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ferrochelatase, FECH
The protein encoded by this gene is localized to the mitochondrion, where it catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway. Mutations in this gene are associated with erythropoietic protoporphyria. Two transcript variants encoding different isoforms have been found for this gene. A pseudogene of this gene is found on chromosome 3.[provided by RefSeq, May 2010] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, STEP, V1a
Papers using ferrochelatase antibodies
Sphingosine-1-phosphate receptor type 1 regulates glioma cell proliferation and correlates with patient survival
Hamada J-I et al., In British Journal of Cancer, 2008
... Rabbit polyclonal antibody and mouse polyclonal antibody against FECH were purchased from LifeSpan Biosciences (Seattle, WA, USA) ...
Papers on ferrochelatase
Protoporphyrin IX: the Good, the Bad, and the Ugly.
Ma et al., Galveston, United States. In J Pharmacol Exp Ther, Feb 2016
PPIX serves as the substrate for ferrochelatase, the final enzyme in heme biosynthesis, and its homeostasis is tightly regulated during heme synthesis.
Identification and characterization of haemofungin, a novel antifungal compound that inhibits the final step of haem biosynthesis.
Osherov et al., Tel Aviv-Yafo, Israel. In J Antimicrob Chemother, Feb 2016
Genetic and biochemical analyses in A. nidulans and Aspergillus fumigatus indicate that haemofungin primarily inhibits ferrochelatase (HemH), the last enzyme in the haem biosynthetic pathway.
[Erythropoietic protoporphyria : Clinical manifestations, diagnosis and new therapeutic possibilities].
Neumann et al., Düsseldorf, Germany. In Hautarzt, Jan 2016
BACKGROUND: Erythropoietic protoporphyria, the second most common type of the cutaneous porphyrias, is due to an enzymatic deficiency of ferrochelatase, the last enzyme in heme biosynthesis.
A metabolomic perspective of griseofulvin-induced liver injury in mice.
Ma et al., Pittsburgh, United States. In Biochem Pharmacol, Jan 2016
Griseofulvin (GSF) causes hepatic porphyria in mice, which mimics the liver injury associated with erythropoietic protoporphyria (EPP) in humans.
X-linked dominant protoporphyria: The first reported Japanese case.
Moriwaki et al., Ōsaka, Japan. In J Dermatol, Oct 2015
To obtain a definitive diagnosis, genetic analyses were performed using samples from all family members, which revealed no mutations in the ferrochelatase-encoding gene (FECH), which is responsible for EPP.
The influence of host genetics on erythrocytes and malaria infection: is there therapeutic potential?
Burgio et al., Canberra, Australia. In Malar J, 2014
These novel findings include the reliance of the parasite on the host enzyme ferrochelatase, and the discovery of basigin and CD55 as obligate erythrocyte receptors for parasite invasion.
A Novel Mutation in the FECH Gene in a Czech Family with Erythropoietic Protoporphyria and a Population Study of IVS3-48C Variant Contributing to the Disease.
Martásek et al., Praha, Czech Republic. In Folia Biol (praha), 2014
In most EPP patients, clinical expression requires coinheritance of a private ferrochelatase (FECH) mutation trans- to a hypomorphic FECH*IVS3-48C allele.
Tracking cancer drugs in living cells by thermal profiling of the proteome.
Drewes et al., Heidelberg, Germany. In Science, 2014
We identified the heme biosynthesis enzyme ferrochelatase as a target of kinase inhibitors and suggest that its inhibition causes the phototoxicity observed with vemurafenib and alectinib.
A commentary on the role of skin temperature on the effectiveness of ALA-PDT in Dermatology.
Mordon, Lille, France. In Photodiagnosis Photodyn Ther, 2014
Several mechanisms could be responsible: a better ALA uptake and/or an higher PpIX production into cells due to an improved enzymatic process, mainly due to the increased activity of ferrochelatase.
[Heme metabolism as an integral part of iron homeostasis].
Staroń et al., Panama. In Postepy Hig Med Dosw (online), 2013
The biogenesis of [Fe-S] centers is crucial for heme synthesis because these co-factors determine the activity of IRP1 and that of ferrochelatase, an enzyme responsible for the insertion of an iron into protoporphyrin IX to produce heme.
Mitochondrial Atpif1 regulates haem synthesis in developing erythroblasts.
Paw et al., Boston, United States. In Nature, 2012
Defects in the availability of haem substrates or the catalytic activity of the terminal enzyme in haem biosynthesis, ferrochelatase (Fech), impair haem synthesis and thus cause human congenital anaemias.
Erythropoietic Protoporphyria, Autosomal Recessive
Desnick et al., Seattle, United States. In Unknown Journal, 2012
CLINICAL CHARACTERISTICS: Erythropoietic protoporphyria (EPP) is characterized by cutaneous photosensitivity (usually beginning in infancy or childhood) that results in tingling, burning, pain, and itching within minutes of sun/light exposure and may be accompanied by swelling and redness.
5-aza-2'-deoxycytidine activates iron uptake and heme biosynthesis by increasing c-Myc nuclear localization and binding to the E-boxes of transferrin receptor 1 (TfR1) and ferrochelatase (Fech) genes.
Nie et al., Beijing, China. In J Biol Chem, 2011
5-aza-2'-deoxycytidine activates iron uptake and heme biosynthesis by increasing c-Myc nuclear localization and binding to the E-boxes of transferrin receptor 1 (TfR1) and ferrochelatase (Fech) genes.
Erythropoietic protoporphyria: a family study and report of a novel mutation in the FECH gene.
Azevedo et al., Porto, Portugal. In Eur J Dermatol, 2011
Erythropoietic protoporphyria patients and their mother revealed heterozygosity for a novel mutation (c.1052delA) in FECH gene of both children, and heterozygosity for the hypomorphic allele IVS3-48T>C in all of them.
Identification and characterization of an inhibitory metal ion-binding site in ferrochelatase.
Ferreira et al., Tampa, United States. In J Biol Chem, 2011
analysis of the inhibitory metal ion-binding site in ferrochelatase
The low expression allele (IVS3-48C) of the ferrochelatase gene leads to low enzyme activity associated with erythropoietic protoporphyria.
Taketani et al., In Int J Hematol, 2010
role of IVS3-48C allele in erythropoietic protoporphyria
[Inheritance in erythropoietic protoporphyria].
Puy et al., Colombes, France. In Pathol Biol (paris), 2010
More than 96% of unrelated EPP patients have ferrochelatase deficiency (MIM 177000). Inheritance of a common hypomorphic IVS3-48C FECH allele trans to a deleterious FECH mutation reduces FECH activity below a critical threshold. Review.
The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH.
Deybach et al., Colombes, France. In Nat Genet, 2002
Erythropoietic protoporphyria (EPP) is an inherited disorder of heme biosynthesis caused by a partial deficiency of ferrochelatase (FECH, EC
Long-term cure of the photosensitivity of murine erythropoietic protoporphyria by preselective gene therapy.
Leboulch et al., Cambridge, United States. In Nat Med, 1999
Erythropoietic protoporphyria is a genetic disease in which ferrochelatase is defective.
A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria.
Dailey et al., Cape Town, South Africa. In Nat Genet, 1996
While earlier workers thought the distal haem biosynthetic enzyme ferrochelatase may be involved in the genesis of VP, it was shown in the early 1980's, and is now accepted, that VP is associated with decreased protoporphyrinogen oxidase activity (PPO) (E.C.
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