Role of Basic Residues of Human Lactoferrin in the Interaction with B Lymphocytes

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 2, 2000, Pages 314-318

  Kawasaki, Yoshihiro ^a   Sato, Kaoru ^a   Shinmoto, Hiroshi ^a   Dosako, Shunichi ^a  

^a SNOW BRAND MILK PRODUCTS CO LTD   (Japan)

Author keywords

Amino groups acylation; B lymphocytes; Lactoferrin; Peptide conjugation

Indexed keywords

LACTOFERRIN;

AMINO ACID SEQUENCE; ARTICLE; B LYMPHOCYTE; CHEMISTRY; HUMAN; METABOLISM;

AMINO ACID SEQUENCE; B-LYMPHOCYTES; HUMANS; LACTOFERRIN;

EID: 0034133290     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.314     Document Type: Article

References (19)

1. Bennett, R. and Davis, J., Lactoferrin binding to human peripheral blood cells: an interaction with a B-enriched population of lymphocytes and a subpopulation of adherent mononuclear cells. J. Immunol., 127, 1211-1216 (1981).
2. Hu, W. L., Mazurier, J., Sawatzki, G., Montreuil, J., and Spik, G., Lactoferrin receptor of mouse small-intestinal brush border. Binding characteristics of membrane-bound and Triton X-100-solubi-lized forms. Biochem. J., 249, 435-441 (1988).
3. Zimecki, M., Kapp, J., Machnicki, M., Zagulski, T., Wlaszczyk, A., Kubler, A., Mazurier, J., and Spik, G., Lactoferrin. Its role in maturation and function of cells of the immune system and protection against shock in mice. Adv. Exp. Med. Biol., 443, 331-336 (1998).
4. 4 of human lactoferrin interact with sulphated molecules but not with the receptor present on Jurkat human lymphoblastic T-cells. Biochem. J., 327, 841-846 (1997).
5. Sato, K., Shinmoto, H., Tanimoto, M., Dosako, S., and Nakajima, I., Uptake and re-secretion of human lactoferrin by B lymphocytes. Agric. Biol. Chem., 54, 1275-1279 (1990).
6. Sato, K., Shinmoto, H., Tanimoto, M., Kawasaki, Y., Dosako, S., and Taneya, S., Interaction between human lactoferrin and B lymphocytes. In “Animal Cell Culture and Production of Biologi-cals,” eds. Sasaki, R. and Ikura, I., Kluwer Academic Publishers, London, pp. 367-372 (1991).
7. Kawakami, H., Shinmoto, H., Dosako, S., and Sogo, Y., One-step isolation of lactoferrin using immobilized monoclonal antibodies. J. Dairy Sci., 70, 752-759 (1987).
8. Shinmoto, H., Murakami, H., Dosako, S., Shinohara, K., and Omura, M., Human-human hybridomas secreting IgM-like immunoglobulin with a andp heavy chains. Agric. Biol. Chem., 50, 2217-2223 (1986).
9. Lindsay, D. G. and Shall, S., The acetylation of insulin. Biochem. J., 121, 733-745 (1971).
10. Tesser, G. I. and B. Geers, The methylsul-fonylethyloxyearbonyl group, a new and versatile amino protective function. Int. J. Pept. Protein Res., 7, 295-305 (1975).
11. Kimmel, J. R., Guanidination of protein. In “Methods in enzymology, vol. XT’ ed. Hirs, C. H. W., Academic Press, New York, pp. 584-589 (1967).
12. Kawasaki, Y., Murakami, M., Dosako, S., Azuse, I., Nakamura, T., and Okai, H., Characteristics of chymotrypsin modified with water-soluble acylating reagents and its peptide synthesis ability in aqueous organic media. Biosci. Biotechnol. Biochem., 56, 441-444 (1992).
13. 5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem. J., 328, 145-151 (1997).
14. Mann, D. H., Romm, E., and Migliorini, M., Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol. Chem., 269, 23661-12667 (1994).
15. Ziere, G. J., van Dijk, M. C. M., Bijsterbusch, M. K., and van Berkel, T. J. C., Lactoferrin uptake by rat liver. J. Biol. Chem., 267, 11229-11235 (1992).
16. Powell, M. J. and Ogden, J. E., Nucleotide sequence of human lactoferrin. Nucl. Acids Res., 18, 4013 (1990).
17. Maccarana, M., Casu, R., and Lindah, U., Minimal sequence in heparin/heparin sulfate required for binding of basic fibroblast growth factor. J. Biol. Chem., 268, 23898-23905 (1993).
18. Miyata, T., Tokunaga, F., Yoneya, T., Yoshikawa, K., Iwanaga, S., Niwa, M., Takao, T., and Shimonishi, Y., Antimicrobial peptide, isolated from Horseshoe crab hemocytes, tachyplesin II, and poly-phemusins I and II: chemical structure and biological activity. J. Biochem., 106, 663-668 (1989).
19. Selsted, M. and Harwig, S. S. L., Purification, primary structure, and antimicrobial activities of a guinea pig neutrophil defensin. Infect. Immun., 55, 2281-2286 (1987).