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Light microscopic detection of sugar residues in glycoconjugates of salivary glands and the pancreas with lectin-horseradish peroxidase conjugates. I. Mouse

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Summary

Mouse salivary glands and pancreases were stained with a battery of ten horseradish peroxidase-conjugated lectins. Lectin staining revealed striking differences in the structure of oligosaccharides of stored intracellular secretory glycoproteins and glycoconjugates associated with the surface of epithelial cells lining excretory ducts. The percentage of acinar cells containing terminal α-N-acetylgalactosamine residues varied greatly in submandibular glands of 30 male mice, but all submandibular acinar cells contained oligosaccharides with terminal sialic acid and penultimate β-galactose residues. The last named dimer was abundant in secretory glycoprotein of all mucous acinar cells in murine sublingual glands and an additional 20–50% of these cells in all glands contained terminalN-acetylglucosamine residues. In contrast, terminal α-N-acetylgalactosamine was abundant in sublingual serous demilune secretions. Serous acinar cells in the exorbital lacrimal gland, posterior lingual gland, parotid gland and pancreas exhibited a staining pattern unique to each organ. In contrast, the apical cytoplasm and surface of striated duct epithelial cells in the submandibular, sublingual, parotid and exorbital lacrimal gland stained similarly. A comparison of staining with conjugated lectins reported biochemically to have very similar carbohydrate binding specificity has revealed some remarkable differences in their reactivity, suggesting different binding specificity for the same terminal sugars having different glycosidic linkages or with different penultimate sugar residues.

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References

  • Allen, H. J., Johnson, E. A. Z. &Matta, K. L. (1977) A comparison of the binding specificities of lectins fromUlex europaeus andLotus tetragonolobus.Immunol. Comm. 6, 585–602.

    Google Scholar 

  • Avrameas, S. (1969) Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugate for the detection of antigens and antibodies.Immunochemistry 6, 43–52.

    Google Scholar 

  • Baenziger, J. U. &Fiete, D. (1979) Structural determinants ofRicinus communis agglutinin and toxin specificity for oligosaccharides.J. biol. Chem. 254, 9795–9.

    Google Scholar 

  • Cuatrecasas, P. (1973) Gangliosides and membrane receptors for cholera toxin.Biochemistry 12, 3558–66.

    Google Scholar 

  • Debray, H., Decout, D., Strecker, G., Spik, G. &Montreuil, J. (1981) Specificity of twelve lectins towards oligosaccharides and glycopeptides related toN-glycosylproteins.Eur. J. Biochem. 117, 41–55.

    Google Scholar 

  • Denny, P. A., Denny, P. C. &Jenkins, K. (1980) Purification and biochemical characterization of a mouse submandibular sialomucin.Carbohydr. Res. 87, 265–74.

    Google Scholar 

  • Denny, P. A. &Denny, P. C. (1982) Localization of a mouse submandibular sialomucin by indirect immunofluorescence.Histochem. J. 14, 403–8.

    Google Scholar 

  • Ebisu, S., Shankar Iyer, P. N. &Goldstein, I. J. (1978) Equilibrium dialysis and carbohydrate-binding studies on the 2-acetamido-2-deoxy-d-glucopyranosyl-binding lectin fromBanderiaea simplicifolia seeds.Carbohydr. Res. 61, 129–38.

    Google Scholar 

  • Etzler, M. E. &Kabat E. A. (1970) Purification and characterization of a lectin (plant hemagglutinin) with blood group A specificity fromDolichos biflorus.Biochemistry 9, 869–77.

    Google Scholar 

  • Goldstein, I. J. &Hayes, C. E. (1978) The lectins: Carbohydrate-binding proteins of plants and animals.Adv. Carbohydr. Chem. Biochem. 35, 127–340.

    Google Scholar 

  • Hayes, C. E. &Goldstein, I. J. (1974) An α-d-galactosyl-binding lectin fromBandeiraea simplicifolia seeds.J. biol. Chem. 249, 1904–14.

    Google Scholar 

  • Junqueira, L. C., Sessot, A. &Nahas, L. (1951) Sur la nature des cellules secretaires de la gland parotide.Bull. Microsc. appl. 1, 133–5.

    Google Scholar 

  • Lima, T. G. &Haddad, A. (1981) Light and electron-microscopic radioautographic study of glycoprotein secretion in the granular duct of the submandibular gland of the male mouse.Cell Tissue Res. 220, 405–25.

    Google Scholar 

  • Lotan, R., Skutelsky, E., Danon, D. &Sharon, N. (1975) The purification, composition, and specificity of the anti-t lectin from peanut (Arachis hypogaea).J. biol. Chem. 250, 8518–23.

    Google Scholar 

  • Montreuil, J. (1980) Primary structure of glycoprotein glycans: Basis for the molecular biology of glycoproteins.Adv. Carbohydr. Chem. Biochem. 37, 157–223.

    Google Scholar 

  • Mowry, R. W. &Winkler, C. H. (1956) The coloration of acidic carbohydrates of bacteria and fungi in tissue sections with special reference to capsules ofCryptococcus neoformans, Pneumococci andStaphylococci.Am. J. Path. 32, 628–9.

    Google Scholar 

  • Munhoz, C. O. G. (1971) Histochemical classification of acini and ducts of parotid glands from artiodactyles, carnivores and rodents.Acta histochem. 39, 302–17.

    Google Scholar 

  • Pereira, M. E. A. &Kabat, E. A. (1974) Specificity of purified hemagglutinin (lectin) fromLotus tetragonolobus.Biochemistry 13, 3184–92.

    Google Scholar 

  • Pereira, M. E. A., Kisailus, E. C., Gruezo, R. &Kabat, E. A. (1978) Immunochemical studies on the combining site of the blood group H-specific lectin 1 fromUlex europeus seeds.Arch. Biochem. Biophys. 185, 108–14.

    Google Scholar 

  • Pinkstaff, C. A. (1980) The cytology of salivary glands.Int. Rev. Cytol. 63, 141–261.

    Google Scholar 

  • Roukema, P. A., Oderkerk, C. H. &Salkinoja-Salonen, M. S. (1976) The murine sublingual and submandibular mucins: Their isolation and characterization.Biochim. biophys. Acta. 428, 432–40.

    Google Scholar 

  • Schulte, B. A. &Spicer, S. S. (1983a) Light microscopic histochemical detection of terminal galactose andN-acetylgalactosamine residues in rodent complex carbohydrates using a galactose oxidase Schiff sequence and peanut lectin-horseradish peroxidase conjugate.J. Histochem. Cytochem. 31, 19–24.

    Google Scholar 

  • Schulte, B. A. &Spicer, S. S. (1983b) Light microscopic histochemical detection of sugar residues in secretory glycoproteins of rodent and human tracheal glands with lectin-horseradish peroxidase conjugates and the galactose oxidase-Schiff sequence.J. Histochem. Cytochem. 31, 391–403.

    Google Scholar 

  • Shimizu, S. &Yamada, K. (1979) Localization of concanavalin A binding sites with a concanavalin A-alkaline phosphatase method.Okajimas Folia Anat. Jpn. 56, 193–204.

    Google Scholar 

  • Spicer, S. S. (1960) A correlative study of the histochemical properties of rodent acid mucopolysaccharides.J. Histochem. Cytochem. 8, 18–35.

    Google Scholar 

  • Spicer, S. S. (1961) The use of various cationic reagents in histochemical differentiation of mucopolysaccharides.Am. J. clin. Path. 36, 393–407.

    Google Scholar 

  • Spicer, S. S. (1965) Diamine methods for differentiating mucosubstances histochemically.J. Histochem. Cytochem. 13, 211–34.

    Google Scholar 

  • Spicer, S. S. &Duvenci, J. (1964) Histochemical characteristics of mucopolysaccharides in salivary and exorbital lacrimal glands.Anat. Rec. 149, 333–57.

    Google Scholar 

  • Spicer, S. S., Swarm, R. L. &Burtner, H. J. (1961) Comparison of basophilia with S35 label in normal and methylated mucopolysaccharides.Lab. Invest. 10, 256–64.

    Google Scholar 

  • Spicer, S. S. &Warren, L. (1960) The histochemistry of sialic acid containing mucoproteins.J. Histochem. Cytochem. 8, 135–7.

    Google Scholar 

  • Stoward, P. J., Spicer, S. S. &Miller, R. L. (1980) Histochemical reactivity of peanut lectin-horseradish peroxidase conjugate.J. Histochem. Cytochem. 28, 979–90.

    Google Scholar 

  • van Heyningen, S. (1974) Cholera toxin: interaction of subunits with ganglioside GM1.Science N.Y. 183, 656–7.

    Google Scholar 

  • Yamada, K. &Shimizu, S. (1979) The use of peroxidase-labelledLimulus polyphemus agglutinin for the histochemistry of sialic acid-containing glycoproteins in light microscopy.Histochem. J. 11, 457–71.

    Google Scholar 

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Schulte, B.A., Spicer, S.S. Light microscopic detection of sugar residues in glycoconjugates of salivary glands and the pancreas with lectin-horseradish peroxidase conjugates. I. Mouse. Histochem J 15, 1217–1238 (1983). https://doi.org/10.1007/BF01002741

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