Skip to main content

Interaction of Lactoferrin with Mononuclear and Colon Carcinoma Cells

  • Chapter
Book cover Lactoferrin

Part of the book series: Advances in, Experimental Medicine and Biology ((AEMB,volume 357))

Summary

Lactoferrin is known to bind to macrophages/monocytes and intestinal mucosal cells, but the nature and function of these interactions is not clear. We have therefore examined the interaction of lactoferrin in vitro with the promonocytic cell line U937 and with differentiated human colon carcinoma cells. U937 cells bound more lactoferrin than transferrin, although most of the lactoferrin binding was non-specific. Uptake of iron from transferrin was rapid, but uptake from lactoferrin was slow, and may have been due to prior transfer of iron to transferrin in the culture medium as a result of labilisation of iron from membrane-bound lactoferrin. Unlike transferrin, lactoferrin was not internalised by U937 cells. Lactoferrin significantly reduced uptake of non-transferrin-bound iron by the cells, but had no effect on uptake of transferrin-bound iron. Transport of lactoferrin-bound iron across monolayer cultures of differentiated Caco-2 cells in bicameral chambers was similar to that of ferric citrate, while transport of transferrin-bound iron was lower. Lactoferrin and transferrin themselves were not transported, although some proteolytically degraded material did cross the monolayer. Thus lactoferrin, unlike transferrin, is not an important iron donor to monocytic cells, but may instead serve to regulate iron uptake from other sources. It does not seem to enhance iron transport across mucosal cells.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Alvarez-Hernandez X, Nichols GM, Glass J. (1991) Caco-2 cell line: s system for studying intestinal iron transport across epithelial cell monolayers. Biochim Biophys Acta 1070:205–208.

    Article  PubMed  CAS  Google Scholar 

  • Amouric M., Marvaldi J, Pichon J, Bellot F, Figarella C. (1984) Effect of lactoferrin on the growth of a human adenocarcinoma cell line-comparison with transferrin. In Vitro 20:543–548.

    Article  PubMed  CAS  Google Scholar 

  • Andreesen R, Osterholz J, Bodemann H, Bross KJ, Costabel U, Lohr GW. (1984) Expression of transferrin receptors and intracellular ferritin during terminal differentiation of human monocytes. Blut 49:195–202.

    Article  PubMed  CAS  Google Scholar 

  • Azuma N, Mori H, Kaminogawa S, Yamauchi K. (1989) Stimulatory effect of lactoferrin on DNA synthesis in BALB/c 3T3 cells. Agric Biol. Chem 53:31–35.

    Article  CAS  Google Scholar 

  • Birgens HS. (1991) The interaction of lactoferrin with human monocytes. Dan Med Bull 38:244–252.

    PubMed  CAS  Google Scholar 

  • Brock JH. (1980) Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch Dis Child 55:417–421.

    Article  PubMed  CAS  Google Scholar 

  • Dautry-Varsat A. (1986) Receptor-mediated endocytosis: the intracellular journey of transferrin and its receptor. Biochimie 68:375–381.

    Article  PubMed  CAS  Google Scholar 

  • Davidson LA, Litov RE, Lonnerdal, B. (1990) Iron retention from lactoferrin-supplemented formulas in infant rhesus monkeys. Pediat Res 27:170–180.

    Article  Google Scholar 

  • Davidson LA, Lonnerdal, B. (1988) Specific binding of lactoferrin to brush border membrane: ontogeny and effect of glycan chain. Am J Physiol 254:G580–G585.

    PubMed  CAS  Google Scholar 

  • Djeha A, Brock JH. (1992) Effect of transferrin, lactoferrin and chelated iron on human T-lymphocytes. Br J Haematol 80:235–241.

    Article  PubMed  Google Scholar 

  • Fransson GB, Keen, CL, Lonnerdal B. (1983a) Supplementation of milk with iron bound to lactoferrin using weanling mice. I. Effects on hematology and tissue iron. J Pediat Gastroenterol Nutr 2:693–700.

    Article  CAS  Google Scholar 

  • Fransson GB, Thoren-Tolling K, Jones B, Hambraeus L, Lonnerdal B. (1983b) Absorption of lactoferrin iron in suckling pigs. Nutr Res 3:373–384.

    Article  CAS  Google Scholar 

  • Goavec M., Mazurier J, Montreuil J, Spik G. (1985) Role des glycannes dans 1a fixation de la serotransferrine et de 1a lactotransferrine humaines sur les macrophages alvéolaires humains. C R Seances Acad Sci (III) 301:689–694.

    CAS  Google Scholar 

  • Halleux C, Schneider Y-J. (1991) Iron absorption by intestinal epithelial cells: 1. CaCo2 cells cultivated in serum-free medium, on polyethyleneterephthalate microporous membranes, as an in vitro model. In Vitro Cell Dev Biol. 27A:293–302.

    Article  PubMed  CAS  Google Scholar 

  • Hamilton TA, Weiel JA, Adams DO (1984) Expression of the transferrin receptor in murine peritoneal macrophages is modulated in different stages of activation. J Immunol 132:2285–2290.

    PubMed  CAS  Google Scholar 

  • Hidalgo IJ, Raub TJ, Borchardt RT (1989) Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 96:736–749.

    PubMed  CAS  Google Scholar 

  • Hu WL, Mazurier J, Montreuil J, Spik G. (1990) Isolation and partial characterisation of a lactotransferrin receptor from mouse intestinal brush border. Biochemistry 29:535–541.

    Article  PubMed  CAS  Google Scholar 

  • Iturralde M, Vass JK, Oria R, Brock JH. (1992) Effect of iron and retinoic acid on the control of transferrin receptor and ferritin in the human promonocytic cell line U937. Biochim Biophys Acta 1133:241–246.

    Article  PubMed  CAS  Google Scholar 

  • Johansson BG (1969) Isolation of crystalline lactoferrin from human milk. Acta Chem Scand 23:683–684.

    Article  PubMed  CAS  Google Scholar 

  • Mazurier J, Legrand D, Hu WL, Montreuil J, Spik G. (1989) Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by antiligand-affinity chromatography. Eur J Biochem 179:481–487.

    CAS  Google Scholar 

  • Mazurier J, Spik G. (1980) Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin. Biochim Biophys Acta 629:399–408.

    Article  CAS  Google Scholar 

  • McAbee DD, Esbensen K. (1991) Binding and endocytosis of apo-and holo-lactoferrin by isolated rat hepatocytes. J Biol. Chem 266:23624–23631.

    PubMed  CAS  Google Scholar 

  • Oria R, Alvarez-Hernandez X, Liceaga J, Brock JH (1988) Uptake and handling of iron from transferrin, lactoferrin and immune complexes by a macrophage cell line. Biochem J 252:221–225.

    PubMed  CAS  Google Scholar 

  • Oria R, Ismail M., Sanchez L, Calvo M., Brock JH. (1993) The effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes. J Dairy Res 60:363–369.

    Article  PubMed  CAS  Google Scholar 

  • Pippard MJ. (1989) Clinical use of iron chelation. In Iron in immunity, cancer and inflammation (ed. De Sousa M and Brock JH), John Wiley, Chichester, UK, pp361–392.

    Google Scholar 

  • Reid PA, Watts C. (1990) Cycling of cell-surface MHC glycoproteins through primaquine-sensitive intracellular compartments. Nature 346:655–657.

    Article  PubMed  CAS  Google Scholar 

  • Van Snick JL, Masson PL, Heremans, J. (1974) The involvement of lactoferrin in the hyposideremia of acute inflammation. J Exp Med 140:1068–1084.

    Article  PubMed  Google Scholar 

  • Ziere GJ, Van Dijk MCM, Bijsterbosch MK, Van Berkel TJC. (1992) Lactoferrin uptake by the rat liver. Characterization of the recognition site and effect of selective modification of the arginine residues. J Biol. Chem, 267:11229–11235.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Springer Science+Business Media New York

About this chapter

Cite this chapter

Brock, J.H., Ismail, M., Sánchez, L. (1994). Interaction of Lactoferrin with Mononuclear and Colon Carcinoma Cells. In: Hutchens, T.W., Rumball, S.V., Lönnerdal, B. (eds) Lactoferrin. Advances in, Experimental Medicine and Biology, vol 357. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2548-6_15

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-2548-6_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6087-2

  • Online ISBN: 978-1-4615-2548-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics