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抗Rat (Rattus) FECH 抗体:
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Cow (Bovine) Polyclonal FECH Primary Antibody for WB - ABIN2776936
Najahi-Missaoui, Dailey: Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases. in Blood 2005
Show all 2 Pubmed References
The plastidic type II ferrochelatase contains a C-terminal chlorophyll a/b (CAB) motif, a conserved hydrophobic stretch homologous to the CAB domain of plant light- harvesting proteins.
The apparent surplus of FeCH activity in the wild type is critical for cell viability under high light due to a regulatory role of FeCH in the distribution of Chl into apoproteins.
Analysis of the recombinant full-length and truncated ferrochelatase (FeCH) demonstrated that the C-terminal extension is critical for activity of the FeCH and that it is strictly required for oligomerization of this enzyme.
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.
analysis of the inhibitory metal ion-binding site in ferrochelatase
Fech forms an oligomeric complex with Mfrn1 and Abcb10 to synergistically integrate mitochondrial iron importation and use for heme biosynthesis.
Ferrochelatase activity and protein levels were dramatically decreased in Irp2(-/-) spleens, whereas ferrochelatase mRNA levels were increased, demonstrating posttranscriptional regulation of ferrochelatase in vivo
analysis of skin ferrochelatase and photosensitivity in mice and man
Binding of protoporphyrin IX and metal derivatives to the active site of wild-type enzyme at low porphyrin-to-protein ratios
exon 10-deleted ferrochelatase heterozygous mice exhibited skin photosensitivity but no liver disease
analysis of the active site loop motif of murine ferrochelatase
hydrogen bonding between ferrochelatase and mesoporphyrin is a key factor in the thermodynamics of the binding reaction
Protoporphyric (Fech(m1pas)/Fech(m1pas) mice (C57BL/6J) showed a higher degree of liver pathology and more protoporphyrin accumulation than corresponding SJL/J and BALB/cJ mice. In the latter mice, mitochondrial respiratory chain activity was increased.
These results suggest that specific conserved loop residues (especially Trp256) are directly involved in the saddling of the porphyrin substrate.
The kinetic mechanisms of inhibition of two variants of ferrochelatase by N-methylprotoporphyrin are reported.
Ferrochelatase knockout mice are a model for erythropoietic protoporphyria (EPP). Accumulation of protoporphyrin in EPP was not affected by stimulation of fecal fat excretion.
conversion of zinc mesoporphyrin to mesoheme was observed to be dependent on ferrochelatase
These results provide new insights into the role of the active site residues of ferrochelatase in controlling stereospecificity, distortion and metallation.
3-D structural models are presented (for wild-type and mutant expressed forms); binding of porphyrin (primary product) is studied using simulation models; amino acid sequence and alignment with 5 other ferrochelatase sequences are presented
ferrochelatase localizes to both the mitochondrial outer and inner membranes, and the change in the equilibrium position of the forward and reverse activities may be regulated by the phosphorylation of ferrochelatase
the iron-removal reverse activity of FECH
The results of FECH gene expression suggested that the homozygosity for the c.315-48T>C variant could be considered pathological. Thus, this study identified the homozygotes for the c.315-48T>C variant as pathological. By extension, when the samples were categorised according to the haplotypes, the GTC haplotype in homozygosis was pathological.
FECH mRNA was largely significantly decreased in colon adenocarcinomas relative to normal colon tissues.
Using a forward chemical genetic approach, the authors identified the heme synthesis enzyme ferrochelatase (FECH) as necessary for angiogenesis in vitro and in vivo FECH is overexpressed in wet age-related macular degeneration eyes and murine choroidal neovascularization.
Using surface plasmon resonance, physiologically relevant concentrations of isatin (25-100 muM) were found to increase affinity of interactions between human recombinant ferrochelatase (FECH) and NADPH-dependent adrenodoxin reductase (ADR).
In this study, QM/MM and quantum mechanical thermodynamic cycle perturbation free energy calculations were performed to investigate the porphyrin metalation in human ferrochelatase. It suggests a most reasonable pathway including the steps of the ferrous iron approaching from the site with Met76 coordinated and His263 playing the role of accepting proton.
These findings suggest that homozygous polymorphism of the FECH gene is associated with a slight elevation of the protoporphyrin level in erythrocytes, resulting in a mild EPP phenotype
a novel mutation, c.84G >A, in the FECH gene in four individuals with Erythropoietic Protoporphyria, is reported.
High ferrochelatase expression is associated with growth of malarial parasites in erythropoietic protoporphyria patients.
of ASO-V1 into developing human erythroblasts from an overtly EPP subject markedly increased the production of WT FECH mRNA and reduced the accumulation of PPIX to a level similar to that measured in asymptomatic EPP subjects
Sequence analysis of the FECH gene identified a novel missense mutation in exon 4 (c.418>A, G140R) of the FECH gene, as well as the common FECH IVS3-48 polymorphism in erythropoietic protoporphyria.
Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria.
The mutation analysis in the FECH gene identified different genotypes with the t/t genotype, 7 with the t/M genotype, 14 with the c/t genotype and 10 with c/M genotype from different EPP families.
Sequencing of the ferrochelatase gene did not show a mutation in any of the patients studied. Furthermore, the hypomorphic allele IVS3-48C was absent in all individuals.
Molecular dynamic simulations provided insight into the conformational movements and function of the active site residues of human ferrochelatase.
function of solvent-filled channels in human ferrochelatase
Report ferrochelatase functional variants resulting in erythropoietic protoporphyria in an Ashkenazi Jewish family.
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.
role of IVS3-48C allele in erythropoietic protoporphyria
A novel homoallelic missense mutation (p.Ser318Tyr) was identified in the FECH gene in erythropoietic protoporphyria and palmar keratoderma
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 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.
, ferrochelatase, mitochondrial
, heme synthase
, heme synthetase
, protoheme ferro-lyase