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. 1981 Feb;78(2):1019–1022. doi: 10.1073/pnas.78.2.1019

L-Fucose-terminated glycoconjugates are recognized by pinocytosis receptors on macrophages.

V L Shepherd, Y C Lee, P H Schlesinger, P D Stahl
PMCID: PMC319937  PMID: 6940120

Abstract

125I-Labeled L-fucose-albumin complex and rat preputial beta-glucuronidase are rapidly cleared from plasma after intravenous infusion. L-Fucose-albumin retards the plasma clearance of beta-glucuronidase whereas D-fucose-albumin is inactive. In vitro, 125I-labeled L-fucose-albumin is taken up into rat or rabbit alveolar macrophages by receptor-mediated pinocytosis. Uptake (37 degrees C) is time-dependent, is saturable with increasing ligand concentration (Kuptake = 4.4 X 10(-8) M), and requires Ca2+. 125I-labeled D-fucose-albumin is poorly taken up. Binding (4 degrees C) is saturable and Ca2+ dependent. Binding and uptake are fully inhibited by yeast mannan. A series of neoglycoproteins, including L-fucose-albumin, were tested as inhibitors of uptake of 125I-labeled beta-glucuronidase into macrophages. The following order of potency was observed: L-Fuc = D-Man greater than GlcNAc approximately D-Glc greater than D-Xyl much greater than than D-Gal = L-Ara = D-Fuc. L-Fucose-terminated oligosaccharides coupled to bovine serum albumin also block 125I-labeled beta-glucuronidase uptake into macrophages.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Achord D. T., Brot F. E., Bell C. E., Sly W. S. Human beta-glucuronidase: in vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells. Cell. 1978 Sep;15(1):269–278. doi: 10.1016/0092-8674(78)90102-2. [DOI] [PubMed] [Google Scholar]
  2. Achord D. T., Brot F. E., Sly W. S. Inhibition of the rat clearance system for agalacto-orosomucoid by yeast mannans and by mannose. Biochem Biophys Res Commun. 1977 Jul 11;77(1):409–415. doi: 10.1016/s0006-291x(77)80213-1. [DOI] [PubMed] [Google Scholar]
  3. Baynes J. W., Wold F. Effect of glycosylation on the in vivo circulating half-life of ribonuclease. J Biol Chem. 1976 Oct 10;251(19):6016–6024. [PubMed] [Google Scholar]
  4. Brown T. L., Henderson L. A., Thorpe S. R., Baynes J. W. The effect of alpha-mannose-terminal oligosaccharides on the survival of glycoproteins in the circulation. Rapid uptake and catabolism of bovine pancreatic ribonuclease B by nonparenchymal cells of rat liver. Arch Biochem Biophys. 1978 Jun;188(2):418–428. doi: 10.1016/s0003-9861(78)80026-5. [DOI] [PubMed] [Google Scholar]
  5. Day J. F., Thornburg R. W., Thorpe S. R., Baynes J. W. Carbohydrate-mediated clearance of antibody . antigen complexes from the circulation. The role of high mannose oligosaccharides in the hepatic uptake of IgM . antigen complexes. J Biol Chem. 1980 Mar 25;255(6):2360–2365. [PubMed] [Google Scholar]
  6. GREENWOOD F. C., HUNTER W. M., GLOVER J. S. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY. Biochem J. 1963 Oct;89:114–123. doi: 10.1042/bj0890114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Grant D. A., Magee A. I., Meeks D., Regan C., Bainbridge D. R., Hermon-Taylor J. Identification of a defence mechanism in vivo against the leakage of enterokinase into the blood. Biochem J. 1979 Dec 15;184(3):619–626. doi: 10.1042/bj1840619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Himeno M., Ohara H., Arakawa Y. Beta-glucuronidase of rat preputial gland. Crystallization, properties, carbohydrate composition, and subunits. J Biochem. 1975 Feb;77(2):427–438. doi: 10.1093/oxfordjournals.jbchem.a130742. [DOI] [PubMed] [Google Scholar]
  9. Hubbard A. L., Wilson G., Ashwell G., Stukenbrok H. An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver. I. Distribution of 125I-ligands among the liver cell types. J Cell Biol. 1979 Oct;83(1):47–64. doi: 10.1083/jcb.83.1.47. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kaplan J., Nielsen M. Pinocytic activity of rabbit alveolar macrophages in vitro. J Reticuloendothel Soc. 1978 Dec;24(6):673–685. [PubMed] [Google Scholar]
  11. Kawasaki T., Etoh R., Yamashina I. Isolation and characterization of a mannan-binding protein from rabbit liver. Biochem Biophys Res Commun. 1978 Apr 14;81(3):1018–1024. doi: 10.1016/0006-291x(78)91452-3. [DOI] [PubMed] [Google Scholar]
  12. Kornfeld R., Kornfeld S. Comparative aspects of glycoprotein structure. Annu Rev Biochem. 1976;45:217–237. doi: 10.1146/annurev.bi.45.070176.001245. [DOI] [PubMed] [Google Scholar]
  13. Krantz M. J., Holtzman N. A., Stowell C. P., Lee Y. C. Attachment of thioglycosides to proteins: enhancement of liver membrane binding. Biochemistry. 1976 Sep 7;15(18):3963–3968. doi: 10.1021/bi00663a009. [DOI] [PubMed] [Google Scholar]
  14. Leake E. S., Myrvik Q. N. Changes in morphology and in lysozyme content of free alveolar cells after the intravenous injection of killed BCG in oil. J Reticuloendothel Soc. 1968 Feb;5(1):33–53. [PubMed] [Google Scholar]
  15. Lee Y. C., Stowell C. P., Krantz M. J. 2-Imino-2-methoxyethyl 1-thioglycosides: new reagents for attaching sugars to proteins. Biochemistry. 1976 Sep 7;15(18):3956–3963. doi: 10.1021/bi00663a008. [DOI] [PubMed] [Google Scholar]
  16. Prieels J. P., Pizzo S. V., Glasgow L. R., Paulson J. C., Hill R. L. Hepatic receptor that specifically binds oligosaccharides containing fucosyl alpha1 leads to 3 N-acetylglucosamine linkages. Proc Natl Acad Sci U S A. 1978 May;75(5):2215–2219. doi: 10.1073/pnas.75.5.2215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Remold H. G. Requirement for alpha-L-fucose on the macrophage membrane receptor for MIF. J Exp Med. 1973 Nov 1;138(5):1065–1076. doi: 10.1084/jem.138.5.1065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Schlesinger P. H., Doebber T. W., Mandell B. F., White R., DeSchryver C., Rodman J. S., Miller M. J., Stahl P. Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver non-parenchymal cells. Studies with beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, ribonuclease B and agalacto-orosomucoid. Biochem J. 1978 Oct 15;176(1):103–109. doi: 10.1042/bj1760103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schlesinger P. H., Rodman J. S., Doebber T. W., Stahl P. D., Lee Y. C., Stowell C. P., Kuhlenschmidt T. B. The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine. Biochem J. 1980 Nov 15;192(2):597–606. doi: 10.1042/bj1920597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Stahl P. D., Rodman J. S., Miller M. J., Schlesinger P. H. Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1399–1403. doi: 10.1073/pnas.75.3.1399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Stahl P. D., Touster O. Beta-glucuronidase of rat liver lysosomes. Purification, properties, subunits. J Biol Chem. 1971 Sep 10;246(17):5398–5406. [PubMed] [Google Scholar]
  22. Stahl P., Rodman J. S., Schlesinger P. Clearance of lysosomal hydrolases following intravenous infusion. Kinetic and competition experiments with beta-glucuronidase and N-acetyl-beta-D-glucosaminidase. Arch Biochem Biophys. 1976 Dec;177(2):594–605. doi: 10.1016/0003-9861(76)90471-9. [DOI] [PubMed] [Google Scholar]
  23. Stahl P., Schlesinger P. H., Sigardson E., Rodman J. S., Lee Y. C. Receptor-mediated pinocytosis of mannose glycoconjugates by macrophages: characterization and evidence for receptor recycling. Cell. 1980 Jan;19(1):207–215. doi: 10.1016/0092-8674(80)90402-x. [DOI] [PubMed] [Google Scholar]
  24. Stahl P., Six H., Rodman J. S., Schlesinger P., Tulsiani D. R., Touster O. Evidence for specific recognition sites mediating clearance of lysosomal enzymes in vivo. Proc Natl Acad Sci U S A. 1976 Nov;73(11):4045–4049. doi: 10.1073/pnas.73.11.4045. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Steer C. J., Clarenburg R. Unique distribution of glycoprotein receptors on parenchymal and sinusoidal cells of rat liver. J Biol Chem. 1979 Jun 10;254(11):4457–4461. [PubMed] [Google Scholar]
  26. Stockert R. J., Morell A. G., Scheinberg I. H. The existence of a second route for the transfer of certain glycoproteins from the circulation into the liver. Biochem Biophys Res Commun. 1976 Feb 9;68(3):988–993. doi: 10.1016/0006-291x(76)91243-2. [DOI] [PubMed] [Google Scholar]
  27. Stowell C. P., Lee R. T., Lee Y. C. Studies on the specificity of rabbit hepatic carbohydrate-binding protein using neoglycoproteins. Biochemistry. 1980 Oct 14;19(21):4904–4908. doi: 10.1021/bi00562a031. [DOI] [PubMed] [Google Scholar]
  28. Stowell C. P., Lee Y. C. Preparation of some new neoglycoproteins by amidination of bovine serum albumin using 2-imino-2-methoxyethyl 1-thioglycosides. Biochemistry. 1980 Oct 14;19(21):4899–4904. doi: 10.1021/bi00562a030. [DOI] [PubMed] [Google Scholar]
  29. Stowell C. P., Lee Y. C. The binding of d-glucosyl-neoglycoproteins to the hepatic asialoglycoprotein receptor. J Biol Chem. 1978 Sep 10;253(17):6107–6110. [PubMed] [Google Scholar]
  30. Townsend R., Stahl P. Isolation and characterization of a mannose/N-acetylglucosamine/fucose-binding protein from rat liver. Biochem J. 1981 Jan 15;194(1):209–214. doi: 10.1042/bj1940209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Watkins W. M. Blood-group substances. Science. 1966 Apr 8;152(3719):172–181. doi: 10.1126/science.152.3719.172. [DOI] [PubMed] [Google Scholar]
  32. Winkelhake J. L., Nicolson G. L. Aglycosylantibody. Effects of exoglycosidase treatments on autochthonous antibody survival time in the circulation. J Biol Chem. 1976 Feb 25;251(4):1074–1080. [PubMed] [Google Scholar]
  33. Zopf D. A., Tsai C. M., Ginsburg V. Antibodies against oligosaccharides coupled to proteins: characterization of carbohydrate specificity by radioimmune assay. Arch Biochem Biophys. 1978 Jan 15;185(1):61–71. doi: 10.1016/0003-9861(78)90144-3. [DOI] [PubMed] [Google Scholar]

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