The serine protease TMPRSS6 is required to sense iron deficiency

Science

Volumn 320, Issue 5879, 2008, Pages 1088-1092

  Du, Xin ^a   She, Ellen ^a   Gelbart, Terri ^a   Truksa, Jaroslav ^a   Lee, Pauline ^a   Xia, Yu ^a   Khovananth, Kevin ^a   Mudd, Suzanne ^a   Mann, Navjiwan ^a   Moresco, Eva Marie Y ^a   Beutler, Ernest ^a   Beutler, Bruce ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEPCIDIN; SERINE PROTEINASE; ANTIMICROBIAL CATIONIC PEPTIDE; IRON; MATRIPTASE 2; MEMBRANE PROTEIN; TMPRSS6 PROTEIN, HUMAN;

ANEMIA; DIET; ENZYME ACTIVITY; HAIR; IRON; MEMBRANE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FEMALE; GENE; GENE ACTIVATION; GENE OVEREXPRESSION; GENE TMPRSS6; GENETIC TRANSCRIPTION; HAMP GENE; IRON DEFICIENCY; IRON DEPLETION; MALE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PRIORITY JOURNAL; PROMOTER REGION; ANIMAL; BIOLOGICAL MODEL; BLOOD; CHEMISTRY; GENE EXPRESSION REGULATION; GENETIC TRANSFECTION; GENETICS; HUMAN; MACROCYTIC ANEMIA; METABOLISM; MOUSE MUTANT; MUTATION; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION; TRANSGENIC MOUSE; TUMOR CELL LINE;

ANEMIA, MACROCYTIC; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CELL LINE, TUMOR; GENE EXPRESSION REGULATION; HUMANS; IRON; MEMBRANE PROTEINS; MICE; MICE, MUTANT STRAINS; MICE, TRANSGENIC; MODELS, BIOLOGICAL; MUTATION; PHENOTYPE; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, TERTIARY; SERINE ENDOPEPTIDASES; SIGNAL TRANSDUCTION; TRANSFECTION;

EID: 44449177930     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1157121     Document Type: Article

References (30)

1. E. Nemeth, T. Ganz, Annu. Rev. Nutr. 26, 323 (2006).
2. E. Nemeth et al., Science 306, 2090 (2004).
3. G. Nicolas et al., Proc. Natl. Acad. Sci. U.S.A. 99, 4596 (2002).
4. K. A. Ahmad et al., Blood Cells Mol. Dis. 29, 361 (2002).
5. H. Kawabata et al., Blood 105, 376 (2005).
6. G. Papanikolaou et al., Nat. Genet. 36, 77 (2004).
7. R. H. Wang et al., Cell Metab. 2, 399 (2005).
8. G. Nicolas et al., J. Clin. Invest. 110, 1037 (2002).
9. Materials and methods are available as supporting material on Science Online.
10. See the supporting material on Science Online.
11. G. Velasco, S. Cal, V. Quesada, L. M. Sanchez, C. Lopez-Otin, J. Biol. Chem. 277, 37637 (2002).
12. Genomics Institute of the Novartis Research Foundation (GNF) SymAtlas, http://symatlas.gnf.org/SymAtlas/.
13. E. Nemeth et al., Blood 101, 2461 (2003).
14. P. Lee, H. Peng, T. Gelbart, L. Wang, E. Beutler, Proc. Natl. Acad. Sci. U.S.A. 102, 1906 (2005).
15. C. N. Roy, N. C. Andrews, Curr. Opin. Hematol. 12, 107 (2005).
16. J. Truksa, H. Peng, P. Lee, E. Beutler, Proc. Natl. Acad. Sci. U.S.A. 103, 10289 (2006).
17. J. L. Babitt et al., Nat. Genet. 38, 531 (2006).
18. J. Truksa, P. Lee, H. Peng, J. Flanagan, E. Beutler, Blood 110, 3436 (2007).
19. J. Truksa, H. Peng, P. Lee, E. Beutler, Br. J. Haematol. 139, 138 (2007).
20. F. Bazzoni, B. Beutler, N. Engl. J. Med. 334, 1717 (1996).
21. S. S. Watowich, D. J. Hilton, H. F. Lodish, Mol. Cell. Biol. 14, 3535 (1994).
22. D. Gitlin, A. Cruchaud, J. Clin. Invest. 41, 344 (1962).
23. C. Deloche et al., Eur. J. Dermatol. 17, 507 (2007).
24. E. S. Russell, E. C. McFarland, E. L. Kent, Transplant. Proc. 2, 144 (1970).
25. L. A. McNeill et al., Mol. Biosyst. 1, 321 (2005).
26. C. Peyssonnaux et al., J. Clin. Invest. 117, 1926 (2007).
27. D. Yoon et al., J. Biol. Chem. 281, 25703 (2006).
28. E. Beutler, Science 306, 2051 (2004).
29. T. Tanno et al., Nat. Med. 13, 1096 (2007).
30. This work was supported by NIH (grant numbers AI054523 and DK53505-09) and by the Stein Endowment Fund.