Hostname: page-component-8448b6f56d-tj2md Total loading time: 0 Render date: 2024-04-24T19:46:01.470Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes

Published online by Cambridge University Press:  01 June 2009

Rosa Oria ,
Maznah Ismail ,
Lourdes Sánchez ,
Miguel Calvo  and
Jeremy H. Brock
Rosa Oria
Affiliation:
Tecnología de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, c/Miguel Servet 177, 50013 Zaragoza, España
Maznah Ismail
Affiliation:
University Department of Immunology, Western Infirmary, Glasgow G11 6NT, UK
Lourdes Sánchez
Affiliation:
Tecnología de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, c/Miguel Servet 177, 50013 Zaragoza, España
Miguel Calvo
Affiliation:
Tecnología de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, c/Miguel Servet 177, 50013 Zaragoza, España
Jeremy H. Brock
Affiliation:
University Department of Immunology, Western Infirmary, Glasgow G11 6NT, UK
Get access Rights & Permissions [Opens in a new window]

Summary

The interaction of lactoferrin from human and bovine milk with the human promonocytic cell line U937 has been studied. Both human and bovine Fe-lactoferrins bound to the cells. Binding of bovine lactoferrin was inhibited by excess bovine lactoferrin but not by human lactoferrin, suggesting that the binding mechanisms for the two proteins are different. Binding of human but not bovine lactoferrin was inhibited by bovine lactoperoxidase, while a 20-fold excess of human IgA inhibited binding of human but not bovine lactoferrin. Human and bovine α-lactalbumins, bovine β-lactoglobulin, and human lysozyme had no effect on binding of lactoferrin from either species. Samples of bovine Fe- and apolactoferrin in capillary tubes were exposed to temperatures of 72 °C for 20 s, 85 °C for 20 min or 137 °C for 8 s. All the heated samples inhibited binding of native Fe- and apolactoferrin, though to a lesser extent than the native proteins. Both heated and native lactoferrins enhanced [3H]thymidine incorporation by U937 cells, except for Fe-lactoferrin heated at 85 °C for 20 min, which was inhibitory. These results suggest that heat treatment of lactoferrin under conditions used for industrial processing does not greatly affect its ability to interact with and stimulate monocytic cells, and that other milk proteins in general do not interfere with lactoferrin–monocyte interactions. It may thus be feasible to incorporate biologically active lactoferrin into infant formulas.

Type
Original Articles
Information
Journal of Dairy Research , Volume 60 , Issue 3 , August 1993 , pp. 363 - 369
Copyright
Copyright © Proprietors of Journal of Dairy Research 1993

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Amouric, M., Marvaldi, J., Pichon, J., Bellot, F. & Figarella, C. 1984 Effect of lactoferrin on the growth of a human colon adenocarcinoma cell line—comparison with transferrin. In Vitro 20 543–548CrossRefGoogle ScholarPubMed
Baker, E. N., Rumball, S. V. & Anderson, B. F. 1987 Transferring: insights into structure and function from studies on lactoferrin. Trends in Biochemical Sciences 12 350–353CrossRefGoogle Scholar
Birgens, H. S., Hansen, N. E., Karle, H. & Kristensen, L. Ø. 1983 Receptor binding of lactoferrin by human monocytes. British Journal of Haematology 54 383–391CrossRefGoogle ScholarPubMed
Birgens, H. S., Kristensen, L. Ø., Borregaard, N., Karle, H. & Hansen, N. E. 1988 Lactoferrin-mediated transfer of iron to intracellular ferritin in human monocytes. European Journal of Haematology 41 52–57CrossRefGoogle ScholarPubMed
Chetley, A. 1979 The Baby Killer Scandal. London: War on WantGoogle Scholar
Dautry-Varsat, A. 1986 Receptor-mediated endocytosis: the intracellular journey of transferrin and its receptor. Biochimie 68 375–381CrossRefGoogle ScholarPubMed
Davidson, L. A. & Lönnerdal, B. 1988 Specific binding of lactoferrin to brush-border membrane: ontogeny and effect of glycan chain. American Journal of Physiology 254 G580–G585Google ScholarPubMed
Diaz De Villegas, C., Oria, R., Sala, F. J. & Calvo, M. 1987 Lipid binding by β-lactoglobulin of cow milk. Milchwissenschaft 42 357–358Google Scholar
Graf, E., Mahoney, J. R., Bryant, R. G. & Eaton, J. W. 1984 Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site. Journal of Biological Chemistry 259 3620–3624CrossRefGoogle ScholarPubMed
Graham, G. & Bates, G. W. 1976 Approaches to the standardization of serum unsaturated iron-binding capacity. Journal of Laboratory and Clinical Medicine 88 477–486Google Scholar
Greenwood, F. C., Hunter, W. M. & Glover, J. S. 1963 The preparation of 131I-labelled human growth hormone of high specific radioactivity. Biochemical Journal 89 114–123CrossRefGoogle Scholar
Iturralde, M., Vass, J. K., Oria, R. & Brock, J. H. 1992 Effect of iron and retinoic acid on the control of transferrin receptor and ferritin in the human promonocytic cell line U937. Biochimica et Biophysica Acta 1133 241–246CrossRefGoogle ScholarPubMed
Johannson, B. G. 1969 Isolation of crystalline lactoferrin from human milk. Acta Chemica Scandinavica 23 683–684CrossRefGoogle Scholar
Jorieux, S., Mazurier, J., Montreuil, J. & Spik, G. 1985 Characterization of lactotransferrin complexes in human milk. Protides of the Biological Fluids 32 115–118CrossRefGoogle Scholar
Kawakami, H., Dosako, S. & Lönnerdal, B. 1990 Iron uptake from transferrin and lactoferrin by rat intestinal brush-border membrane vesicles. American Journal of Physiology 258 G535–G541Google ScholarPubMed
Lampreave, F., Piñeiro, A., Brock, J. H., Castillo, H., Sánchez, L. & Calvo, M. 1990 Interaction of bovine lactoferrin with other proteins of milk whey. International Journal of Biological Macromolecules 12 2–5CrossRefGoogle ScholarPubMed
Mazurier, J., Legrand, D., Hu, W. L., 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. European Journal of Biochemistry 179 481–487CrossRefGoogle ScholarPubMed
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. Biochimica et Biophysica Acta 629 399–408CrossRefGoogle ScholarPubMed
Oria, R., Alvarez-Hernández, X., Licéaga, J. & Brock, J. H. 1988 Uptake and handling of iron from transferrin, lactoferrin and immune complexes by a macrophage cell line. Biochemical Journal 252 221–225CrossRefGoogle ScholarPubMed
Sánchez, L., Calvo, M. & Brock, J. H. 1992 a Biological role of lactoferrin. Archives of Disease in Childhood 67 657–661CrossRefGoogle ScholarPubMed
Sánchez, L., Peiró, J. M., Castillo, H., Pérez, M. D., Ena, J. M. & Calvo, M. 1992 b Kinetic parameters for denaturation of lactoferrin in milk. Journal of Food Science in pressCrossRefGoogle Scholar
Sussman, H. H. 1989 Iron and tumour cell growth. In Iron in Immunity, Cancer and Inflammation, pp. 261–282 (Eds de Sousa, M. & Brock, J. H.). Chichester: John WileyGoogle Scholar
Watanabe, T., Nagura, H., Watanabe, K. & Brown, W. R. 1984 The binding of human milk lactoferrin to immunoglobulin A. FEES Letters 168 203–207CrossRefGoogle ScholarPubMed