Iron status in mice carrying a targeted disruption of lactoferrin

Molecular and Cellular Biology

Volumn 23, Issue 1, 2003, Pages 178-185

  Ward, Pauline P ^a   Mendoza Meneses, Marisela ^a   Cunningham, Grainne A ^a   Conneely, Orla M ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IRON; IRON BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; GENE DISRUPTION; GENE TARGETING; HOMEOSTASIS; INTESTINE; IRON BLOOD LEVEL; IRON METABOLISM; IRON TRANSPORT; KNOCKOUT MOUSE; MILK LEVEL; MOUSE; MUCOSA; NEUTROPHIL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; SECRETORY GRANULE;

ANIMALS; ANIMALS, NEWBORN; ANIMALS, SUCKLING; DUODENUM; FEMALE; HOMEOSTASIS; INTESTINES; IRON; LACTOFERRIN; MALE; MICE; MICE, INBRED STRAINS; MICE, KNOCKOUT; MILK; RNA, MESSENGER; TRANSFERRIN;

ANIMALIA;

EID: 0037214319     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.1.178-185.2003     Document Type: Article

References (52)

1. Anderson, B. F., H. M. Baker, E. J. Dodson, G. E. Norris, S. V. Rumball, J. M. Waters, and E. N. Baker. 1987. Structure of human lactoferrin at 3.2-A resolution. Proc. Natl. Acad. Sci. USA 84:1769-1773.
2. Anderson, B. F., H. M. Baker, G. E. Norris, D. W. Rice, and E. N. Baker. 1989. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 A resolution. J. Mol. Biol. 209:711-734.
3. Andrews, N. C. 2000. Iron homeostasis: Insights from genetics and animal models. Nat. Rev. Genet. 1:208-217.
4. Bailey, S., R. W. Evans, R. C. Garratt, B. Gorinsky, S. Hasnain, C. Horsburgh, H. Jhoti, P. F. Lindley, A. Mydin, R. Sarra, et al. 1988. Molecular structure of serum transferrin at 3.3-A resolution. Biochemistry 27:5804-5812.
5. Baranov, V. S., A. L. Schwartzman, V. N. Gorbunova, V. S. Gaitskhoki, N. B. Rubtsov, N. A. Timchenko, and S. A. Neifakh. 1987. Chromosomal localization of ceruloplasmin and transferrin genes in laboratory rats, mice and in man by hybridization with specific DNA probes. Chromosoma 96:60-66,
6. Baveye, S., E. Elass, J. Mazurier, G. Spik, and D. Legrand. 1999. Lactoferrin: A multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin. Chem. Lab. Med. 37:281-286.
7. Bernstein, S. E. 1987. Hereditary hypotransferrinemia with hemosiderosis, a murine disorder resembling human atransferrinemia. J. Lab. Clin. Med. 110:690-705.
8. Brock, J. 1995. Lactoferrin: A multifunctional immunoregulatory protein? Immunol. Today 16:417-419.
9. 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.
10. Canonne-Hergaux, F., S. Gruenheid, P. Ponka, and P. Gros. 1999. Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93:4406-4417.
11. Cheng, H., and C. P. Leblond. 1974. Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. V. Unitarian theory of the origin of the four epithelial cell types. Am. J. Anat. 141:537-561.
12. Clothier, B., S. Robinson, R. A. Akhtar, J. E. Francis, T. J. Peters, K. Raja, and A. G. Smith. 2000. Genetic variation of basal iron status, ferritin and iron regulatory protein in mice: Potential for modulation of oxidative stress. Biochem. Pharmacol. 59:115-122.
13. Cohn, S. M., T. C. Simon, K. A. Roth, E. H. Birkenmeier, and J. I. Gordon. 1992. Use of transgenic mice to map cis-acting elements in the intestinal fatty acid binding protein gene (Fabpi) that control its cell lineage-specific and regional patterns of expression along the duodenal-colonic and crypt-villus axes of the gut epithelium. J. Cell Biol. 119:27-44.
14. Cox, T. M., J. Mazurier, G. Spik, J. Montreuil, and T. J. Peters. 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 588:120-128.
15. Cunningham, G. A., D. R. Headon, and O. M. Conneely. 1992. Structural organization of the mouse lactoferrin gene. Biochem. Biophys. Res. Commun. 189:1725-1731.
16. Davidson, L. A., and B. Lonnerdal. 1987. Persistence of human milk proteins in the breast-fed infant. Acta Paediatr. Scand. 76:733-740.
17. Feder, J. N., A. Gnirke, W. Thomas, Z. Tsuchihashi, D. A. Ruddy, A. Basava, F. Dormishian, R. Domingo, Jr., M. C. Ellis, A. Fullan, L. M. Hinton, N. L. Jones, B. E. Kimmel, G. S. Kronmal, P. Lauer, V. K. Lee, D. B. Loeb, F. A. Mapa, E. McClelland, N. C. Meyer, G. A. Mintier, N. Moeller, T. Moore, E. Morikang, R. K. Wolff, et al. 1996. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat. Genet. 13:399-408.
18. Fleming, M. D., M. A. Romano, M. A. Su, L. M. Garrick, M. D. Garrick, and N. C. Andrews. 1998. Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. USA 95:1148-1153.
19. Fleming, M. D., C. C. Trenor III, M. A. Su, D. Foernzler, D. R. Beier, W. F. Dietrich, and N. C. Andrews. 1997. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16:383-386.
20. Fleming, R. E., C. C. Holden, S. Tomatsu, A. Waheed, E. M. Brunt, R. S. Britton, B. R. Bacon, D. C. Roopenian, and W. S. Sly. 2001. Mouse strain differences determine severity of iron accumulation in Hfe knockout model of hereditary hemochromatosis. Proc. Natl. Acad. Sci. USA 98:2707-2711.
21. Fleming, R. E., and W. S. Sly. 2002. Mechanisms of iron accumulation in hereditary hemochromatosis. Annu. Rev. Physiol. 64:663-680.
22. Gunshin, H., B. Mackenzie, U. V. Berger, Y. Gunshin, M. F. Romero, W. F. Boron, S. Nussberger, J. L. Gollan, and M. A. Hediger. 1997. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388:482-488.
23. Iyer, S., and B. Lonnerdal. 1993. Lactoferrin, lactoferrin receptors and iron metabolism. Eur. J. Clin. Nutr. 47:232-241.
24. Komiya, T., Y. Tanigawa, and S. Hirohashi. 1998. Cloning of the novel gene intelectin, which is expressed in intestinal Paneth cells in mice. Biochem. Biophys. Res. Commun. 251:759-762.
25. Leboeuf, R. C., D. Tolson, and J. W. Heinecke. 1995. Dissociation between tissue iron concentrations and transferrin saturation among inbred mouse strains, J. Lab. Clin. Med. 126:128-136.
26. Lee, E. Y., M. H. Barcellos-Hoff, L. H. Chen, G. Parry, and M. J. Bissell. 1987. Transferrin is a major mouse milk protein and is synthesized by mammary epithelial cells. In Vitro Cell. Dev. Biol. 23:221-226.
27. Levay, P. F., and M. Viljoen. 1995. Lactoferrin: A general review. Haematologica 80:252-267.
28. Levy, J. E., O. Jin, Y. Fujiwara, F. Kuo, and N. C. Andrews. 1999. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21:396-399.
29. Levy, J. E., L. K. Montross, D. E. Cohen, M. D. Fleming, and N. C. Andrews. 1999. The C282Y mutation causing hereditary hemochromatosis does not produce a null allele. Blood 94:9-11.
30. Mansour, S. L., K. R. Thomas, and M. R. Capecchi. 1988. Disruption of the proto-oncogene int-2 in mouse embryo-derived stem cells: A general strategy for targeting mutations to non-selectable genes. Nature 336:348-352.
31. Masson, P. L., J. F. Heremans, and E. Schonne. 1969. Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130:643-658.
32. Masson, P. L., Heremans, J. F., and C. Dive. 1966. An iron-binding protein common to many external secretions. Clin, Chim. Acta 14:735-739.
33. McLaren, G. D. 1989. Reticuloendothelial iron stores and hereditary hemochromatosis: A paradox. J. Lab. Clin. Med. 113:137-138.
34. Metz-Boutigue, M. H., J. Jolles, J. Mazurier, F. Schoentgen, D. Legrand, G. Spik, J. Montreuil, and P. Jolles. 1984. Human lactotransferrin: Amino acid sequence and structural comparisons with other transferrins. Eur. J. Biochem. 145:659-676.
35. Neville, M. C., K. Chatfield, L. Hansen, A. Lewis, J. Monks, J. Nuijens, M. Ollivier-Bousquet, F. Schanbacher, V. Sawicki, and P. Zhang. 1998. Lactoferrin secretion into mouse milk. Development of secretory activity, the localization of lactoferrin in the secretory pathway, and interactions of lactoferrin with milk iron. Adv. Exp. Med. Biol. 443:141-153.
36. Nuijens, J. H., P. H. van Berkel, and F. L. Schanbacher. 1996. Structure and biological actions of lactoferrin. J. Mammary Gland Biol. Neoplasia 1:285-295.
37. Pentecost, B. T., and C. T. Teng. 1987. Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions. J. Biol. Chem. 262:10134-10139.
38. Pietrangelo, A. 2002. Physiology of iron transport and the hemochromatosis gene. Am. J. Physiol. Gastrointest. Liver Physiol. 282:G403-G414.
39. Sigmund, C. D. 2000. Viewpoint: Are studies in genetically altered mice out of control? Arterioscler. Thromb. Vasc. Biol. 20:1425-1429.
40. Soriano, P., C. Montgomery, R. Geske, and A. Bradley. 1991. Targeted disruption of the c-src proto-oneogene leads to osteopetrosis in mice. Cell 64:693-702.
41. Sproule, T. J., E. C. Jazwinska, R. S. Britton, B. R. Bacon, R. E. Fleming, W. S. Sly, and D. C. Roopenian. 2001. Naturally variant autosomal and sex-linked loci determine the severity of iron overload in beta 2-microglobulin-deficient mice. Proc. Natl. Acad. Sci. USA 98:5170-5174.
42. Suzuki, Y. A., K. Shin, and B. Lonnerdal. 2001. Molecular cloning and functional expression of a human intestinal lactoferrin receptor. Biochemistry 40:15771-15779.
43. Teng, C. T., B. T. Pentecost, A. Marshall, A. Solomon, B. H. Bowman, P. A. Lalley, and S. L. Naylor. 1987. Assignment of the lactotransferrin gene to human chromosome 3 and to mouse chromosome 9. Somat. Cell Mol. Genet. 13:689-693.
44. Tsuji, S., J. Uehori, M. Matsumoto, Y. Suzuki, A. Matsuhisa, K. Toyoshima, and T. Seya. 2001. Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall. J. Biol. Chem. 276:23456-23463.
45. van Renswoude, J., K. R. Bridges, J. B. Harford, and R. D. Klausner. 1982. Receptor-mediated endocytosis of transferrin and the uptake of Fe in K562 cells: Identification of a nonlysosomal acidic compartment. Proc. Natl. Acad. Sci. USA 79:6186-6190.
46. Ward, P. P., H. Chu, X. Zhou, and O. M. Conneely. 1997. Expression and characterization of recombinant murine lactoferrin. Gene 204:171-176.
47. Ward, P. P., M. Mendoza-Meneses, B. Mulac-Jericevic, G. A. Cunningham, O. Saucedo-Cardenas, C. T. Teng, and O. M. Conneely. 1999. Restricted spatiotemporal expression of lactoferrin during murine embryonic development. Endocrinology 140:1852-1860.
48. Ward, P. P., S. Uribe-Luna, and O. M. Conneely. 2002. Lactoferrin and host defense. Biochem. Cell Biol. 80:95-102.
49. Weinberg, E. D. 2001. Human lactoferrin: A novel therapeutic with broad spectrum potential. J. Pharm. Pharmacol. 53:1303-1310.
50. Wessling-Resnick, M. 2000: Iron transport. Annu. Rev. Nutr. 20:129-151.
51. Wice, B. M., and J. I. Gordon. 1998. Forced expression of Id-1 in the adult mouse small intestinal epithelium is associated with development of adenomas. J. Biol. Chem. 273:25310-25319.
52. Zhou, X. Y., S. Tomatsu, R. E. Fleming, S. Parkkila, A. Waheed, J. Jiang, Y. Fei, E. M. Brunt, D. A. Ruddy, C. E. Prass, R. C. Schatzman, R. O'Neill, R. S. Britton, B. R. Bacon, and W. S. Sly. 1998. HFE gene knockout produces mouse model of hereditary hemochromatosis. Proc. Natl. Acad. Sci. USA 95:2492-2497.