Skip to main content

Lactoferrin Structure-Function Relationships

An Overview

  • Chapter
Lactoferrin

Part of the book series: Experimental Biology and Medicine ((EBAM,volume 28))

Summary

Although lactoferrin was first isolated over 30 years ago, its function remains unclear. Structurally, it closely resembles the iron-transport protein transferrin, suggesting that lactoferrin may also have an iron-transport role, and lactoferrin-binding sites or receptors have been reported on a variety of cells and tissues. However, the high pI of lactoferrin (~8.5–9.0) allows it to interact with many macromolecules, which makes identification of genuine receptors difficult. The idea that lactoferrin in breast milk acts as a specific transporter of iron to the mucosal cells of the infant gut could explain the high bioavailability of breast milk iron, but good evidence for this is lacking, and there are indications that lactoferrin may actually inhibit iron absorption. Another possible function is as an antimicrobial agent, particularly in the infant gut, and also at inflammatory foci where lactoferrin is released by degran-ulating neutrophils. There is ample in vitro evidence that lactoferrin exerts a bacteriostatic effect through its ability to sequester iron, and more recently, a bactericidal activity that is independent of iron-binding and mediated through an N-terminal basic peptide has been reported. However, there are disappointingly few in vivo data in support of the antimicrobial hypothesis. Lactoferrin is also reported to have various effects on the immune system, such as regulation of antibody production, complement activation, and natural killer (NK) cell function, but it is not known how it carries out these activities. The biological role of lactoferrin thus remains an enigma.

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 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover 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

  • Aisen, P. and Leibman, A. (1972) Lactoferrin and transferrin: a comparative study. Biochim. Biophys. Acta 257,314–323.

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Anderson, B. R, Baker, H. M., Norris, G. E., Rice, D. W., and Baker, E. N. (1989) Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8Å resolution. J. Mol Biol. 209, 711–734.

    Article  CAS  Google Scholar 

  • Arnold, R. R., Cole, M. R, and McGhee, J. R. (1977) A bactericidal effect for human lactoferrin. Science 197, 263–265.

    Article  CAS  Google Scholar 

  • Arnold, R. R., Russell, J. E., Champion, W. J., and Gauthier, J. J. (1981) Bactericidal activity of human lactoferrin: influence of physical condition and metabolic state of the target microorganism. Infect. Immun. 328, 655–660.

    Google Scholar 

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

    Article  CAS  Google Scholar 

  • Balmer, S. E., Scott, P. H., and Wharton, B. A. (1989) Diet and fecal flora in the newborn: lactoferrin. Arch. Dis. Child 64, 1685–1690.

    Article  CAS  Google Scholar 

  • Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., and Tomita, M. (1992) Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta 1121, 130–136.

    Article  CAS  Google Scholar 

  • Bennett, R. M. and Davis, J. (1982) Lactoferrin interacts with deoxyribonucleic acid: a preferential reactivity with double-stranded DNA and dissociation of DNA-anti-DNA complexes. J. Lab. Clin. Med. 99, 127–138.

    CAS  Google Scholar 

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

    CAS  Google Scholar 

  • Birgens, H. S., Hansen, N. E., Karle, H., and Kristenesen, L. O. (1983) Receptor binding of lactoferrin by human monocytes. Br. J. Haematol. 54, 383–391.

    Article  CAS  Google Scholar 

  • Birgens, H. S., Kristenesen, L. O., Borregaard, N., Karle, H., and Hansen, N. E. (1988) Lactoferrin-mediated transfer of iron to intracellular ferritin in human monocytes. Eur. J. Haematol. 41, 52–57.

    Article  CAS  Google Scholar 

  • Boxer, L. A., Coates, T. D., Haak, R. A., Wolach, J. B., Hoffstein, S., and Baehner, R. L. (1982) Lactoferrin deficiency associated with altered granulocyte function. New Engl. J. Med. 303, 404–410.

    Article  Google Scholar 

  • Breton-Gorius, J., Mason, D. Y, Buriot, D., Vilde, J.-L., and Griscelli, C. (1980) Lactoferrin deficiency as a consequence of a lack of specific granules in neutrophils from a patient with recurrent infections. Am. J. Pathol. 99, 413–428.

    CAS  Google Scholar 

  • Brines, R. D. and Brock, J. H. (1983) The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum: unusual resistance of human apolactoferrin to proteolytic digestion. Biochim. Biophys. Acta 759, 229–235.

    CAS  Google Scholar 

  • Britigan, B. E., Serody, J. S., Hayek, M. B., Charniga, L. M., and Cohen, M. S. (1991) Uptake of lactoferrin by mononuclear phagocytes inhibits their ability to form hydroxyl radical and protects them from membrane autoperoxidation. J. Immunol. 147, 4271–4277.

    CAS  Google Scholar 

  • Brock, J. H. (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  CAS  Google Scholar 

  • Brock, J. H. and Esparza, I. (1979) Failure of reticulocytes to take up iron from lactoferrin saturated by various methods. Br. J. Haematol. 42, 481–483.

    Article  CAS  Google Scholar 

  • Broxmeyer, H. E. (1989) Iron-binding proteins and the regulation of hematopoietic cell proliferation/differentiation, in Iron in Immunity, Cancer and Inflammation (de Sousa, M. and Brock, J. H., eds.), Wiley, Chichester, UK, pp. 199–221.

    Google Scholar 

  • Bullen, J. J. and Joyce, P. R. (1982) Abolition of the bactericidal function of polymorphs by ferritin-antiferritin complexes. Immunology 46, 497–505.

    CAS  Google Scholar 

  • Bullen, J. J., Rogers, H. J., and Leigh, L. (1972) Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Br. Med. J. 1, 69–75.

    Article  CAS  Google Scholar 

  • Byatt, J. C, Schmuke, J. J., Comens, R G., Johnson, D. A., and Collier, R. J. (1990) The effect of bovine lactoferrin on muscle growth in vivo and in vitro. Biochem. Biophys. Res. Commun. 173, 548–553.

    Article  CAS  Google Scholar 

  • Chen, C.-Y., Berish, S. A., Morse, S. A., and Mietzner, T. A. (1993) The ferric iron-binding protein of Neisseria spp. functions as a periplasmic transport protein in the acquisition of iron from human transferrin. Mol. Microbiol. 10, 311–318.

    Article  CAS  Google Scholar 

  • Cox, T. M., Mazurier, J., Spik, G., Montreuil, J., and Peters, T. J. (1979) Iron binding proteins and influx of iron across the duodenal brush border. Evidence for specific lactotransferrin receptors in the human intestine. Biochim. Biophys. Acta 558, 129–141.

    Google Scholar 

  • Crouch, S. P. M., Slater, K. J., and Fletcher, J. (1992) Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 80, 235–240.

    CAS  Google Scholar 

  • Davidsson, L., Kastenmayer, P., Yuen, M., Lönnerdal, B. and Hurrell, R. F. (1994) Influence of lactoferrin on iron absorption from human milk in infants. Pediatr. Res. 35, 117–124.

    Article  CAS  Google Scholar 

  • De Lillo, A., Tejerina, J. M., and Fierro, J. F. (1992) Interaction of calmodulin with lactoferrin. FEBS Lett. 298, 195–198.

    Article  Google Scholar 

  • De Mingo, J. C., Sánchez, L., Mata, L., Perez, M. D., and Calvo, M. (1994) Study of the interaction between ribonuclease and lactoferrin from bovine and human milk. European Iron Club Meeting, Gargnano, Italy, abstract P19.

    Google Scholar 

  • Devi, A. S., Das, M. R., and Pandit, M. W. (1994) Lactoferrin contains structural motifs of ribonuclease. Biochim. Biophys. Acta 1205, 275–281.

    Article  CAS  Google Scholar 

  • Duncan, R. L. and McArthur, W. P. (1981) Lactoferrin-mediated modulation of mononuclear cell activities. 1. Suppression of the murine in vitro primary antibody response. Cell Immunol 63, 308–320.

    Article  CAS  Google Scholar 

  • Erdei, J., Forsgren, A., and Naidu, A. S. (1994) Lactoferrin binds to porins OmpF and OmpC in Escherichia coli. Infect. Immun. 62, 1236–1240.

    CAS  Google Scholar 

  • Fairweather-Tait, S. J., Balmer, S. E., Scott, P. H., and Minski, M. J. (1987) Lactoferrin and iron absorption in newborn infants. Pediatr. Res. 22, 651–654.

    Article  CAS  Google Scholar 

  • Fletcher, J. (1989) Iron, the iron-binding proteins and bone marrow cell differentiation, in Iron in Immunity, Cancer and Inflammation (de Sousa, M. and Brock, J. H., eds.), Wiley, Chichester, UK, pp. 223–244.

    Google Scholar 

  • Furmanski, P., Li, Z.-P., Fortuna, M. B., Swamy, C. V. B., and Das, M. R. (1989) Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity. J. Exp. Med. 170, 415–429.

    Article  CAS  Google Scholar 

  • Garré, C, Bianchi-Scarrà, G., Sirito, M., Musso, M., and Ravazzolo, R. (1992) Lactoferrin binding sites and nuclear localization in K562(S) cells. J. Cell Physiol. 153,477–482.

    Article  Google Scholar 

  • Griffiths, E. and Bullen, J. J. (1987) Iron binding proteins and host defence, in Iron and Infection (Bullen, J. J. and Griffiths, E., eds.), Wiley, Chichester, UK, pp. 171–209.

    Google Scholar 

  • Halliwell, B. and Gutteridge, J. M. C. (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Meth. Enzymol. 186, 1–85.

    Article  CAS  Google Scholar 

  • Hauer, J., Voetsch, W., and Anderer, F. A. (1994) Identification of a man-nose-acetate-specific 87-kDa receptor responsible for human NK and LAK activity. Immunol. Lett. 42, 7–12.

    Article  CAS  Google Scholar 

  • Hekman, A. (1971) Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility. Biochim. Biophys. Acta 251, 380–387.

    CAS  Google Scholar 

  • Hentges, D. J., Marsh, W. W., Petschow, B. W., Thal, W. R., and Carter, M. K. (1992) Influence of infant diets on the ecology of the intestinal tract of human flora-associated mice. J. Pediatr. Gastroenterol. Nutr. 14, 146–152.

    Article  CAS  Google Scholar 

  • Hovanessian, A. G. and Awdeh, Z. L. (1976) Gel isoelectric focusing of human-serum transferrin. Eur. J. Biochem. 68, 333–338.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Ismail, M. and Brock, J. H. (1993) Binding of lactoferrin and transferrin to the human promonocytic cell line U937. Effect on iron uptake and release. J. Biol. Chem. 268, 21,618–21,625.

    CAS  Google Scholar 

  • Iyer, S. and Lönnerdal, B. (1993) Lactoferrin, lactoferrin receptors and iron metabolism. Eur. J. Clin. Nutr. 47, 232–241.

    CAS  Google Scholar 

  • Jorieux, S., Mazurier, J., Montreuil, J., and Spik, G. (1985) Characterization of lactotransferrin complexes in human milk. Protides Biol. Fluids 32, 115–118.

    Google Scholar 

  • Kajikawa, M., Ohta, T., Takase, M., Kawase, K., Shimamura, S., and Matsuda, I. (1994) Lactoferrin inhibits cholesterol accumulation in macrophages mediated by acetylated or oxidized low-density lipoproteins. Biochim. Biophys. Acta 1213, 82–90.

    CAS  Google Scholar 

  • Kawakami, H., Dosako, S., and Lönnerdal, B. (1990) Iron uptake from transferrin and lactoferrin by rat intestinal brush-border membrane vesicles. Am. J. Physiol. 258, G535-G541.

    CAS  Google Scholar 

  • Kawakami, H., Hiratsuka, M., and Dosako, S. (1988) Effects of iron-saturated lactoferrin on iron absorption. Agric. Biol Chem. 52, 903–908.

    Article  CAS  Google Scholar 

  • Kawakami, H. and Lönnerdal, B. (1991) Isolation and function of a receptor for human lactoferrin in human fetal intestinal brush-border membranes. Am. J. Physiol. 261, G841-G846.

    CAS  Google Scholar 

  • Kawasaki, Y., Isoda, H., Tanimoto, M., Dosako, S., Idota, T., and Ahiko, K. (1992) Inhibition by lactoferrin and K-casein glycomacropeptide of binding of Cholera toxin to its receptor. Biosci. Biotechnol Biochem. 56, 195–198.

    Article  CAS  Google Scholar 

  • Kijlstra, A. and Broersma, L. (1984) Lactoferrin stimulates the production of leucocyte migration inhibitory factor by human peripheral mononuclear phagocytes. Clin. Exp. Immunol. 55, 459–464.

    CAS  Google Scholar 

  • Kohno, Y, Shiraki, K., Mura, T., and Ikawa, S. (1993) Iron-saturated lactoferrin as a co-mitogenic substance for rat hepatocytes in primary culture. Acta Paediatr. 82, 650–655.

    CAS  Google Scholar 

  • Kulics, J. and Kijlstra, A. (1987) The effect of lactoferrin on complement mediated modulation of immune complex size. Immunol Lett. 14, 349–353.

    Article  CAS  Google Scholar 

  • Lampreave, F., Piñeiro, A., Brock, J. H., Castillo, H., Sánchez, L., and Calvo, M. (1990) Interaction of bovine lactoferrin with other proteins of milk whey. Int. J. Biol Macromol. 12, 2–5.

    Article  CAS  Google Scholar 

  • Legrand, D., Mazurier, J., Elass, A., Rochard, E., Vergoten, G., Maes, P., Montreuil, J., and Spik, G. (1992) Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactotransferrin. Biochemistry 31, 9243–9251.

    Article  CAS  Google Scholar 

  • Lima, M. F. and Kierszenbaum, F. (1985) Lactoferrin effects on phagocytic cell function. I. Increased uptake and killing of an intracellular parasite by murine macrophages and human monocytes. J. Immunol. 134, 4176–4183.

    CAS  Google Scholar 

  • Loisillier, F., Burtin, P., and Grabar, P. (1968) Isolement et caractérisation de l’autoantigène responsable de la formation d’auto-anticorps chez les malades atteints de lesions mammaires (cancereuses ou non). Ann. Inst. Pasteur 115, 829–840.

    CAS  Google Scholar 

  • Machnicki, M., Zimecki, M., and Zagulski, T. (1993) Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo. Int. J. Exp. Pathol. 74, 433–439.

    CAS  Google Scholar 

  • Malmquist, J. and Johansson, B. G. (1971) Interaction of lactoferrin with agar gels and with trypan blue. Biochim. Biophys. Acta 236, 38–46.

    CAS  Google Scholar 

  • Mann, D. M., Romm, E., and Migliorini, M. (1994) Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol Chem. 269, 23,661–23,667.

    CAS  Google Scholar 

  • Masson, P. L. and Heremans, J. F. (1971) Lactoferrin in milk from different species. Comp. Biochem. Physiol 39B, 119–129.

    Google Scholar 

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

    Article  CAS  Google Scholar 

  • Mazurier, J., Montreuil, J., and Spik, G. (1985) Visualisation of lactotransferrin brush-border receptors by ligand blotting. Biochim. Biophys. Acta 821, 453–460.

    Article  CAS  Google Scholar 

  • McAbee, D. D. and Esbensen, K. (1991) Binding and endocytosis of apo- and holo-lactoferrin by isolated rat hepatocytes. J. Biol Chem. 266, 23,624–23,631.

    CAS  Google Scholar 

  • McAbee, D. D., Nowatzke, W., Oehler, C., Sitaram, M., Sbaschnig, E., Opferman, J. T., Carr, J., and Esbensen, K. (1993) Endocytosis and degradation of bovine apo- and holo-lactoferrin by isolated rat hepatocytes are mediated by recycling calcium-dependent binding sites. Biochemistry 32, 13,749–13,760.

    Article  CAS  Google Scholar 

  • McCormick, J. A., Markey, G. M., and Morris, T. C. M. (1991) Lactoferrin-inducible monocyte cytotoxicity for K562 cells and decay of natural killer lymphocyte cytotoxicity. Clin. Exp. Immunol. 83, 154–156.

    Article  CAS  Google Scholar 

  • Mikogami, T., Heyman, M., Spik, G., and Desjeux, J.-F. (1994) Apical-to-basolateral transepithelial transport of human lactoferrin in the intestinal cell line HT-29cl.l9A. Am. J. Physiol. 267, G308-G315.

    CAS  Google Scholar 

  • Miyazawa, K., Mantel, C., Lu, L., Morrison, D. C., and Broxmeyer, H. E. (1991) Lactoferrin-lipopolysaccharide interactions. Effect on lactoferrin binding to monocyte/macrophage-differentiated HL-60 cells. J. Immunol. 146, 723–729.

    CAS  Google Scholar 

  • Moguilevsky, N., Masson, P.-L., and Courtoy, P.-J. (1987) Lactoferrin uptake and iron processing into macrophages: a study in familial haemochromatosis. Br. J. Haematol. 66, 129–136.

    CAS  Google Scholar 

  • Moguilevsky, N., Retegui, L. A., and Masson, P. L. (1985) Comparison of human lactoferrins from milk and neutrophilic leucocytes. Biochem. J. 229, 353–359.

    CAS  Google Scholar 

  • Montreuil, J., Tonnelat, J., and Mullet, S. (1960) Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait du femme. Biochim. Biophys. Acta 45, 413–421.

    Article  CAS  Google Scholar 

  • Moreau, M. C., Duval-Iflah, Y., Muller, M. C, Raibaud, P., Vial, M., Gabilan, J. C., and Daniel, N. (1983) Effet de la lactoferrine bovine et des IgG bovines donnés per os sur l’implantation de Escherichia coli dans le tube digestif de souris gnotoxéniques et de nouveau-nés humains. Ann. Microbiol (Inst. Pasteur) 134B, 429–441.

    CAS  Google Scholar 

  • Nichols, B. L., McKee, K. S., and Huebers, H. A. (1990) Iron is not required in the lactoferrin stimulation of thymidine incorporation into the DNA of rat crypt enterocytes. Pediatr. Res. 27, 525–528.

    Article  CAS  Google Scholar 

  • Oram, J. D. and Reiter, B. (1968) Inhibition of bacteria by lactoferrin and other iron-chelating agents. Biochim. Biophys. Acta 170, 351–365.

    CAS  Google Scholar 

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

    CAS  Google Scholar 

  • Otto, B. R., Verweij-van Vught, A. M. J. J., and MacLaren, D. M. (1992) Transferrins and heme-compounds as iron sources for pathogenic bacteria. Crit. Rev. Microbiol. 18, 217–233.

    Article  CAS  Google Scholar 

  • Pettersson, A., Maas, A., and Tommassen, J. (1994) Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor. J. Bacteriol. 176, 1764–1766.

    CAS  Google Scholar 

  • Rainard, P. (1993) Activation of the classical pathway of complement by binding of bovine lactoferrin to unencapsulated Streptococcus agalactiae. Immunology 79, 648–652.

    CAS  Google Scholar 

  • Roberts, A. K., Chierici, R., Sawatzki, G., Hill, M. J., Volpato, S., and Vigi, V. (1992) Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant fecal flora. Acta Paediatr. 81, 119–124.

    Article  CAS  Google Scholar 

  • Roberts, T. K. and Boettcher, B. L. (1969) Identification of sperm-coating antigen. J. Reprod. Fertil. 18, 347–350.

    Article  CAS  Google Scholar 

  • Rochard, E., Legrand, D., Lecocq, M., Hamelin, R., Crepin, M., Montreuil, J., and Spik, G. (1992) Characterization of lactotransferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas. Anticanc. Res. 12, 2047–2052.

    CAS  Google Scholar 

  • Saarinen, U. M., Siimes, M. A., and Dallman, P. R. (1977) Iron absorption in infants: high bioavailability of breast milk iron as indicated by the extrinsic tag method of iron absorption and by the concentration of serum ferritin. J. Pediatr. 91, 36–39.

    Article  CAS  Google Scholar 

  • Sanchez, L., Calvo, M., and Brock, J. H. (1992) Biological role of lactoferrin. Arch. Dis. Child 67, 657–661.

    Article  CAS  Google Scholar 

  • Schryvers, A. B. and Morris, L. J. (1988) Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect. Immun. 56, 1144–1149.

    CAS  Google Scholar 

  • Schulz-Lell, G., Dörner, K., Oldigs, K.-H., Sievers, E., and Schaub, J. (1991) Iron availability from an infant formula supplemented with bovine lactoferrin. Acta Paediatr. Scand. 80, 155–158.

    Article  CAS  Google Scholar 

  • Shau, H., Kim, A., and Golub, S. H. (1992) Modulation of natural killer and lymphokine-activated killer cell cytotoxicity by lactoferrin. J. Leuk. Biol. 51, 343–349.

    CAS  Google Scholar 

  • Sun, I. L., Crane, F. L., Morré, D. J., Low, H., and Faulk, W. P. (1991) Lactoferrin activates plasma membrane oxidase and Na+/H+ antiport activity. Biochem. Biophys. Res. Commun. 176, 498–504.

    Article  CAS  Google Scholar 

  • Thaler, C. J., Vanderpuye, O. A., Mclntyre, J. A., and Faulk, W. R (1990) Lactoferrin binding molecules in human seminal plasma. Biol Reprod. 43, 712–717.

    Article  CAS  Google Scholar 

  • Van der Weil-Korstanje, J. A. A., and de Vries, W. (1973) Cytochrome synthesis by bifidobacterium during growth in media supplemented with blood. J. Gen. Microbiol. 75, 417–419.

    Google Scholar 

  • Van Snick, J. L., Markowetz, B., and Masson, P. L. (1977) The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin. J. Exp. Med. 146, 817–827.

    Article  Google Scholar 

  • Van Snick, J. L. and Masson, P. L. (1976) The binding of lactoferrin to mouse peritoneal cells. J. Exp. Med. 144, 1568–1580.

    Article  Google Scholar 

  • Watanabe, T, Nagura, H., Watanabe, K., and Brown, W. R. (1984) The binding of human milk lactoferrin to immunoglobulin A. FEBS Lett. 168, 203–207.

    Article  CAS  Google Scholar 

  • Zagulski, T, Lipinski, P., Zagulska, A., Broniek, S., and Jarzabek, Z. (1989) Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo. Brit. J. Exp. Pathol 70, 697–704.

    CAS  Google Scholar 

  • Ziere, G. J., Bijsterbosch, M. K., and van Berkel, T. J. C. (1993) Removal of 14 N-terminal amino acids of lactoferrin enhances its affinity for parenchymal liver cells and potentiates the inhibition of ß-very low density lipoprotein binding. J. Biol. Chem. 268, 27,069–27,075.

    CAS  Google Scholar 

  • Zimecki, M., Mazurier, J., Machnicki, M., Wieczorek, Z., Montreuil, J., and Spik, G. (1991) Immunostimulatory activity of lactotransferrin and maturation of CD4”CD8” murine thymocytes. Immunol Lett. 30, 119–124.

    Article  CAS  Google Scholar 

  • Zou, S., Magura, C. E., and Hurley, W. L. (1992) Heparin-binding properties of lactoferrin and lysozyme. Comp. Biochem. Physiol 103B, 889–895.

    CAS  Google Scholar 

  • Zucali, J. R., Broxmeyer, H. E., Levy, D., and Morse, C. (1989) Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1. Blood 74, 1531–1536.

    CAS  Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1997 Humana Press Inc.

About this chapter

Cite this chapter

Brock, J.H. (1997). Lactoferrin Structure-Function Relationships. In: Hutchens, T.W., Lönnerdal, B. (eds) Lactoferrin. Experimental Biology and Medicine, vol 28. Humana Press. https://doi.org/10.1007/978-1-4612-3956-7_1

Download citation

  • DOI: https://doi.org/10.1007/978-1-4612-3956-7_1

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-4612-8439-0

  • Online ISBN: 978-1-4612-3956-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics