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Chemical Compound Review

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

Synonyms: Aflexa, GlcNAc, NAcGlc, Maxi GS, CID899, ...
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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 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].


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