Lectin affinity high-performance liquid chromatography: Interactions of N-glycanase-released oligosaccharides with leukoagglutinating phytohemagglutinin, concanavalin A, Datura stramonium agglutinin, and Vicia villosa agglutinin

Green, Eric D.; Brodbeck, Robbin; Baenziger, Jacques U.

doi:10.1016/0003-2697(87)90134-5

Cited by 67 publications

(43 citation statements)

References 35 publications

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“…These inhibitiory effects were irreversible in the presence of 30 mM galactose. Effect of RCA120 on the histamine release induced by compound 48/80, bradykinin and PEI6 The effects of RCA120 on the histamine re lease in the presence of 1 mM calcium were examined, because it hardly binds to the glyco proteins rich in sialic acid residues (18). We found that RCA120 had only a small effect on the histamine release induced by compound 48/80 and PEI6 and was ineffective on that by bradykinin ( Table 2).…”

Section: Chemicalsmentioning

confidence: 90%

Sugar-Specific Inhibitory Effects of Wheat Germ Agglutinin and Phytohemagglutinin-E4 on Histamine Release Induced by Basic Secretagogues from Rat Peritoneal Mast Cells and Their Possible Action Sites

Suzuki-Nishimura

Nagaya

Matsuda

et al. 1991

Japanese Journal of Pharmacology

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ABSTRACT-The histamine release induced by compound 48/80, bradykinin or polyethylenimine with a molecular weight of 600 (PEI6) was inhibited by wheat germ agglutinin (WGA) and phytohemagglutinin E-subunits (PHA-E4), and the inhibition was specifically reversed by N-acetyl glucosamine and N-acetyl galactosamine, respec tively. Concanavalin A (Con A) and phytohemagglutinin L-subunits (PHA-L4) did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI6. The histamine release induced by substance P was also inhibited sugar-specifically by WGA and PHA-E4. The binding sites for compound 48/80, bradykinin, PEI6 and sub stance P, therefore, seemed to especially overlap each other. These binding sites were found to be glycoproteins having affinities to WGA and PHA-E4, but not to Con A and PHA-L4. The binding of WGA and PHA-E4 to the glycoproteins resulted in inhibition of the interaction between the basic secretagogues including bradykinin and substance P and their binding sites on the mast cells. The bindings of five lectins to mast cell glycoproteins were examined by lectin-blotting. Several glycoproteins, which had specific affinities to WGA and PHA-E4, but not to Con A and PHA-L4 were de tected. We assumed that the binding sites for basic secretagogues which are coupled with histamine-releasing mechanisms exist among these glycoproteins. A 41-kDa pro tein (a-subunit of pertussis toxin-sensitive G protein) was not detected by WGA, sug gesting that the binding sites for the basic secretagogues were not G proteins.Stimulus-secretion coupling mechanisms in rat peritoneal mast cells are thought to involve G proteins, because GTP-analogues enhanced histamine release (1). Moreover, histamine re lease induced by compound 48/80 or brady kinin is inhibited by pertussis toxin, but that induced by antigen or anti-IgE is not (2-4). We found that the histamine release induced by polyethylenimine (MW = 600, PEI6) was inhibited by pertussis toxin (5). Compound 48/80, bradykinin and polyethylenimine are all basic secretagogues. There is, however, no similarity in their chemical structures. The ac tion sites for compound 48/80 on the plasma

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Section: Chemicalsmentioning

confidence: 90%

Sugar-Specific Inhibitory Effects of Wheat Germ Agglutinin and Phytohemagglutinin-E4 on Histamine Release Induced by Basic Secretagogues from Rat Peritoneal Mast Cells and Their Possible Action Sites

Suzuki-Nishimura

Nagaya

Matsuda

et al. 1991

Japanese Journal of Pharmacology

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“…Lectin histochemistry [for lectin specificity refer to; 2, 13,14,17,25,30,31] was performed using the respective biotinylated lectin (Honen Co. Ltd., Japan), as illustrated in Table 2. Deparaffinized and hydrated sections were treated Table 2, by the substitution of unconjugated lectins for biotinylated lectin-conjugates, and by the exposure of sections to the PO-DAB system without lectin.…”

Section: Histology and Histochemistrymentioning

confidence: 99%

“…Since PNA and RCA-120 lose their binding affinity due to the existence of sialic acid residues at terminal positions of the sugar chain [2,14,17], the neuraminidase digestion was performed prior to reaction with PNA and RCA-120. To substantiate the sialic acid binding specificities of the SSA and MAA lectins, digestion with neuraminidase was performed prior to the particular lectin stainings.…”

Section: Enzyme Digestions and Saponificationmentioning

confidence: 99%

Histochemical Analysis of Glycoconjugates in the Disseminate Prostate Gland of the Wild Boar (Sus scrofa riukiuanus)

Sakairi

Tsukise

Nara

et al. 2003

Acta Histochem. Cytochem

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The results obtained in the present study demonstrated the precise localization and characterization of glycoconjugates in the disseminate prostate gland of the wild boar, using glycohistochemical methods including lectin techniques in light microscopy. According to the present results, it was apparent that glycoconjugates with neutral and acidic groupings were contained in the secretory epithelial cells and luminal secretions. In these glycoconjugates, a series of saccharide residues were visualized such as a-D-glucose, a-D-mannose, a-Lfucose, b-D-galactose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, and N-acetyl-neuraminic acid (sialic acid). In addition, an abundance of glycoconjugates with terminal sialic acids was revealed in the peripheral parts of the prostate gland, as compared with its central parts. The terminal saccharide residues of glycoconjugates were more abundant in Siaa2-6Gal/GalNAc than those in Siaa2-3Galb1-4GlcNAc. Furthermore, some specifically MAA reactive acinous cells were detected in the glandular epithelium. The present histochemical results provide useful information regarding the close correlation between the physiological role of the disseminate prostate gland and the glandular glycoconjugates in the wild boar.

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“…A member of the A-B family of toxins, ricin is comprised of a single enzymatic 'A' subunit and a single lectin-like 'B' subunit (20). The ricin B subunit binds with micromolar affinity to ␤(1,4)-linked galactose residues and with slightly lower affinity to ␤(1,3)-linked galactose residues (21)(22)(23)(24), thereby mediating toxin attachment to both glycolipids and glycoproteins on epithelial cell surfaces. Once bound to the cell surface the toxin is then rapidly internalized into host cells via multiple endocytic pathways (20).…”

mentioning

confidence: 99%

Oligosaccharide Side Chains on Human Secretory IgA Serve as Receptors for Ricin

Mantis

Farrant

Mehta

2004

The Journal of Immunology

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Secretory IgA (sIgA) Abs are polymeric Igs comprised of two or more IgA monomers joined together at their C termini and covalently associated with a 70-kDa glycoprotein called secretory component. As the predominant Ig type in gastrointestinal sections, sIgA Abs are centrally important in adaptive immunity to enteropathogenic bacteria, viruses, and toxins. In this study, we demonstrate that sIgA Abs may also function in innate defense against ricin, a naturally occurring, galactose-specific plant lectin with extremely potent shiga toxin-like enzymatic activity. In lectin blot overlay assays, we found that ricin bound to secretory component and the H chain of human IgA, and this binding was inhibited by the addition of excess galactose. The toxin also recognized IgM (albeit with less affinity than to IgA), but not IgG. Ricin bound to both human IgA1 and IgA2, primarily via N-linked oligosaccharide side chains. At 100-fold molar excess concentration, sIgA (but not IgG) Abs inhibited ricin attachment to the apical surfaces of polarized intestinal epithelial cells grown in culture. sIgA Abs also visibly reduced toxin binding to the luminal surfaces of human duodenum in tissue section overlay assays. We conclude that sIgA Abs in mucosal secretions may serve as receptor analogues for ricin, thereby reducing the effective dose of toxin capable of gaining access to glycolipid and glycoprotein receptors on epithelial cell surfaces.

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Lectin affinity high-performance liquid chromatography: Interactions of N-glycanase-released oligosaccharides with leukoagglutinating phytohemagglutinin, concanavalin A, Datura stramonium agglutinin, and Vicia villosa agglutinin

Cited by 67 publications

References 35 publications

Sugar-Specific Inhibitory Effects of Wheat Germ Agglutinin and Phytohemagglutinin-E4 on Histamine Release Induced by Basic Secretagogues from Rat Peritoneal Mast Cells and Their Possible Action Sites

Sugar-Specific Inhibitory Effects of Wheat Germ Agglutinin and Phytohemagglutinin-E4 on Histamine Release Induced by Basic Secretagogues from Rat Peritoneal Mast Cells and Their Possible Action Sites

Histochemical Analysis of Glycoconjugates in the Disseminate Prostate Gland of the Wild Boar (Sus scrofa riukiuanus)

Oligosaccharide Side Chains on Human Secretory IgA Serve as Receptors for Ricin

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