Mannose-Binding Proteins of Animal Origin

  • Y. C. Lee
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 228)


More than ninety years ago, Stillmark (1888) discovered that castor-bean extracts caused agglutination of human red cells. Boyd and Shapeleigh (1954) invented the term “lectin” (from legere, to select) for this group of plant proteins which are capable of hemagglutination. It soon became apparent that lectins are carbohydrate-binding proteins. Modern nomenclature defines lectins as carbohydrate-binding proteins which are not immunoglobulins or enzymes.


Alveolar Macrophage Lysosomal Enzyme Chicken Liver Lung Macrophage Chicken Serum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Achord, D., Brot, F., and Sly, W. (1977). “Inhibition of the ratclearance system for agalacto-orosomucoid by yeast mannan and by mannose.” Biochem. Biophys. Res, Commun. 77:409–415.CrossRefGoogle Scholar
  2. Ashwell, G. and Harford, J. (1982). “Carbohydrate-specific receptors of the liver.” Ann. Rev. Biochem. 51:531–554.PubMedCrossRefGoogle Scholar
  3. Ashwell, G. and Morell, A. (1974). “The role of surface carbohydrates in the hapatic recognition and transport of circulating glycoproteins.” Adv. Enzymol. Relat. Areas Mol. Biol. 41:99–128.PubMedGoogle Scholar
  4. Barondes, S.H. (1984). “Soluble lectins: a new class of extracellular proteins.” Science 223:1259–1264.PubMedCrossRefGoogle Scholar
  5. Baynes, J., and Mold, F. (1976). “Effect of glycosylation on the in vivo circulating half-life of ribonuclease.” J. Biol. Chem. 261: 6016–6124.Google Scholar
  6. Bodmer, J. L. and Dean, R. T. (1983). “Does the induction of macrophage lysosomal enzyme secretion by zymosan involve the mannose receptor?” Biochem. Biophys. Res. Commun. 113, 192–198.PubMedCrossRefGoogle Scholar
  7. Boyd, W. Co and Shapeleigh, E. (1954). “Specific precipitating activity of plant agglutinins (Lectins).” Science 119:419.PubMedCrossRefGoogle Scholar
  8. Brownell, M. D., Colley, K. J., and Baenziger, J. U. (1984). “Synthesis, processing, and secretion of the core-specific lectin by rat hepatocytes and hepatpoma cells.” J. Biol. Chem. 259:3925–3932.PubMedGoogle Scholar
  9. Colley, K. J. and Baenziger, J. U. (1985). “Relationship of post-translational modification to complex assembly and secretion of the rat core-specific lectin.” Proc. VIIIth Interntl. Symp. on Glycoconjugates (Houston, TX), Praeger, NY, p„ 353.Google Scholar
  10. Doebber, T. W., Wu, M. S., Bugianess, R. L., Ponpipom, M. M„, Furbish, F. S., Barranger, J9J Brady, R.O., and Shen, T. Y. (1982). “Enhanced macrophage uptake of synthetically glycosylated human placenatal p-glucoscerebrosidase.” J. Biol. Chem. 257:2193–2199.PubMedGoogle Scholar
  11. Hoppe, C. A. and Lee, Y. C. (1982). “Stimulation of mannose-binding activity in the rabbit alveolar macrophage by simple sugars.” J. Biol. Chem. 257:12831–12834.PubMedGoogle Scholar
  12. Hoppe, C. A. and Lee, Y. C. (1983). “The binding and processing of mannose-binding serum albumin derivatives by rabbit alveolar macrophages.” J. Biol. Chem. 258;14193–14199.PubMedGoogle Scholar
  13. Kawasaki, T. (1979). “Mannan-bind ing protein — a receptor for lysosomal enzymes.” Seikagaku, 51;447–451.PubMedGoogle Scholar
  14. Kawasaki, T., Etoh, R., and Yamashina, I. (1978). “Isolation and char ac ter i z at ion of a mannan-binding protein from rabbit liver.” Biochem. Biophys. Res. Commun. 81:1018–1024.PubMedCrossRefGoogle Scholar
  15. Kawasaki, N., Kawasaki, T., and Yamashina, I. (1983). “Isolation and characterication of mannan-binding protein from human serum.” J. Biochem. (Tokyo) 94:937–947.Google Scholar
  16. Kawasaki, T., Mizuno, Y., Masuda, T., and Yamashina, I. (1980). “Mannan-binding protein in lymphoid tissues of rats.” J. Biochem. (Tokyo) 88:1891–1894.Google Scholar
  17. Kawasaki, T., Mori, K., Oka, S., Ikeda, K., and Yamashina, I (1985) Proc. VIIIth Internatl. Symposium on Glycoconjugates, (Houston, TX), Praeger, N.Y., p.146.Google Scholar
  18. Kozutsumi, Y., Kawasaki, T., and Yamashina, I. (1980). “Isolation and characterization of a mannan-binding protein from rabbit serum.” Biochem. Biophys. Res. Commun. 95:658–664.PubMedCrossRefGoogle Scholar
  19. Kuhlenschmidt, T. and Lee, Y. C. (1982). “Isolation of a mannose- binding protein from chicken serum.” Fed. Proc. 41:1033.Google Scholar
  20. Kuhlenschmidt, T. and Lee, Y. C. (1984). “Specificity of chicken liver carbohydrate binding protein.” Biochemistry 23:3569–3575.PubMedCrossRefGoogle Scholar
  21. Kuhlenschmidt, T., Kuhlenschmidt, M., Roseman, S., and Lee, Y. C. (1984) Biochemistry 23:437–6444.Google Scholar
  22. Largent, B. L., Walton, K. M., Hoppe, C. A., Lee, Y. C., and Schnaar, R. L. (1984). “Carbohydrate-specific adhesion of alveolar macrophages to mannose-derivatized surfaces.” J. Biol. Chem. 259:1764–1769.PubMedGoogle Scholar
  23. Lee, R.T. and Lee, Y.C. (1982). “Neoglycoprote ins as probes for binding and cellular uptake of glycoconjugates.” in “The Glycoconjugates”, Vol. 4 (Ed. M. Horowitz), Acad. Press, N.Y., p.57–83.Google Scholar
  24. Loeken, M. R. and Roth, T. F. (1983). “Analysis of maternal I subpopulations which are transported into the chicken oocyte.” Immunology 49:21–28.PubMedGoogle Scholar
  25. Maynard, Y. and Baenziger, J. U. (1981). “Oligosaccharide-specific endocytosis by isolated rate hepatic reticuloendothelial cells.” J. Biol. Chem. 256:8063–8068.PubMedGoogle Scholar
  26. Mizuno, Y., Kozutsumi, Y., Kawasaki, T., Yamashina, I. (1981). Isolation and characterization of a mannan-binding protein from rat liver.” J. Biol. Chem. 256:4247–4252.PubMedGoogle Scholar
  27. Mori, K., Kawasaki, T., Yamashina, I. (1983). “Identification of the mannan-binding protein from rat livers as a hepatocyte protein distinct from the mannan receptor on sinusoidal cells.” Arch. Biochem. Biophys. 222:542–552.PubMedCrossRefGoogle Scholar
  28. Oka, S., Kawasaki, T., and Yamashina, I. (1985). “Isolation and characterization of mannan-binding proteins from chicken liver.” Arch. Biochem. Biophys. 241;95–105.PubMedCrossRefGoogle Scholar
  29. Pless, D.D., Lee, Y.C., Roseman, S., and Schnaar, R.L. (1983). “Specific cell adhesion to immobilized glycoproteins demonstrated using new reagents for protein and glycoprotein immobilization.” J. Chem. 258:2340–2349.Google Scholar
  30. Ponpipom, M. M., Bugianesi, R. L., Robbins, J. C., Doebber, T. W., and Shen, T.Y. (1981). “Cell-specific ligands for selective drug delivery to tissues and organs.” J. Med. Chem. 24:1388–1395.PubMedCrossRefGoogle Scholar
  31. Riches, D. W., Watkins, J. L., and Stanworth, D. R. (1983). “Biochemical differences in the mechanism of macrophage lysosomal exocytosis initiated by zymosan particles and weak bases.” Biochem. J. 212: 869–874.PubMedGoogle Scholar
  32. Roche, A. C., Midoux, P., Mayer, R., and Monsigny, M. (1985). “Activation of murine macrophages and human monocytes by membrane lectin-mediated endocytosis of activators-bound to neoglyco- proteins.” Proc. VIIIth International Symposium on Glycoconjugates, Houston, TX, Praeger, N.Y., p.569.Google Scholar
  33. Schlesinger, P. H., Rodman, J. S., Doebber, T. W., Stahl, P., Lee, Y. C., Stowell, C. P., and Kuhlenshmidt, T. (1980). “The role of extra-hepatic tissues in the receptor-mediated plasma of glycoproteins terminated by mannose or N-acetylglucosamine.” Proc. Natl. Acad. Sci. U.S.A. 192:597–606.Google Scholar
  34. Shepherd, V. L., Lee, Y. C., Schlesinger, P. H., and Stahl, P. D. (1981). “L-Fucose-terminated glycoconjugates are recognized by pinocytosis receptors on macrophages.” Proc. Natl. Acad. Sci. (USA) 78:1019–1022.CrossRefGoogle Scholar
  35. Sly, W.S. and Fischer, H.D. (1982). “The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes.” J. Cell. Biochem. 18:67–85.PubMedCrossRefGoogle Scholar
  36. Stahl, P., Six, H., Rodman, J. S., Schlesinger, P., Tulsiani, D. R. P., and Touster, O. (1976). “Evidence for specific recognition sites mediating clearance of lysosomal enzymes in vivo.” Proc. Natl. Acad. Sci. U.S.A. 73:4045.PubMedCrossRefGoogle Scholar
  37. Stahl, P., Rodman, J. S., Miller, M. J., and Schlesinger, P. H. (1978). “Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages.” Proc. Natl. Acad. Sci U.S.A. 73:1399–1403.CrossRefGoogle Scholar
  38. Stillmark, H. (1888) Inaug. Diss., Dorpat., as cited in Goldstein and Hayes (1978).Google Scholar
  39. Sung, S.J., Nelson, R.S., and Silverstein, S.C. (1983). “Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages.” J. Cell. Biol. 96:160–166.PubMedCrossRefGoogle Scholar
  40. Tietze, C., Schlesinger, P. H., and Stahl, P. (1980). Chloroquine and ammonium ion inhibit receptor-mediated endocytosis of mannose- glycoconjugates by macrophages: apparent inhibition of receptor recycling.” Biochem. Biophys. Res. Commun. 93:1–8.CrossRefGoogle Scholar
  41. Tietze, C., Schlesinger, P. H., and Stahl, P. (1982). “Mannose-specific endocytosis receptor of alveolar macrophages: Demonstration of two functionally distinct intracellular pools of receptor and their roles in receptor recycling.” J. Cell Biol. 92:417–424.PubMedCrossRefGoogle Scholar
  42. Tolleshaug, H., Berg, T., and Blomhoff, R. (1984). “Uptake of mannose- termmateci giycoprdteins in isolated rat river cells. Evidence for receptor-mediated endocytosis in hepatocytes.” Biochem. J. 223: 151–160.PubMedGoogle Scholar
  43. Townsend, R. and Stahl, P. (1981). Isolation and characterization of a mannose/N-acetylglucosamine/fucose-binding protein from rat liver.” Biochem. J. 194:209–214.PubMedGoogle Scholar
  44. Wang, K. Y., Kuhlenschmidt, T. B., and Lee, Y. C. (1985). “Isolation and characterization of the major mannose-binding protein in chicken serum.”Google Scholar
  45. Warr, G. (1980). “A macrophage receptor for (mannose/glucosamine)- glycoproteins of potential importance in phagoytic activity.” Biochem. Biophys. Res. Commun. 93:737–745.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Y. C. Lee
    • 1
  1. 1.Biology DepartmentThe Johns Hopkins UniversityBaltimoreUSA

Personalised recommendations