlcNAc T are seen in breast cancer cells and correlate with differences in the structure of the O-glycans synthesized (Brockhausen et al., 1995; Lloyd et al., 1996) [5].
 

Psychiatry related information on N-acetyl-D-glucosamine

  • Under the conditions comprising 2.0 x 10(-3) M labeling reagent and 1.0 x 10(-5) M human lysozyme at pH 5.4, 37 degrees C, the reaction time required to reduce the lytic activity against Micrococcus luteus cells to 50% of its initial activity was lengthened by 3.7 times through the substitution of the nonreducing end sugar residue, GlcNAc to Gal [6].
 

High impact information on N-acetyl-D-glucosamine

  • Here, we demonstrate that Eri1 is a component of the GPI-GlcNAc transferase (GPI-GnT) complex in the ER, which catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins [7].
  • Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not [8].
  • This glycosylation occurs when G protein is transported during mixed incubations from the "donor" compartment in Golgi from VSV-infected CHO clone 15B cells (missing a key Golgi GlcNAc transferase) to the next, successive "acceptor" compartment (containing the GlcNAc transferase) in Golgi from wild-type CHO cells [9].
  • Transport of the VSV-encoded glycoprotein (G protein) between successive compartments of the Golgi has been reconstituted in a cell-free system and is measured, in a rapid and sensitive new assay, by the coupled incorporation of 3H-N-acetylglucosamine (GlcNAc) [9].
  • Mgat5 initiates GlcNAc beta1,6 branching on N-glycans, thereby increasing N-acetyllactosamine, the ligand for galectins, which are proteins known to modulate T-cell proliferation and apoptosis [10].
 

Chemical compound and disease context of N-acetyl-D-glucosamine

  • The primary defect responsible for mucolipidosis III is a deficiency of UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine 1-phosphotransferase activity (GlcNAc phosphotransferase) [11].
  • Unlike the E. coli mannose permease, V. furnissii IIMan is inactive with GlcNAc and Fru, and is encoded by four genes rather than three [12].
  • Chinese hamster ovary cells deficient in the synthesis of heparan sulfate and lacking alpha-GlcNAc-TII activity and S49 Thy 1-a lymphoma cells deficient in alpha GlcNAc addition to phosphatidylinositol have wild-type alpha-GlcNAc-TI activity [13].
  • The second enzyme catalyzes the polymerization of heparan sulfate and can be measured by the transfer of GlcNAc from UDP-GlcNAc to the nonreducing terminal GlcUA present in oligosaccharide fragments prepared from the Escherichia coli K5 capsular polysaccharide, N-acetylheparosan [13].
  • We demonstrate that a single sugar, GlcNAc, can be incorporated to LPS of Escherichia coli K-12 [14].
 

Biological context of N-acetyl-D-glucosamine

  • Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II [8].
  • Studies with free natural and synthetic oligosaccharides identified the disaccharide GlcNAc beta 1 leads to 3Gal beta as one critical binding site [15].
  • Plasma membrane glycoproteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with iodinated WGA, BSII, and leukoagglutinin also indicated an intermediate phenotype, with the presence of both GlcNAc-terminating structures and sialylated complex [2].
  • Finally, replacement of the 2-N-acetyl substituent of the GlcNAc by an azido or amino group resulted in substantial increases in activity, with the most potent inhibitor being amino substituted sLea, which was 36-fold more active (IC50 = 21 +/- 3 microM) than the reducing tetrasaccharide sLex [16].
  • The presence of the milk protein alpha-lactalbumin specifically modifies the substrate specificity of sperm galactosyltransferase away from GlcNAc and towards glucose and simultaneously inhibits sperm binding to the zona pellucida [17].
 

Anatomical context of N-acetyl-D-glucosamine

  • Glycosylation mutants of a metastatic tumor cell line were selected that are deficient in both beta 1-6 GlcNAc transferase V activity and metastatic potential in situ [18].
  • Thus, in addition to unmodified peptides, posttranslationally modified cytosolic peptides carrying O-beta-linked GlcNAc can be presented by class I MHC molecules to the immune system [19].
  • Since the agglutination of leukemic and DNP-tagged normal lymphocytes was equally inhibited by GlcNAc, this suggests that the same or similar receptor sites were involved in the two reactions [20].
  • Although GlcNAc modified proteins exist on both the nuclear and cytoplasmic sides of the nuclear pore complex, ribosomal subunit export was inhibited only when wheat germ agglutinin was injected into the nucleus [21].
  • This modification was found on proteins distributed throughout the cell, although proteins bearing O-linked GlcNAc moieties were particularly abundant in the cytosolic and nuclear envelope fractions of rat liver [22].
 

Associations of N-acetyl-D-glucosamine with other chemical compounds

 

Gene context of N-acetyl-D-glucosamine

  • In the absence of the bisecting GlcNAc in Mgat3-/- mice, the factor is reduced in activity, and tumor progression is severely retarded [26].
  • Mutant mice bearing a targeted disruption of the heparan sulfate (HS) modifying enzyme GlcNAc N-deacetylase/N-sulfotransferase 1 (Ndst1) exhibit severe developmental defects of the forebrain and forebrain-derived structures, including cerebral hypoplasia, lack of olfactory bulbs, eye defects and axon guidance errors [27].
  • N-Acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) catalyzes the transfer of sulfate from adenosine 3'-phosphate,5'-phosphosulfate to the C-6 position of the non-reducing GlcNAc [28].
  • Consistent with its homology to brn, we demonstrate that C. elegans bre-5 rescues the Drosophila brn mutant and that BRE-5 encodes the dominant UDP-GlcNAc:Man GlcNAc transferase activity in C. elegans [29].
  • Although both EXT1 and EXT2 exhibit GlcNAc transferase and GlcUA transferase activities required for the HS synthesis, no HS chain polymerization has been demonstrated in vitro using recombinant enzymes [30].
 

Analytical, diagnostic and therapeutic context of N-acetyl-D-glucosamine

  • A GlcNAc kinase (ATP:2-acetamido-2-deoxy-D-glucose 6-phosphotransferase, EC 2.7.1.59)-enriched fraction, prepared by affinity chromatography on Sepharose-N-(6-aminohexanoyl)-GlcNAc, had a Km of 25 microM for GlcNAc [31].
  • Indirect ELISA demonstrated GlcNAc- and galactosylation-inhibitable binding of the mAbs to a 65-kDa human erythrocyte cytosolic protein known to contain O-GlcNAc [32].
  • Using another mAb with a broad specificity for nuclear GlcNAc-containing proteins, we show by immunofluorescence and protein blotting of subnuclear fractions that some of these proteins are in the interior of the nucleus, and others are most likely located in the pore complex [33].
  • Surface plasmon resonance analysis showed that lamprey C1q specifically bound to GlcNAc, but not various other carbohydrates tested [34].
  • Sequence analysis of a 4-kb genomic clone containing NAG1 indicates that this gene is part of a cluster containing two other genes of the GlcNAc catabolic pathway, i.e., DAC1, GlcNAc-6-phosphate deacetylase, and HXK1, hexokinase [35].

References

  1. Mimicry and autoantibody-mediated neuronal cell signaling in Sydenham chorea. Kirvan, C.A., Swedo, S.E., Heuser, J.S., Cunningham, M.W. Nat. Med. (2003) [Pubmed]
  2. Partial reversion of the metastatic phenotype in a wheat germ agglutinin-resistant mutant of the murine tumor cell line MDAY-D2 selected with Bandeiraea simplicifolia seed lectin. Dennis, J.W. J. Natl. Cancer Inst. (1985) [Pubmed]
  3. Cytotoxic mAb from rheumatic carditis recognizes heart valves and laminin. Galvin, J.E., Hemric, M.E., Ward, K., Cunningham, M.W. J. Clin. Invest. (2000) [Pubmed]
  4. A receptor decoy inhibits the enterotoxic effects of Clostridium difficile toxin A in rat ileum. Castagliuolo, I., LaMont, J.T., Qiu, B., Nikulasson, S.T., Pothoulakis, C. Gastroenterology (1996) [Pubmed]
  5. A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans. Whitehouse, C., Burchell, J., Gschmeissner, S., Brockhausen, I., Lloyd, K.O., Taylor-Papadimitriou, J. J. Cell Biol. (1997) [Pubmed]
  6. Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling. Muraki, M., Harata, K., Sugita, N., Sato, K. Biochemistry (1996) [Pubmed]
  7. Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Sobering, A.K., Watanabe, R., Romeo, M.J., Yan, B.C., Specht, C.A., Orlean, P., Riezman, H., Levin, D.E. Cell (2004) [Pubmed]
  8. O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Jackson, S.P., Tjian, R. Cell (1988) [Pubmed]
  9. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Balch, W.E., Dunphy, W.G., Braell, W.A., Rothman, J.E. Cell (1984) [Pubmed]
  10. Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Demetriou, M., Granovsky, M., Quaggin, S., Dennis, J.W. Nature (2001) [Pubmed]
  11. Heterogeneity of N-acetylglucosamine 1-phosphotransferase within mucolipidosis III. Little, L.E., Mueller, O.T., Honey, N.K., Shows, T.B., Miller, A.L. J. Biol. Chem. (1986) [Pubmed]
  12. Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the mannose/glucose permease. Bouma, C.L., Roseman, S. J. Biol. Chem. (1996) [Pubmed]
  13. Two N-acetylglucosaminyltransferases catalyze the biosynthesis of heparan sulfate. Fritz, T.A., Gabb, M.M., Wei, G., Esko, J.D. J. Biol. Chem. (1994) [Pubmed]
  14. The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat. Feldman, M.F., Marolda, C.L., Monteiro, M.A., Perry, M.B., Parodi, A.J., Valvano, M.A. J. Biol. Chem. (1999) [Pubmed]
  15. Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells. Andersson, B., Dahmén, J., Frejd, T., Leffler, H., Magnusson, G., Noori, G., Edén, C.S. J. Exp. Med. (1983) [Pubmed]
  16. Higher-affinity oligosaccharide ligands for E-selectin. Nelson, R.M., Dolich, S., Aruffo, A., Cecconi, O., Bevilacqua, M.P. J. Clin. Invest. (1993) [Pubmed]
  17. A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida. Shur, B.D., Hall, N.G. J. Cell Biol. (1982) [Pubmed]
  18. Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Dennis, J.W., Laferté, S., Waghorne, C., Breitman, M.L., Kerbel, R.S. Science (1987) [Pubmed]
  19. Presentation of cytosolic glycosylated peptides by human class I major histocompatibility complex molecules in vivo. Haurum, J.S., Høier, I.B., Arsequell, G., Neisig, A., Valencia, G., Zeuthen, J., Neefjes, J., Elliott, T. J. Exp. Med. (1999) [Pubmed]
  20. Agglutination of leukemic and 2,4-dinitrophenyl-tagged normal human lymphocytes by wheat germ agglutinin. Madyastha, P.R., Barth, R.F., Madyastha, K.R. J. Natl. Cancer Inst. (1975) [Pubmed]
  21. Cytoplasmic transport of ribosomal subunits microinjected into the Xenopus laevis oocyte nucleus: a generalized, facilitated process. Bataillé, N., Helser, T., Fried, H.M. J. Cell Biol. (1990) [Pubmed]
  22. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. Holt, G.D., Snow, C.M., Senior, A., Haltiwanger, R.S., Gerace, L., Hart, G.W. J. Cell Biol. (1987) [Pubmed]
  23. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Malhotra, R., Wormald, M.R., Rudd, P.M., Fischer, P.B., Dwek, R.A., Sim, R.B. Nat. Med. (1995) [Pubmed]
  24. Co-ordinated regulation of amino sugar biosynthesis and degradation: the NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites. Plumbridge, J. EMBO J. (1995) [Pubmed]
  25. Lysosomal delivery of the major myelin glycoprotein in the absence of myelin assembly: posttranslational regulation of the level of expression by Schwann cells. Brunden, K.R., Poduslo, J.F. J. Cell Biol. (1987) [Pubmed]
  26. Progression of hepatic neoplasms is severely retarded in mice lacking the bisecting N-acetylglucosamine on N-glycans: evidence for a glycoprotein factor that facilitates hepatic tumor progression. Bhaumik, M., Harris, T., Sundaram, S., Johnson, L., Guttenplan, J., Rogler, C., Stanley, P. Cancer Res. (1998) [Pubmed]
  27. Cerebral hypoplasia and craniofacial defects in mice lacking heparan sulfate Ndst1 gene function. Grobe, K., Inatani, M., Pallerla, S.R., Castagnola, J., Yamaguchi, Y., Esko, J.D. Development (2005) [Pubmed]
  28. Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression. Uchimura, K., El-Fasakhany, F.M., Hori, M., Hemmerich, S., Blink, S.E., Kansas, G.S., Kanamori, A., Kumamoto, K., Kannagi, R., Muramatsu, T. J. Biol. Chem. (2002) [Pubmed]
  29. Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions. Griffitts, J.S., Huffman, D.L., Whitacre, J.L., Barrows, B.D., Marroquin, L.D., Müller, R., Brown, J.R., Hennet, T., Esko, J.D., Aroian, R.V. J. Biol. Chem. (2003) [Pubmed]
  30. In vitro heparan sulfate polymerization: crucial roles of core protein moieties of primer substrates in addition to the EXT1-EXT2 interaction. Kim, B.T., Kitagawa, H., Tanaka, J., Tamura, J., Sugahara, K. J. Biol. Chem. (2003) [Pubmed]
  31. Chromatographic resolution and kinetic characterization of glucokinase from islets of Langerhans. Meglasson, M.D., Burch, P.T., Berner, D.K., Najafi, H., Vogin, A.P., Matschinsky, F.M. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  32. Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies. Turner, J.R., Tartakoff, A.M., Greenspan, N.S. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  33. Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Davis, L.I., Blobel, G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  34. Origin of the classical complement pathway: Lamprey orthologue of mammalian C1q acts as a lectin. Matsushita, M., Matsushita, A., Endo, Y., Nakata, M., Kojima, N., Mizuochi, T., Fujita, T. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  35. The inducible N-acetylglucosamine catabolic pathway gene cluster in Candida albicans: discrete N-acetylglucosamine-inducible factors interact at the promoter of NAG1. Kumar, M.J., Jamaluddin, M.S., Natarajan, K., Kaur, D., Datta, A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
 
WikiGenes - Universities