CHEBI:17716 - lactose

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ChEBI Name lactose ChEBI ID CHEBI:17716 Definition A glycosylglucose disaccharide, found most notably in milk, that consists of D-galactose and D-glucose fragments bonded through a β-1→4 glycosidic linkage. The glucose fragment can be in either the α- or β-pyranose form, whereas the galactose fragment can only have the β-pyranose form. Stars This entity has been manually annotated by the ChEBI Team. Secondary ChEBI IDs CHEBI:27755, CHEBI:22760, CHEBI:14497, CHEBI:10296, CHEBI:22460, CHEBI:25005, CHEBI:613009, CHEBI:10380, CHEBI:27968, CHEBI:28577 Supplier Information ChemicalBook:CB8710411 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C12H22O11 Net Charge 0 Average Mass 342.297 Monoisotopic Mass 342.11621 InChI InChI=1S/C12H22O11/c13-1-3-5(15)6(16)9(19)12(22-3)23-10-4(2-14)21-11(20)8(18)7(10)17/h3-20H,1-2H2/t3-,4-,5+,6+,7-,8-,9-,10-,11?,12+/m1/s1 InChIKey GUBGYTABKSRVRQ-QKKXKWKRSA-N SMILES OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O Metabolite of Species Details Homo sapiens (NCBI:txid9606) See: DOI Roles Classification Biological Role(s): human metabolite Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens). View more via ChEBI Ontology ChEBI Ontology Outgoing lactose (CHEBI:17716) has role human metabolite (CHEBI:77746) lactose (CHEBI:17716) is a glycosylglucose (CHEBI:24405) Incoming α-L-Fucp-(1→4)-β-D-Galp-(1→4)-D-Glcp (CHEBI:146544) has functional parent lactose (CHEBI:17716) β-D-Galp-(1→3)-β-D-Galp-(1→4)-D-Glcp (CHEBI:147880) has functional parent lactose (CHEBI:17716) β-D-Galp-(1→4)-[α-D-Glcp-(1→2)]-D-Glcp (CHEBI:147953) has functional parent lactose (CHEBI:17716) β-D-Galp-(1→6)-β-D-Galp-(1→4)-D-Glcp (CHEBI:147735) has functional parent lactose (CHEBI:17716) β-D-Galp6S-(1→4)-D-Glcp (CHEBI:152163) has functional parent lactose (CHEBI:17716) β-D-GlcpNAc-(1→4)-β-D-Galp-(1→4)-D-Glcp (CHEBI:147065) has functional parent lactose (CHEBI:17716) β-D-GlcpNAc-(1→6)-β-D-Galp-(1→4)-D-Glcp (CHEBI:148195) has functional parent lactose (CHEBI:17716) β-L-Fucp-(1→4)-β-D-Galp-(1→4)-D-Glcp (CHEBI:146770) has functional parent lactose (CHEBI:17716) 2'-fucosyllactose (CHEBI:147155) has functional parent lactose (CHEBI:17716) 3-(hexadecylsulfonyl)-2-[(hexadecylsulfonyl)methyl]propyl β-D-galactosyl-(1→4)-β-D-glucoside (CHEBI:63531) has functional parent lactose (CHEBI:17716) 3-fucosyllactose (CHEBI:90065) has functional parent lactose (CHEBI:17716) D-Galp-(1→3)-β-D-Galp-(1→4)-D-Glcp (CHEBI:146614) has functional parent lactose (CHEBI:17716) D-Galp-(1→6)-β-D-Galp-(1→4)-D-Glcp (CHEBI:149402) has functional parent lactose (CHEBI:17716) lactobionic acid (CHEBI:55481) has functional parent lactose (CHEBI:17716) lactose 6'-phosphate (CHEBI:28339) has functional parent lactose (CHEBI:17716) lactose phosphate (CHEBI:25004) has functional parent lactose (CHEBI:17716) α-lactose (CHEBI:36219) is a lactose (CHEBI:17716) β-lactose (CHEBI:36218) is a lactose (CHEBI:17716) IUPAC Name β-D-galactopyranosyl-(1→4)-D-glucopyranose Synonyms Sources (+)-lactose NIST Chemistry WebBook (Gal)1 (Glc)1 KEGG GLYCAN 1-beta-D-Galactopyranosyl-4-D-glucopyranose KEGG COMPOUND 4-(β-D-galactosido)-D-glucose NIST Chemistry WebBook 4-O-β-D-galactopyranosyl-D-glucose IUPAC beta-D-Gal-(1->4)-D-Glc KEGG COMPOUND beta-D-Gal-(1->4)-D-Glc KEGG COMPOUND β-D-Galp-(1→4)-D-Glcp IUPAC β-Gal1,4-Glc ChEBI D-lactose ChemIDplus Galβ1-4Glc ChEBI Lac JCBN lactobiose NIST Chemistry WebBook lactose UniProt Laktobiose ChEBI Laktose ChEBI Milchzucker ChEBI Milk sugar KEGG COMPOUND milk sugar NIST Chemistry WebBook WURCS=2.0/2,2,1/[a2122h-1x_1-5][a2112h-1b_1-5]/1-2/a4-b1 GlyTouCan Manual Xrefs Databases C00001136 KNApSAcK C00243 KEGG COMPOUND D00046 KEGG DRUG G10504 KEGG GLYCAN G74621DY GlyGen G74621DY GlyTouCan View more database links Registry Numbers Types Sources 1292745 Reaxys Registry Number Reaxys 63-42-3 CAS Registry Number ChemIDplus 63-42-3 CAS Registry Number NIST Chemistry WebBook 882872 Gmelin Registry Number Gmelin Citations Arthurs J, Lin JY, Ocampo R, Reilly S (2017) Lactose malabsorption and taste aversion learning. Physiology & behavior 180, 39-44 [PubMed:28807538] [show Abstract] Consumption of foods can be suppressed by two feeding system defense mechanisms: conditioned taste aversion (CTA) or taste avoidance learning (TAL). There is a debate in the literature about which form of intake suppression is caused by various aversive stimuli. For instance, illness-inducing stimuli like lithium chloride are the gold standard for producing CTA and external (or peripheral) painful stimuli, such as footshock, are the traditional model of TAL. The distinction between CTA and TAL, which have identical effects on intake, is based on differential effects on palatability. That is, CTA involves a decrease in both intake and palatability, whereas TAL suppresses intake without influencing palatability. We evaluated whether lactose, which causes gastrointestinal pain in adult rats, produces CTA or TAL. Using lick pattern analysis to simultaneously measure intake and palatability (i.e., lick cluster size and initial lick rate), we found that pairing saccharin with intragastric infusions of lactose suppressed both the intake and palatability of saccharin. These results support the conclusion that gastrointestinal pain produced by lactose malabsorption produces a CTA, not TAL as had previously been suggested. Furthermore, these findings encourage the view that the CTA mechanism is broadly tuned to defend against the ingestion of foods with aversive post-ingestive effects. Storhaug CL, Fosse SK, Fadnes LT (2017) Country, regional, and global estimates for lactose malabsorption in adults: a systematic review and meta-analysis. The lancet. Gastroenterology & hepatology 2, 738-746 [PubMed:28690131] [show Abstract] Background Studies have shown wide variation in the prevalence of lactose malabsorption across the world, but no systematic reviews or meta-analyses have recently assessed the prevalence of lactose malabsorption in different geographical areas. We aimed to present an updated systematic review and meta-analysis on the prevalence of lactose malabsorption in adults, by countries and regions, and to assess the variation between different testing methods. Methods Studies reporting on prevalence of lactose malabsorption and lactase persistence were identified by searching MEDLINE and Embase from database inception to Nov 2, 2016. We evaluated studies presenting lactose malabsorption or lactase persistence prevalence data in adults and children aged 10 years or older, including cross-sectional and prospective studies, using genotyping, hydrogen breath tests, lactose tolerance tests, and other testing methods. We excluded studies in children younger than 10 years, studies using self-reported data, and studies including inpatients and outpatients at gastroenterological wards. Studies were screened by two authors (CLS and SKF) and data values were extracted by two authors (CLS and SKF) independently. The primary outcome was the prevalence of lactose malabsorption. This study is registered with PROSPERO, number CRD42017064802. Findings We screened 2665 records, and 306 study populations from 116 full-text articles were included (primary sources); data for 144 additional study populations from 59 articles were obtained from review articles, because full-text primary articles could not be obtained (secondary sources). Of the 450 study populations included, 231 were assessed by genotyping, 83 by hydrogen breath tests, 101 by lactose tolerance tests, and 35 by other methods or methods that were not described sufficiently. The studies included 62 910 participants from 89 countries (covering 84% of the world's population). When standardising for country size, the global prevalence estimate of lactose malabsorption was 68% (95% CI 64-72), ranging from 28% (19-37) in western, southern, and northern Europe to 70% (57-83) in the Middle East. When assessing the global prevalence using genotyping data only, the estimate was 74% (69-80), whereas prevalence was 55% (46-65) using lactose tolerance test data, and 57% (46-67) using hydrogen breath test data. Risk of bias was assessed based on ten indicators; 12 of the articles had a score of ten, indicating low risk of bias, 76 had a score of nine, 26 a score of eight, and two articles a score of seven (indicating higher risk of bias). There was substantial heterogeneity between studies within most of the assessed countries. Interpretation Lactose malabsorption is widespread in most of the world, with wide variation between different regions and an overall frequency of around two-thirds of the world's population. Acknowledging regional patterns of lactose malabsorption is important to guide management of gastrointestinal symptoms. Funding None. Sarabia-Sainz AI, Ramos-Clamont G, Winzerling J, Vázquez-Moreno L (2011) Bacterial recognition of thermal glycation products derived from porcine serum albumin with lactose. Acta biochimica Polonica 58, 95-100 [PubMed:21403918] [show Abstract] Recently, glyco-therapy is proposed to prevent the interaction of bacterial lectins with host ligands (glycoconjugates). This interaction represents the first step in infection. Neoglycans referred to as PSA-Lac (PSA-Glu (β1-4) Gal) were obtained by conjugation of porcine serum albumin (PSA) with lactose at 80 °C, 100 °C and 120 ºC. Characterization studies of the products showed that PSA could contain 1, 38 or 41 added lactoses, depending on the reaction temperature. These neoglycans were approximately 10 times more glycated than PSA-Lac obtained in previous work. Lactose conjugation occurred only at lysines and PSA-Lac contained terminal galactoses as confirmed by Ricinus communis lectin recognition. Furthermore, Escherichia coli K88+, K88ab, K88ac and K88ad adhesins showed affinity toward all PSA-Lac neoglycans, and the most effective was the PSA-Lac obtained after 100 ºC treatment. In vitro, this neoglycan partially inhibited the adhesion of E. coli K88+ to piglet mucin (its natural ligand). These results provide support for the hypothesis that glycated proteins can be used as an alternative for bioactive compounds for disease prevention. Wu JH, Wu AM, Yang Z, Chen YY, Singha B, Chow LP, Lin JY (2010) Recognition intensities of submolecular structures, mammalian glyco-structural units, ligand cluster and polyvalency in abrin-a-carbohydrate interactions. Biochimie 92, 147-156 [PubMed:19913595] [show Abstract] Abrin-a is the most toxic fraction of lectins isolated from Abrus precatorius seeds and belongs to the family of type 2 ribosome inactivating proteins (RIP). This toxin may act as a defense molecule in plants against viruses, fungi and insects, where attachment of abrin-a to the exposed glycans on the surface of target cells is the crucial and initial step of its cytotoxicity. Although it has been studied for over four decades, the recognition factors involved in abrin-a-carbohydrate interaction remains to be clarified. In this study, roles of mammalian glyco-structural units, ligand clusters and polyvalency in abrin-a recognition were comprehensively analyzed by enzyme-linked lectinosorbent binding and inhibition assays. The results indicate that: (i) this toxin prefers oligosaccharides having alpha-anomer of galactose (Gal) at the non-reducing terminal than the corresponding beta-anomer; (ii) Galalpha1-3Galalpha1- (B(alpha)), Galalpha1-4Gal (E), Galbeta1-3GalNAc (T) and Galbeta1-3/4GlcNAc (I/II) related oligosaccharides were the active glyco-structural units; (iii) tri-antennary II(beta), prepared from N-glycan of asialo fetuin, played a dominant role in recognition; (iv) many high-density polyvalent I(beta)/II(beta) and E(beta) glycotopes enhanced the reactivity; (v) the carbohydrate recognition domain of abrin-a is proposed to be a combination of a small cavity type of Gal as major site and a groove type of additional one to tetrasaccharides as subsites with a preference of alpha1-3/4/6Gal, beta1-3GalNAc, beta1-3/4/6GlcNAc, beta1-4/6Glc, beta1-3DAra and beta1-4Man as subterminal sugars; (vi) size of the carbohydrate recognition domain may be as large enough to accommodate a linear pentasaccharide and complementary to Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc (gailipenta) sequence. A comparison of the recognition factors and combining sites of abrin-a with ricin, another highly toxic lectin, was also performed to further understand the differences in recognition factors between these two type 2 RIPs. Ohshiro T, Ohmoto Y, Ono Y, Ohkita R, Miki Y, Kawamoto H, Izumi Y (2010) Isolation and characterization of a novel fucoidan-degrading microorganism. Bioscience, biotechnology, and biochemistry 74, 1729-1732 [PubMed:20699559] [show Abstract] A bacterium utilizing fucoidan from the brown alga Cladosiphon okamuranus as sole carbon source was isolated and identified as Flavobacterium sp. F-31. The strain produced intracellular enzymes involved in fucoidan degradation and desulfation, but desulfation activity was not detected until the molecular weight of fucoidan fell to less than several tens of thousands due to enzymatic degradation. Only fucoidan proved to be an inducible substance for the production of the degrading enzymes. Kumar A, Ramanujam B, Singhal NK, Mitra A, Rao CP (2010) Interaction of aromatic imino glycoconjugates with jacalin: experimental and computational docking studies. Carbohydrate research 345, 2491-2498 [PubMed:20961532] [show Abstract] Altering the lectin properties by chemically modified glycoconjugates can have profound effect on their biological applications. In the present case, jacalin has been chosen to study the binding aspects toward glycoconjugates modified by connecting aromatic moieties through imine conjugation at their C-1- or C-2-positions. Out of 10 glycoconjugates, the galactosyl-naphthyl imine (1c) was found to be most effective toward agglutination inhibition (260 times better than galactose), quenching fluorescence intensity, and exhibiting greater binding (K(a), 1.3 × 10(4)M(-1)) with jacalin. The specific binding of galactose conjugates and the nonspecific binding of other conjugates have been demonstrated based on ITC. Changes in the secondary structures have been addressed by far- and near-UV CD spectroscopy. The present studies demonstrated that galactose-based conjugates bind at carbohydrate recognition domain (CRD) mainly through polar interactions in addition to exhibiting some nonpolar/hydrophobic interactions, whereas the conjugates other than galactose primarily interact through hydrophobic interactions. Binding of galactosyl conjugates at CRD has been further demonstrated by rigid docking. Ribeiro JP, André S, Cañada FJ, Gabius HJ, Butera AP, Alves RJ, Jiménez-Barbero J (2010) Lectin-based drug design: combined strategy to identify lead compounds using STD NMR spectroscopy, solid-phase assays and cell binding for a plant toxin model. ChemMedChem 5, 415-9, 314 [PubMed:20094999] [show Abstract] The growing awareness of the sugar code--i.e. the biological functionality of glycans--is leading to increased interest in lectins as drug targets. The aim of this study was to establish a strategic combination of screening procedures with increased biorelevance. As a model, we used a potent plant toxin (viscumin) and lactosides synthetically modified at the C6/C6' positions and the reducing end aglycan. Changes in the saturation transfer difference (STD) in NMR spectroscopy, applied in inhibition assays, yielded evidence for ligand activity and affinity differences. Inhibitory potency was confirmed by the blocking of lectin binding to a glycoprotein-bearing matrix. In cell-based assays, iodo/azido-substituted lactose derivatives were comparatively active. Interestingly, cell-type dependence was observed, indicating the potential of synthetic carbohydrate derivative to interact with lectins in a cell-type (glycan profile)-specific manner. These results are relevant to research into human lectins, glycosciences, and beyond. Diehl C, Engström O, Delaine T, Håkansson M, Genheden S, Modig K, Leffler H, Ryde U, Nilsson UJ, Akke M (2010) Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3. Journal of the American Chemical Society 132, 14577-14589 [PubMed:20873837] [show Abstract] Rational drug design is predicated on knowledge of the three-dimensional structure of the protein-ligand complex and the thermodynamics of ligand binding. Despite the fundamental importance of both enthalpy and entropy in driving ligand binding, the role of conformational entropy is rarely addressed in drug design. In this work, we have probed the conformational entropy and its relative contribution to the free energy of ligand binding to the carbohydrate recognition domain of galectin-3. Using a combination of NMR spectroscopy, isothermal titration calorimetry, and X-ray crystallography, we characterized the binding of three ligands with dissociation constants ranging over 2 orders of magnitude. (15)N and (2)H spin relaxation measurements showed that the protein backbone and side chains respond to ligand binding by increased conformational fluctuations, on average, that differ among the three ligand-bound states. Variability in the response to ligand binding is prominent in the hydrophobic core, where a distal cluster of methyl groups becomes more rigid, whereas methyl groups closer to the binding site become more flexible. The results reveal an intricate interplay between structure and conformational fluctuations in the different complexes that fine-tunes the affinity. The estimated change in conformational entropy is comparable in magnitude to the binding enthalpy, demonstrating that it contributes favorably and significantly to ligand binding. We speculate that the relatively weak inherent protein-carbohydrate interactions and limited hydrophobic effect associated with oligosaccharide binding might have exerted evolutionary pressure on carbohydrate-binding proteins to increase the affinity by means of conformational entropy. Tompkins L, Lynch C, Haidar S, Polli J, Wang H (2010) Effects of commonly used excipients on the expression of CYP3A4 in colon and liver cells. Pharmaceutical research 27, 1703-1712 [PubMed:20503067] [show Abstract] Purpose The objective of this investigation was to assess whether common pharmaceutical excipients regulate the expression of drug-metabolizing enzymes in human colon and liver cells. Methods Nineteen commonly used excipients were evaluated using a panel of experiments including cell-based human PXR activation assays, real-time RT-PCR assays for CYP3A4 mRNA expression, and immunoblot analysis of CYP3A4 protein expression in immortalized human liver cells (HepG2 and Fa2N4), human primary hepatocytes, and the intestinal LS174T cell models. Results No excipient activated human PXR or practically induced CYP3A4. However, three excipients (polysorbate 80, pregelatinized starch, and hydroxypropyl methylcellulose) tended to decrease mRNA and protein expression across experimental models. Conclusion This study represents the first investigation of the potential role of excipients in the expression of drug-metabolizing enzymes. Findings imply that some excipients may hold potential for excipient-drug interactions by repression of CYP3A4 expression. Adhya M, Singha B, Chatterjee BP (2009) Macoma birmanica agglutinin recognizes glycoside clusters of beta-GlcNAc/Glc and alpha-Man. Carbohydrate research 344, 2489-2495 [PubMed:19846069] [show Abstract] Macoma birmanica agglutinin (MBA) that seems to play crucial roles in the innate immunity of marine bivalve, M. birmanica has been earlier defined as GlcNAc/Man specific. However, most complementary carbohydrate structures to its binding domain and ligand clustering in its recognition profile have not been established. In this study, the complete recognition profile of MBA was examined by enzyme-linked lectin-sorbent assay and inhibition assay. Among the monosaccharides tested, GlcNAc was more reactive followed by Man and Glc, others were non-reactive; revealing the importance of equatorial -NAc group at C-2, -OH group at C-4 and C-6, and pyranose conformation of hexose. Moreover, beta-glycosides of GlcNAc and Glc were more potent whereas for Man it was alpha-glycoside. MBA recognized both exposed and internal alpha-Man and beta-GlcNAc/Glc residues well with most linkages except (beta1-4). This binding pattern was further extended and confirmed by polyvalent glycoside clusters of GlcNAc(beta1-2)Man(alpha1-, which was a better inhibitor than Man(alpha1-2/3/6)Man(alpha1- or Man(alpha1-3/6)Man(beta1- present in well-defined naturally occurring glycoproteins. This broad range specificity explains the importance of MBA as an important pattern recognition molecule that provides more realistic picture of carbohydrate-based immune response triggering. Buchini S, Buschiazzo A, Withers SG (2008) A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors. Angewandte Chemie (International ed. in English) 47, 2700-2703 [PubMed:18300214] Delaine T, Cumpstey I, Ingrassia L, Le Mercier M, Okechukwu P, Leffler H, Kiss R, Nilsson UJ (2008) Galectin-inhibitory thiodigalactoside ester derivatives have antimigratory effects in cultured lung and prostate cancer cells. Journal of medicinal chemistry 51, 8109-8114 (Source: ChEMBL) [PubMed:19053747] [show Abstract] Aromatic 3,3'-diesters of thiodigalactoside were synthesized in a rapid three-step sequence from commercially available thiodigalactoside and evaluated as inhibitors of cancer- and immunity-related galectins. For each of galectins-1, -3, -7, and -9N-terminal domain, aromatic 3,3'-diesters of thiodigalactoside were found to have affinities in the low micromolar range, which represents a 7-70 fold enhancement over thiodigalactoside itself. No significant improvement was found for galectin-8 N-terminal domain. Two of the compounds were selected for testing in cell culture and were shown to have potent antimigratory effects on human PC-3 prostate and human A549 nonsmall-cell lung cancer cells. Nakatani S, Mano H, Im R, Shimizu J, Wada M (2007) Glucosamine regulates differentiation of a chondrogenic cell line, ATDC5. Biological & pharmaceutical bulletin 30, 433-438 [PubMed:17329833] [show Abstract] Osteoarthritis (OA) is a slowly progressing chronic joint disease. Glucosamine (GlcN) is a saccharide that is widely used to relieve symptoms associated with OA. However, the mechanism of the effects of GlcN on articular cartilage remains unclear. We studied the effects of GlcN and its analogues, including chitin derivatives included in health supplements containing GlcN, on a chondrogenic cell line, ATDC5. We examined the effects of these saccharides on the proliferation and differentiation of ATDC5 cells. Glucosamine analogues, such as N-acetyl glucosamine and chitobiose, did not affect the proliferation or differentiation of ATDC5 cells. While GlcN did not affect the proliferation of ATDC5 cells, it inhibited their differentiation. Next, we examined whether GlcN affects mineralization and glycosaminoglycan (GAG) production by ATDC5 cells. Mineralization was markedly inhibited by addition of GlcN to the cell culture medium. Moreover, GlcN induced the formation of sulfated GAG in ATDC5. We also analyzed the mRNA levels in ATDC5 cells. GlcN reduced the mRNA levels of Smad2, Smad4 and MGP. GlcN might inhibit expression of MGP mRNA and induce the production of chondroitin sulfate in ATDC5 cells. The mechanism by which GlcN inhibits mineralization may be by regulating the expression of mRNA for the Smad2 and Smad4 chondrogenic master genes. 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. Tanaka K, Yamamoto M, Matsumoto M, Saito M, Funabashi M, Yoshimatsu S (1992) [An outbreak of food poisoning suspected due to Aeromonas and characteristics of the isolated strains]. [Nihon koshu eisei zasshi] Japanese journal of public health 39, 707-713 [PubMed:1292745] [show Abstract] On June 7, 1990, food poisoning with main symptoms of abdominal pain and diarrhea occurred in Inuyama City, Aichi Prefecture. From results of bacteriological examination, three kinds of mesophilic Aeromonas spp. were detected from patients, leftover foods, well water, and cookers, one of which was A. hydrophila which was shown to produce haemolysin thought to be the cause of the food poisoning. On the other hand, A. sobria and A. caviae isolated from various materials did not produce haemolysin. The latter two strains of mesophilic Aeromonas spp. did not produce any other enterotoxins. Therefore, it appears that the well water containing A. hydrophila, A. sobria and A. caviae polluted the foods, which then had caused the food poisoning. Of nine strains of A. hydrophila, five do not dissolve sucrose, and these are typed as serogroup O:22 or O:23. The other four strains dissolve sucrose, and these are typed as serogroup O:16. According to the drug sensitivity test, all of these nine strains of A. hydrophila were resistant to Ampicillin, Erythromycin and Cephaloridine. Brodin NT, Dahmén J, Nilsson B, Messeter L, Mårtensson S, Heldrup J, Sjögren HO, Lundblad A (1988) Monoclonal antibodies produced by immunization with neoglycoproteins containing Gal alpha 1-4Gal beta 1-4Glc beta-O and Gal alpha 1-4Gal beta 1-4GlcNAc beta-O residues: useful immunochemical and cytochemical reagents for blood group P antigens and a differentiation marker in Burkitt lymphoma and other B-cell malignancies. International journal of cancer 42, 185-194 [PubMed:2456994] [show Abstract] Several monoclonal antibodies (MAbs) directed to blood group P1 (Gal alpha 1-4Gal beta 1-4GlcNAc beta-O) and Pk (Gal alpha 1-4Gal beta 1-4Glc beta-O) determinants were produced with high efficiency by using synthetic neoglycoproteins as immunogens. The specificity of IgM and IgG1 MAbs was characterized by binding to defined oligosaccharides and glycoconjugates. Antibodies that bound equally well to P1 and Pk determinants and to Gal alpha 1-4Gal beta 1-O-derivatives were obtained, together with others that showed selective recognition of the entire trisaccharide chain. Selected antibodies were shown to be useful as reagents for detection of the blood group P antigens in glycolipid extracts of erythrocytes and on the surface of erythrocytes of different P phenotypes, demonstrated both by radioimmune assays and hemagglutination. Six IgM MAbs directed to the Pk determinant bound selectively to Burkitt lymphoma cells and 2 of these antibodies (424/3D9 and 424/6A2) could be used as auxiliary reagents in immunofluorescence for diagnosis and classification of B-cell lymphomas and leukemias using flow cytometric analysis. Eight normal individuals and 37 patients with lymphoma or leukemia were studied. Tumor cells of 2/2 patients with "Burkitt-like" lymphoma, 1 patient with centroblastic lymphoma and 2 patients with acute leukemia were strongly stained for the Pk antigen. The staining patterns for differentiation markers classified the tumor cells to a developmental stage closely related to the Burkitt cell type. Uchigata Y, Spitalnik SL, Tachiwaki O, Salata KF, Notkins AL (1987) Pancreatic islet cell surface glycoproteins containing Gal beta 1-4GlcNAc-R identified by a cytotoxic monoclonal autoantibody. The Journal of experimental medicine 165, 124-139 [PubMed:2432147] [show Abstract] To investigate the autoimmune pathogenesis of spontaneously occurring diabetes mellitus in BB rats, spleen cells of newly diagnosed diabetic BB rats were fused with mouse myeloma cells. Hybridoma supernatants were screened for antibodies by indirect immunofluorescence and by 51Cr-release assays using the RINm5F rat insulinoma cell line. One clone, E5C2, produced an IgM kappa antibody that was cytotoxic for RINm5F cells, but not for other rat cell lines nor for primary rat islet cells. However, treatment of primary rat islet cells with neuraminidase exposed surface antigens and rendered the cells susceptible to complement-mediated lysis by antibody E5C2. Using immunostaining of glycolipids separated by thin-layer chromatography, hapten inhibition assays with defined carbohydrates, and Western blots, the antigens recognized by E5C2 on RINm5F cells were identified as glycoproteins with molecular weights of 60,000 and 68,000. The antibody recognizes a carbohydrate antigen containing the sequence Gal beta 1-4GlcNAc-R, which on RINm5F cells is predominantly hidden by covalently bound sialic acid. These studies raise the possibility that hidden antigenic determinants on islet cells exposed by a variety of means may be the target of autoimmune attack. Gooi HC, Uemura K, Edwards PA, Foster CS, Pickering N, Feizi T (1983) Two mouse hybridoma antibodies against human milk-fat globules recognise the I(Ma) antigenic determinant beta-D-Galp-(1 leads to 4)-beta-D-GlcpNAc-(1 leads to 6). Carbohydrate research 120, 293-302 [PubMed:6194884] [show Abstract] Two mouse hybridoma antibodies (LICR-LON-M39 and LICR-LON-M18) against the human-milk-fat globules were found to resemble human autoantibodies of anti-I type in their cold agglutinating property and their preferential reactions with erythrocytes of I- rather than i-type. From inhibition of binding assays with glycoproteins having known A, B, H, Lea, Leb, I, and i activities, and oligosaccharides of the Type 1 and Type 2 lacto-N-glycosyl series, it was established that these antibodies are directed at Type 2 structures, and that the I(Ma) determinant, beta-D-Galp-(1 leads to 4)-beta-D-GlcpNAc-(1 leads to 6), which is usually found on branched oligosaccharides, is the preferred sequence. The hybridoma antibodies as well as anti-I Ma were shown to react well with the beta-D-Galp-(1 leads to 4)-beta-D-GlcpNAc-(1 leads to 6)-D-Gal or -D-Man sequence. Studies of the reactions of these antibodies with glycolipids on thin-layer plates showed that the two hybridoma antibodies differ from anti-I Ma in reacting weakly with the unbranched i-type sequence beta-D-Galp-(1 leads to 4)-beta-D-GlcpNAc-(1 leads to 3)-beta-D-Galp-(1 leads to 4)-beta-D-GlcpNAc-(1 leads to 3)-beta-D-galp-(1 leads to 4) as found on lacto-N-norhexasylceramide. Furthermore, they differ from anti-I Ma but resemble anti-I Woj and Sti, and a hybridoma antibody 1B2 in their failure to react with their determinant in the presence of alpha-D-(1 leads to 3)-linked galactosyl groups. From their lack of reactions with blood-group-A and -H active glycoproteins, and their reactions with neuraminidase-treated erythrocytes, it was deduced that the determinants recognised by the two hybridoma antibodies are also masked in the presence of alpha-L-(1 leads to 2)-linked fucosyl groups and sialic acid. Last Modified 09 April 2021