Histochemistry

, Volume 69, Issue 3, pp 289–297 | Cite as

A histochemical study about the zonal distribution of the galactose-binding protein in rat liver

  • M. J. Hardonk
  • H. B. Scholtens
Article

Summary

  1. 1.

    Dog intestinal alkaline phosphatase (IAP), an asialoglycoprotein, appeared to be a good marker for the histochemical detection of the galactose specific binding protein in cryostat sections of rat liver.

     
  2. 2.

    Binding of IAP to the receptor is optimal at neutral or slightly alkaline pH values. The binding could be inhibited by galactose and galactose containing sugars, whereas glucose and mannose did not show any effect. In contrast to fetuin itself desialylated fetuin completely inhibited IAP binding. Pretreatment of sections with phospholipase C or with trypsin inhibited IAP binding; collagenase did not show any influence.

     
  3. 3.

    The presence of the galactose-binding protein showed a distinct zonal distribution. In the area around the central vein (zone 3) the highest IAP binding capacity was found.

     

Keywords

Glucose Sugar Alkaline Phosphatase Trypsin Galactose 

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References

  1. Ashwell G, Morell AG (1974) The role of surface carbohydrate in the hepatic recogniton and transport of circulating glycoproteins. Adv Enzymol 41:99–128Google Scholar
  2. Furbish FS, Steer CJ, Barranger JA, Jones EA, Brady RO (1978) The uptake of native and desialylated glucocerebrosidase by rat hepatocytes and Kupffer cells. Biochem Biophys Res Commun 81:1047–1053Google Scholar
  3. Gregoriadis G (1975) Catabolism of glycoproteins. In: Dingle JT, Dean RT (eds) Lysosomes in biology and pathology. Vol 4. Elsevier, Amsterdam, pp 265–294Google Scholar
  4. Hardonk MJ, Dijkhuis FWJ, Haarsma TJ, Koudstall J, Huijbers WAR (1977a) Application of enzymehistochemical methods to isolated subcellular fractions and to sucrose-ficoll density gradients. A contribution to the comparison of histochemical and biochemical data. Histochemistry 53:165–181Google Scholar
  5. Hardonk MJ, Haarsma TJ, Dijkhuis FWJ, Poel M, Koudstaal J (1977b) Influence of fixation and buffer treatment on the release of enzymes from the plasma membrane. Histochemistry 54:57–66Google Scholar
  6. Horisberger M, Van Lanthen M (1978) Simultaneous localization of an hepatic binding protein specific for galactose and of galactose-containing receptors on rat hepatocytes. J Histochem Cytochem 26:960–966Google Scholar
  7. Hubbard AL, Wilson G, Ashwell G, Stukenbrok H (1979) An electron microscope autoradiography study of the carbohydrate recogniton systems in rat liver. I. Distribution of 125I-Ligands among the liver cell types. J Cell Biol 83:47–64Google Scholar
  8. Hudgin RL, Pricer WE, Ashwell G, Stockert RJ, Morell AG (1974) The isolation and propeties of a rabbit liver binding protein specific for asialoglycoproteins. J Biol Chem 249:5536–5543Google Scholar
  9. Jaques LW, Brown EB, Barrett JM, Brey WS, Weltner W (1977) Sialic acid. A calcium-binding carbohydrate. J Biol Chem 252:4533–4538Google Scholar
  10. Jones EA, Vierling JM, Steer CJ, Reichen J (1979) Cell surface receptors in the liver. In: Popper H, Schaffner F (eds) Progress in liver diseases, Vol 6. Grune and Stratton, New York, pp 43–80Google Scholar
  11. Lunney J, Ashwell G (1974) The effect of phospholipase on the binding of asialoglycoproteins by rat liver plasma membranes. Biochim Biophys Acta 367:304–315Google Scholar
  12. Pricer WE, Ashwell G (1971) The binding of desialylated glycoproteins by plasma membranes of rat liver. J Biol Chem 246:4825–4833Google Scholar
  13. Saini PK, Done J (1972) The diversity of alkaline phosphatase from rat intestine. Isolation and purification of the enzyme(s). Biochim Biophys Acta 258:147–153Google Scholar
  14. Scholtens HB (1980) Hepatic uptake and binding of intestinal alkaline phosphatase by rat liver. A kinetic and morphological study. Thesis, GroningenGoogle Scholar
  15. Spiro RG (1964) Periodate oxidation of the glycoprotein fetuin. J Biol Chem 239:567–573Google Scholar
  16. Steer CJ, Clarenburg R (1979) Unique distribution of glycoprotein receptors on parenchymal and sinusoidal cells of rat liver. J Biol Chem 254:4457–4461Google Scholar
  17. Sternlieb I (1977) Recognition, binding and transport of glycoproteins by the hepatocyte plasma membrane. In: Popper H, Bianchi L, Reutter W (eds) Membrane alterations as basis of liver injury. MTP Press, St. Leonardgate, pp 88–95Google Scholar
  18. Stockert RJ, Morell AG, Scheinberg IH (1977) Hepatic binding protein: the protective role of its sialic acid residues. Science 197:667–668Google Scholar
  19. Tanabe T, Pricer WE, Ashwell G (1979) Subcellular membrane topology and turnover of a rat hepatic binding protein specific for asialoglycoproteins. J Biol Chem 254:1038–1043Google Scholar
  20. Tolleshaug H, Berg T (1977) Uptake and degradation of asialo-fetuin by islolated rat hepatocytes. Acta Biol Med Germ 36:1753–1762Google Scholar
  21. Tolleshaug H, Berg T, Frölich W, Norum KR (1979) Intracellular localization and degradation of asialofetuin in isolated rat hepatocytes. Biochim Biophys Acta 585:71–84Google Scholar
  22. Van Lenten L, Ashwell G (1972) The binding of desialylated glycoproteins by plasma membranes of rat liver. Development of a quantitative inhibition assay. J Biol Chem 247:4633–4640Google Scholar
  23. Weigel PH, Schnaar RL, Kuhlenschmidt MS, Schmell E, Lee RT, Lee YC, Roseman S (1979) Adhesion of hepatocytes to immobilized sugars. A threshold phenomenon. J Biol Chem 254:10830–10838Google Scholar

Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • M. J. Hardonk
    • 1
  • H. B. Scholtens
    • 1
  1. 1.Department of Pathology, Histochemical SectionUniversity of GroningenGroningenThe Netherlands

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