The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

FECH  -  ferrochelatase

Homo sapiens

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of FECH

 

Psychiatry related information on FECH

  • Both job-specific and comprehensive FCEs can be valuable tools in clinical decision-making for the injured worker with foot and ankle dysfunction; however, FCE is an extremely complex and multifaceted process [6].
 

High impact information on FECH

  • The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH [2].
  • However, the amount was 2-3 times more in cultured fibroblasts from patients with protoporphyria, reflecting their deficiency of heme synthetase activity [7].
  • These studies indicate that excessive protoporphyrin accumulation in protoporphyria, which is due principally to deficient heme synthetase activity, may be modified by the rate of ALA formation in heme-producing tissues, and by the availability of iron [7].
  • The mutations of the codons for 2 of the [2Fe-2S] cluster ligands in patients with EPP supports the importance of the iron-sulfur center for the proper functioning of mammalian FECH and, in at least humans, its absence has a direct clinical impact [8].
  • Three of the point mutations, in 3 patients, resulted in FECH variants with 2 of the [2Fe-2S] cluster cysteines substituted with tyrosine, serine, and glycine (ie, C406Y, C406S, and C411G) and with undetectable enzymatic activity [8].
 

Chemical compound and disease context of FECH

 

Biological context of FECH

 

Anatomical context of FECH

  • Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts [18].
  • Contrary to Dista A, FCE 24517 has been found to display potent cytotoxic activity on human and murine tumour cell lines [19].
  • The ribosomal fraction contained heme synthetase activity and its characteristics were similar to that described in avian erythrocytes, human and rat liver, and rabbit reticulocytes [20].
  • The activity of heme synthetase (ferrochelatase), the enzyme(s) which catalyzes the formation of heme from iron and protoporphyrin IX, was studied in the various fractions of a cell-free reticulocyte system which synthesizes hemoglobin [20].
  • The progenitor cells were generally similar in their response to FCE 24517 within a species [21].
 

Associations of FECH with chemical compounds

  • Phase I and endocrine study of exemestane (FCE 24304), a new aromatase inhibitor, in postmenopausal women [22].
  • Plasma concentrations of FCE 23762 and its 13-dihydro metabolite, FCE 26176, were measured in 20 patients at doses > or = 675 micrograms/m2, using HPLC with fluorescence detection [23].
  • We investigated the effects of the antiviral agent distamycin A and of a distamycin derivative (FCE 24517) which possesses antineoplastic activity on the binding of some regulatory proteins to DNA [16].
  • The alkylating benzoyl mustard derivative tallimustine (FCE 24517) has powerful anti-tumor activity [24].
  • FCE 24517, a novel distamycin derivative possessing potent antitumor activity, is under initial clinical investigation in Europe. In spite of the presence of a benzoyl nitrogen mustard group this compound fails to alkylate the N7 position of guanine, the major site of alkylation by conventional nitrogen mustards [15].
  • When compared with the location of N-methylmesoporphyrin in the Bacillus subtilis ferrochelatase, the porphyrin is rotated by approximately 100 degrees and is buried an additional 4.5 A deeper within the active site [25].
 

Analytical, diagnostic and therapeutic context of FECH

References

  1. Human gene mutations. Gene symbol: FECH. Disease: Porphyria, erythropoietic. Di Pierro, E., Moriondo, V., Cappellini, M.D. Hum. Genet. (2004) [Pubmed]
  2. The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH. Gouya, L., Puy, H., Robreau, A.M., Bourgeois, M., Lamoril, J., Da Silva, V., Grandchamp, B., Deybach, J.C. Nat. Genet. (2002) [Pubmed]
  3. Inheritance in erythropoietic protoporphyria: a common wild-type ferrochelatase allelic variant with low expression accounts for clinical manifestation. Gouya, L., Puy, H., Lamoril, J., Da Silva, V., Grandchamp, B., Nordmann, Y., Deybach, J.C. Blood (1999) [Pubmed]
  4. EPP masquerading as angioedema. Weston, W.L. J. Allergy Clin. Immunol. (1978) [Pubmed]
  5. Clinical and bacteriological efficacy and tolerability of FCE 22891 in patients with exacerbations of chronic obstructive pulmonary disease. Boersma, W.G., Puister, S.M., van Altena, R., de Vries-Hospers, H.G., Molinari, M., Koëter, G.H. Antimicrob. Agents Chemother. (1994) [Pubmed]
  6. The role of functional capacity evaluation in management of foot and ankle dysfunction. Lechner, D.E. Foot and ankle clinics. (2002) [Pubmed]
  7. Study of factors causing excess protoporphyrin accumulation in cultured skin fibroblasts from patients with protoporphyria. Bloomer, J.R., Brenner, D.A., Mahoney, M.J. J. Clin. Invest. (1977) [Pubmed]
  8. Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria. Schneider-Yin, X., Gouya, L., Dorsey, M., Rüfenacht, U., Deybach, J.C., Ferreira, G.C. Blood (2000) [Pubmed]
  9. In-vitro activity of the new penems FCE 22101 and FCE 24362 alone or in combination with aminoglycosides against streptococci isolated from patients with endocarditis. Dornbusch, K., Henning, C., Lindén, E. J. Antimicrob. Chemother. (1989) [Pubmed]
  10. Characterisation of a LoVo subline resistant to a benzoyl mustard derivative of distamycin A (FCE 24517). Capolongo, L., Melegaro, G., Broggini, M., Mongelli, N., Grandi, M. Br. J. Cancer (1993) [Pubmed]
  11. Broad phase II and pharmacokinetic study of methoxy-morpholino doxorubicin (FCE 23762-MMRDX) in non-small-cell lung cancer, renal cancer and other solid tumour patients. Bakker, M., Droz, J.P., Hanauske, A.R., Verweij, J., van Oosterom, A.T., Groen, H.J., Pacciarini, M.A., Domenigoni, L., van Weissenbruch, F., Pianezzola, E., de Vries, E.G. Br. J. Cancer (1998) [Pubmed]
  12. Synthesis and aromatase inhibition by potential metabolites of exemestane (6-methylenandrosta-1,4-diene-3,17-dione). Buzzetti, F., Di Salle, E., Longo, A., Briatico, G. Steroids (1993) [Pubmed]
  13. Photosensitivity and acute liver injury in myeloproliferative disorder secondary to late-onset protoporphyria caused by deletion of a ferrochelatase gene in hematopoietic cells. Goodwin, R.G., Kell, W.J., Laidler, P., Long, C.C., Whatley, S.D., McKinley, M., Badminton, M.N., Burnett, A.K., Williams, G.T., Elder, G.H. Blood (2006) [Pubmed]
  14. Molecular analysis of functional and nonfunctional genes for human ferrochelatase: isolation and characterization of a FECH pseudogene and its sublocalization on chromosome 3. Whitcombe, D.M., Albertson, D.G., Cox, T.M. Genomics (1994) [Pubmed]
  15. DNA sequence-specific adenine alkylation by the novel antitumor drug tallimustine (FCE 24517), a benzoyl nitrogen mustard derivative of distamycin. Broggini, M., Coley, H.M., Mongelli, N., Pesenti, E., Wyatt, M.D., Hartley, J.A., D'Incalci, M. Nucleic Acids Res. (1995) [Pubmed]
  16. Distamycins inhibit the binding of OTF-1 and NFE-1 transfactors to their conserved DNA elements. Broggini, M., Ponti, M., Ottolenghi, S., D'Incalci, M., Mongelli, N., Mantovani, R. Nucleic Acids Res. (1989) [Pubmed]
  17. Pharmacokinetics of FCE 22891, a new oral penem. Saathoff, A., Lode, H., Hampel, B., Deppermann, K.M., Borner, K., Koeppe, P. Antimicrob. Agents Chemother. (1990) [Pubmed]
  18. Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts. Bonkowsky, H.L., Bloomer, J.R., Ebert, P.S., Mahoney, M.J. J. Clin. Invest. (1975) [Pubmed]
  19. Biological profile of FCE 24517, a novel benzoyl mustard analogue of distamycin A. Pezzoni, G., Grandi, M., Biasoli, G., Capolongo, L., Ballinari, D., Giuliani, F.C., Barbieri, B., Pastori, A., Pesenti, E., Mongelli, N. Br. J. Cancer (1991) [Pubmed]
  20. Hemoglobin synthesis in a rabbit ribosomal system: localization of heme synthetase activity. Gribble, T.J., Edmunds, D., Schwartz, H.C. Pediatr. Res. (1977) [Pubmed]
  21. Comparative in vitro myelotoxicity of FCE 24517, a distamycin derivative, to human, canine and murine hematopoietic progenitor cells. Volpe, D.A., Du, D.L., Zurlo, M.G., Mongelli, N., Murphy, M.J. Investigational new drugs. (1992) [Pubmed]
  22. Phase I and endocrine study of exemestane (FCE 24304), a new aromatase inhibitor, in postmenopausal women. Evans, T.R., Di Salle, E., Ornati, G., Lassus, M., Benedetti, M.S., Pianezzola, E., Coombes, R.C. Cancer Res. (1992) [Pubmed]
  23. Phase I clinical and pharmacokinetic study of 3'-deamino-3'-(2-methoxy-4-morpholinyl)doxorubicin (FCE 23762). Vasey, P.A., Bissett, D., Strolin-Benedetti, M., Poggesi, I., Breda, M., Adams, L., Wilson, P., Pacciarini, M.A., Kaye, S.B., Cassidy, J. Cancer Res. (1995) [Pubmed]
  24. Distamycin A and tallimustine inhibit TBP binding and basal in vitro transcription. Bellorini, M., Moncollin, V., D'Incalci, M., Mongelli, N., Mantovani, R. Nucleic Acids Res. (1995) [Pubmed]
  25. Substrate interactions with human ferrochelatase. Medlock, A., Swartz, L., Dailey, T.A., Dailey, H.A., Lanzilotta, W.N. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  26. Pharmacokinetics of [14C]FCE 22891, a penem antibiotic, following oral administration to healthy volunteers. Efthymiopoulos, C., Strolin Benedetti, M., Sassella, D., Boobis, A., Davies, D. Antimicrob. Agents Chemother. (1992) [Pubmed]
  27. Mild hypothermia after severe transient hypoxia-ischemia ameliorates delayed cerebral energy failure in the newborn piglet. Thoresen, M., Penrice, J., Lorek, A., Cady, E.B., Wylezinska, M., Kirkbride, V., Cooper, C.E., Brown, G.C., Edwards, A.D., Wyatt, J.S. Pediatr. Res. (1995) [Pubmed]
 
WikiGenes - Universities