[C@H] ([C@@H](/C=C/CCCCCCCCCCCCC)O)(NC(=O)*)CO[C@@H]1O[C@@H]([C@@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O[C@@H]4O[C@@H]([C@H](O)[C@@H]([C@H]4O)O)CO)[C@H](O)[C@H](O3)CO)NC(C)=O)[C@H]([C@@H](CO)O2)O)O)[C@@H]([C@H]1O)O)CO |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
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View more via ChEBI Ontology
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Outgoing
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β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1')-Cer
(CHEBI:17292)
has role
mouse metabolite
(CHEBI:75771)
β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1')-Cer
(CHEBI:17292)
is a
β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide
(CHEBI:90800)
β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1')-Cer
(CHEBI:17292)
is a
D-galactosyl-N-acetyl-D-glucosaminyl-(1→3)-D-galactosyl-(1→4)-D-glucosylceramide
(CHEBI:20971)
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N-[(2S,3R,4E)-1-[β-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→3)-β-D-galactopyranosyl-(1→4)-β-D-glucopyranosyloxy]-3-hydroxyoctadec-4-en-2-yl]alkanamide
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(Gal)2 (Glc)1 (GlcNAc)1 (Cer)1
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KEGG GLYCAN
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1,3-beta-D-Galactosyl-N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-D-glucosylceramide
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KEGG COMPOUND
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a β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-(1↔1ʼ)-Cer(d18:1(4E))
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UniProt
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β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-Glc-Cer
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ChEBI
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β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosylceramide
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ChEBI
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β-D-Galp-(1→3)-β-D-GlcpNAc-(1→3)-β-D-Galp-(1→4)-β-D-Glcp-(1↔1')-Cer
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ChEBI
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β-D-Galp-(1→3)-β-D-GlcpNAc-(1→3)-β-D-Galp-(1→4)-β-D-Glcp-Cer
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ChEBI
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Ceramidetetrasaccharide
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KEGG COMPOUND
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lactotetraosyl ceramide
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ChEBI
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lactotetraosylceramide
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ChEBI
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Lc4Cer
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KEGG COMPOUND
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Paragloboside
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KEGG COMPOUND
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paragloboside (β 1→3)
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ChEBI
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Henry S, Jovall PA, Ghardashkhani S, Elmgren A, Martinsson T, Larson G, Samuelsson B (1997)
Structural and immunochemical identification of Le(a), Le(b), H type 1, and related glycolipids in small intestinal mucosa of a group O Le(a-b-) nonsecretor.
Glycoconjugate journal 14, 209-223 [PubMed:9111138]
[show Abstract]
Total nonacid glycosphingolipids were isolated from small intestine mucosal scrapings of a red cell blood group O Le(a-b-) nonsecretor cadaver. Glycolipids were extracted and fractionated into five fractions based on chromatographic and immunostaining properties. These glycolipid fractions were then analysed by thin-layer chromatography for Lewis activity with antibodies reactive to the type 1 precursor (Le(c)), H type 1 (Le(d)), Le(a) and Le(b) epitopes. Fractions were structurally characterized by mass spectrometry (EI-MS and EI-MS/MS-TOF) and proton NMR spectroscopy. EI-MS/MS-TOF allowed for the identification of trace substances in fractions containing several other glycolipid species. Consistent with the red cell phenotype, large amounts of lactotetraosylceramide (Le(c)-4) were detected. Inconsistent with the red cell phenotype, small quantities of Le(a)-5, H-5-1 and Le(b)-6 glycolipids were immunochemically and structurally identified in the small intestine of this individual. By EI-MS/MS-TOF several large glycolipids with 9 and 10 sugar residues were also identified. The extensive carbohydrate chain elongation seen in this individual with a Lewis negative nonsecretor phenotype supports the concept that Lewis and Secretor blood group fucosylation may be a mechanism to control type 1 glycoconjugate chain extension. | Yu H, Sipes JM, Cashel J, Bakos MA, Goldblum RM, Roberts DD (1995)
Recognition of type 1 chain oligosaccharides and lacto-series glycolipids by an antibody to human secretory component.
Archives of biochemistry and biophysics 322, 299-305 [PubMed:7574700]
[show Abstract]
Binding of the mouse IgM antibody 6C4 is lost after treatment of human free secretory component with peptide N-glycosidase F (Bakos et al. (1991) J. Immunol. 146, 162-168) or periodate, suggesting that asparagine-linked oligosaccharides contain the epitope recognized by this antibody. Inhibition of antibody binding to free secretory component by milk oligosaccharides established that lacto-N-tetraose is the minimum structure recognized by the antibody, but larger oligosaccharides with terminal Gal beta 1-3GlcNAc sequences bind with much higher affinity. Antibody binding is enhanced by substitution with the Lewis Fuc alpha 1-4 and is inhibited by Fuc alpha 1-2Gal substitution. Free secretory component, however, does not bind other antibodies that recognize Le(a) or Leb oligosaccharides, and binding is lost after digestion with a beta-galactosidase that cleaves Gal beta 1-3 linkages but not after digestion with alpha-L-fucosidase. Therefore, the major epitope recognized by 6C4 on free secretory component is probably not an asparagine-linked Le(a) oligosaccharide. The antibody also binds to human milk lactoferrin, some human mucins, and lacto-series glycolipids including III4 alpha Fuc-lactotetraosyl ceramide and lactotetraosyl ceramide. Based on affinity chromatography of oligosaccharides released from free secretory component, the epitope recognized by antibody 6C4 is present on approximately 3.5% of the asparagine-linked oligosaccharides. | Rydberg L, Breimer ME, Holgersson J, Karlsson KA, Nyholm PG, Pascher I, Svensson L, Samuelsson BE (1992)
Characterisation of the anti-A antibody response following an ABO incompatible (A2 to O) kidney transplantation.
Molecular immunology 29, 547-560 [PubMed:1373469]
[show Abstract]
Anti-A,B antibodies produced in a blood group OLe(a-b-) recipient receiving a kidney graft from a blood group A2Le(a-b+) donor have been analysed for their ability to bind to different glycosphingolipid antigens. Solid-phase RIA using pure glycosphingolipid antigens and a chromatogram binding assay using total nonacid glycosphingolipid fractions from erythrocytes of different human blood group phenotypes together with pure glycolipid antigens were used as assay systems. Serum antibodies were shown to bind equally well to A (types 1, 2, 3 and 4) and B (types 1 and 2) antigenic structures but no binding to H antigens (types 1, 2 and 4) was detected. After adsorption of serum antibodies on A1 Le(a-b+) erythrocytes there was a residual anti-A antibody activity which could not be adsorbed by synthetic A-trisaccharides coupled to crystalline silica (Synsorb-A). These residual antibodies, which are not present in a pretransplant serum sample, had a specificity for the A antigen with type 1 core saccharide chain and the binding epitope obviously included both the N-acetylgalactosamine and the N-acetylglucosamine. The fucose residue was apparently not obligate for binding. The conformation of the sugar units involved in the binding epitope was determined. | Holmes EH, Hakomori S, Ostrander GK (1987)
Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic adenocarcinoma and derived cell lines is due to activation of a normally unexpressed beta 1----3N-acetylglucosaminyltransferase.
The Journal of biological chemistry 262, 15649-15658 [PubMed:2960671]
[show Abstract]
Human colonic adenocarcinoma tissue and derived cell lines have been characterized by an abundance of different type 1 and 2 lacto series glycolipid antigens which are either low or not found in normal colonic mucosa. The enzymatic basis for the expression of contrasting glycolipid compositions between adenocarcinomas and normal colonic mucosa, as well as between derived cell lines, has been studied. The following results were of particular interest. (i) Abundant activities of beta 1----4galactosyltransferase associated with synthesis of both lactosylceramide and lactoneotetraosylceramide, beta 1----3galactosyltransferase for synthesis of lactotetraosylceramide, and an alpha 1----3/4fucosyltransferase responsible for synthesis of Lex and Lea antigens were found in normal colonic mucosa or in a normal mucosal epithelial cell line HCMC, or in both. Variable levels of these activities were found in adenocarcinoma tissues and in various established adenocarcinoma cell lines. In striking contrast, significant activity of a beta 1----3N-acetylglucosaminyltransferase responsible for synthesis of lactotriaosylceramide (Lc3) was found in various cases of colonic adenocarcinoma and cell lines, but was undetectable in normal colonic epithelial cells. (ii) In situ transfer of galactose to Lc3 was performed on histologic sections by preincubation of the tissue with acceptor glycolipid followed by incubation with UDP-galactose. The biosynthesized glycolipid was revealed by indirect immunofluorescence with the monoclonal antibody 1B2 which defines lactoneotetraosylceramide antigen. In these studies, histologic sections prepared from frozen normal proximal colon tissue were shown to lack native type 2 chain structures. However, transfer of galactose from UDP-galactose could be demonstrated in the epithelial cells of normal proximal colon after incorporation of Lc3 into the membranes, indicating the ability of normal colonic epithelial cells to synthesize type 2 chain core structures if the precursor Lc3 is available. In contrast, adenocarcinoma tissues showed significant native immunofluorescence with the antibody. These data suggest that an accumulation of both type 1 and 2 chain lacto series glycolipids with alpha 1----3- or alpha 1----4fucosyl substitution in human adenocarcinoma is due to enhanced beta 1----3N-acetylglucosaminyltransferase rather than enhancement of other enzymes. This enzyme may play a key role in regulating the level of various types of lacto series tumor-associated antigens with the lacto type 1 or 2 chain. |
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