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Gene Review

Fech  -  ferrochelatase

Mus musculus

Synonyms: AI894116, Fcl, Ferrochelatase, mitochondrial, Heme synthase, Protoheme ferro-lyase, ...
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Disease relevance of Fech


High impact information on Fech


Chemical compound and disease context of Fech


Biological context of Fech


Anatomical context of Fech


Associations of Fech with chemical compounds


Physical interactions of Fech

  • Function analysis of the promoter by transient transfection assay demonstrated that one Sp1 binding site located at -37/-32 is essential for basic expression of the ferrochelatase gene in both mouse erythroleukemia (MEL) and non-erythroid EL4 cells [17].

Other interactions of Fech


Analytical, diagnostic and therapeutic context of Fech


  1. Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease. Tutois, S., Montagutelli, X., Da Silva, V., Jouault, H., Rouyer-Fessard, P., Leroy-Viard, K., Guénet, J.L., Nordmann, Y., Beuzard, Y., Deybach, J.C. J. Clin. Invest. (1991) [Pubmed]
  2. Hepatic gene expression in protoporphyic Fech mice is associated with cholestatic injury but not a marked depletion of the heme regulatory pool. Davies, R., Schuurman, A., Barker, C.R., Clothier, B., Chernova, T., Higginson, F.M., Judah, D.J., Dinsdale, D., Edwards, R.E., Greaves, P., Gant, T.W., Smith, A.G. Am. J. Pathol. (2005) [Pubmed]
  3. Molecular cloning, sequencing, and expression of mouse ferrochelatase. Taketani, S., Nakahashi, Y., Osumi, T., Tokunaga, R. J. Biol. Chem. (1990) [Pubmed]
  4. Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases. Dailey, H.A., Sellers, V.M., Dailey, T.A. J. Biol. Chem. (1994) [Pubmed]
  5. Long-term cure of the photosensitivity of murine erythropoietic protoporphyria by preselective gene therapy. Pawliuk, R., Bachelot, T., Wise, R.J., Mathews-Roth, M.M., Leboulch, P. Nat. Med. (1999) [Pubmed]
  6. Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells. Sassa, S. J. Exp. Med. (1976) [Pubmed]
  7. Biliary fibrosis associated with altered bile composition in a mouse model of erythropoietic protoporphyria. Meerman, L., Koopen, N.R., Bloks, V., Van Goor, H., Havinga, R., Wolthers, B.G., Kramer, W., Stengelin, S., Müller, M., Kuipers, F., Jansen, P.L. Gastroenterology (1999) [Pubmed]
  8. Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase. Taketani, S., Kakimoto, K., Ueta, H., Masaki, R., Furukawa, T. Blood (2003) [Pubmed]
  9. Mammalian ferrochelatase, a new addition to the metalloenzyme family. Ferreira, G.C., Franco, R., Lloyd, S.G., Pereira, A.S., Moura, I., Moura, J.J., Huynh, B.H. J. Biol. Chem. (1994) [Pubmed]
  10. Expression of ferrochelatase mRNA in erythroid and non-erythroid cells. Chan, R.Y., Schulman, H.M., Ponka, P. Biochem. J. (1993) [Pubmed]
  11. Ferrochelatase, a novel target for photodynamic therapy of cancer. Bhasin, G., Kausar, H., Athar, M. Oncol. Rep. (1999) [Pubmed]
  12. Studies on the mechanism of experimental porphyria and ferrochelatase inhibition produced by 3,5-diethoxycarbonyl-1,4-dihydrocollidine. Tephly, T.R., Gibbs, A.H., Ingall, G., De Matteis, F. Int. J. Biochem. (1980) [Pubmed]
  13. Cloning of murine ferrochelatase. Brenner, D.A., Frasier, F. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  14. Probing the active site loop motif of murine ferrochelatase by random mutagenesis. Shi, Z., Ferreira, G.C. J. Biol. Chem. (2004) [Pubmed]
  15. Reversion of hepatobiliary alterations By bone marrow transplantation in a murine model of erythropoietic protoporphyria. Fontanellas, A., Mazurier, F., Landry, M., Taine, L., Morel, C., Larou, M., Daniel, J.Y., Montagutelli, X., de Salamanca, R.E., de Verneuil, H. Hepatology (2000) [Pubmed]
  16. Hyperlipidemia and atherosclerosis associated with liver disease in ferrochelatase-deficient mice. Bloks, V.W., Plösch, T., van Goor, H., Roelofsen, H., Baller, J., Havinga, R., Verkade, H.J., van Tol, A., Jansen, P.L., Kuipers, F. J. Lipid Res. (2001) [Pubmed]
  17. Structure and transcriptional regulation of the mouse ferrochelatase gene. Taketani, S., Mohri, T., Hioki, K., Tokunaga, R., Kohno, H. Gene (1999) [Pubmed]
  18. Function of the [2FE-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor. Sellers, V.M., Johnson, M.K., Dailey, H.A. Biochemistry (1996) [Pubmed]
  19. Ferrochelatase binds the iron-responsive element present in the erythroid 5-aminolevulinate synthase mRNA. Ferreira, G.C. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  20. Porphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzyme. Franco, R., Bai, G., Prosinecki, V., Abrunhosa, F., Ferreira, G.C., Bastos, M. Biochem. J. (2005) [Pubmed]
  21. The ferrochelatase gene structure and molecular defects associated with erythropoietic protoporphyria. Taketani, S., Fujita, H. J. Bioenerg. Biomembr. (1995) [Pubmed]
  22. Increased plasma transferrin, altered body iron distribution, and microcytic hypochromic anemia in ferrochelatase-deficient mice. Lyoumi, S., Abitbol, M., Andrieu, V., Henin, D., Robert, E., Schmitt, C., Gouya, L., de Verneuil, H., Deybach, J.C., Montagutelli, X., Beaumont, C., Puy, H. Blood (2007) [Pubmed]
  23. Biphasic ordered induction of heme synthesis in differentiating murine erythroleukemia cells: role of erythroid 5-aminolevulinate synthase. Lake-Bullock, H., Dailey, H.A. Mol. Cell. Biol. (1993) [Pubmed]
  24. Effect of Griseofulvin on 5-aminolevulinate synthase and on ferrochelatase in mouse liver neoplastic nodules. Denk, H., Kalt, R., Abdelfattach-Gad, M., Meyer, U.A. Cancer Res. (1981) [Pubmed]
  25. An exon 10 deletion in the mouse ferrochelatase gene has a dominant-negative effect and causes mild protoporphyria. Magness, S.T., Maeda, N., Brenner, D.A. Blood (2002) [Pubmed]
  26. Binding of protoporphyrin IX and metal derivatives to the active site of wild-type mouse ferrochelatase at low porphyrin-to-protein ratios. Lu, Y., Sousa, A., Franco, R., Mangravita, A., Ferreira, G.C., Moura, I., Shelnutt, J.A. Biochemistry (2002) [Pubmed]
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