FECH Antibody

1. FECH mRNA was largely significantly decreased in colon adenocarcinomas relative to normal colon tissues. PMID: 28075030
2. 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. PMID: 28377496
3. 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. PMID: 27801584
4. 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 PMID: 26280465
5. a novel mutation, c.84G >A, in the FECH gene in four individuals with Erythropoietic Protoporphyria, is reported. PMID: 26789144
6. High ferrochelatase expression is associated with growth of malarial parasites in erythropoietic protoporphyria patients. PMID: 25414439
7. 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 PMID: 24680888
8. 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. PMID: 23600449
9. 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. PMID: 23364466
10. 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. PMID: 19656458
11. 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. PMID: 19656459
12. Molecular dynamic simulations provided insight into the conformational movements and function of the active site residues of human ferrochelatase. PMID: 23446439
13. function of solvent-filled channels in human ferrochelatase PMID: 22712763
14. Report ferrochelatase functional variants resulting in erythropoietic protoporphyria in an Ashkenazi Jewish family. PMID: 18758989
15. 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. PMID: 21659066
16. role of IVS3-48C allele in erythropoietic protoporphyria PMID: 21132468
17. A novel homoallelic missense mutation (p.Ser318Tyr) was identified in the FECH gene in erythropoietic protoporphyria and palmar keratoderma PMID: 20337824
18. 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. PMID: 20850938
19. analysis of the inhibitory metal ion-binding site in ferrochelatase PMID: 20966079
20. A novel splicing FECH mutation in a Chinese erythropoietic protoporphyria family is believed to be responsible for generating the phenotypic symptoms in this family. PMID: 19888946
21. the stability of newly formed ferrochelatase protein was dramatically decreased during iron deficiency PMID: 19965627
22. analysis of skin ferrochelatase and photosensitivity in mice and man PMID: 19657351
23. Mutations in the FECH gene could not account the development of liver disease in the severe phenotype of erythropoietic protoporphyria(EPP). PMID: 11929052
24. Data indicate a significant genotype-phenotype correlation between "null allele" mutation and protoporphyrin related liver disease in erythropoietic protoporphyria. PMID: 11929053
25. Modulation of penetrance by the wild-type allele in dominantly inherited erythrohepatic and acute hepatic porphyrias was studied using FECH. PMID: 14669009
26. Mutation in ferrochelatase is associated with erythropoietic porphyria. PMID: 15046047
27. analysis of frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis PMID: 15123683
28. Identification of autosomal recessive FECH mutations in erythropoietic protoporphyria patients with higher risk of severe liver disease in the United Kingdom. PMID: 15286165
29. data for 12 ferrochelatase wild-type/EPP mutant heterodimers show that some mutations result in heterodimers with the residual activity anticipated, whereas others result in heterodimers with significantly lower activity than would be predicted PMID: 15831704
30. mutation in promoter affects binding of a transcription factor and causes erythropoietic protoporphyria phenotype PMID: 15850836
31. A common single-nucleotide polymorphism of FECH gene contributes to the genetic predisposition for erythropoietic protoporphyria. PMID: 16385445
32. Patients with erythropoietic protoporphyria usually have a mutation in 1 Ferrochelatase allele that alters enzyme structure/function, together with a polymorphism in the nonmutant allele that causes low gene expression. PMID: 16819399
33. These data suggest that the first 62 amino acids of ferrochelatase allow targeting to mitochondria but do not contain sufficient information for efficient processing of the protein. PMID: 16844398
34. Mutations and a low-expressed allele IVS3-48c (in trans to the mutation) of the ferrochelatase (FECH) gene are responsible for erythropoietic protoporphyria (EPP) which is characterized clinically by cutaneous photosensitivity. PMID: 17196862
35. Substrate is bound deep within an enclosed pocket, and the binding sites with protoporphyrin IX are mapped in detail. PMID: 17261801
36. results highlight a novel, profilin2-dependent pathway, regulating synaptic physiology, neuronal excitability, and complex behavior PMID: 17566985
37. It was found that in the H263C and H341C variants, but not the F337A variant enzymes, the side chains of N75, M76, R164, H263, F337, H341, and E343 are oriented in a fashion similar to what is found in ferrochelatase with the bound porphyrin substrate PMID: 17567154
38. large deletions of the FECH gene are an important cause of erythropoietic protoporphyria PMID: 17597821
39. mutation associated with erythropoietic protoporphyria in Chinese family PMID: 17723290
40. show that in malignant tissue a transcriptional down-regulation of FECH occurs, which causes endogenous protoporphyrin-IX accumulation PMID: 17875605
41. most cases of EPP result from the coinheritance of IVS3-48C and a mutation in the FECH gene, and also document the existence of patients with mutations in homozygosity that may present a more severe form of the disease. PMID: 17875872
42. Data shows ferrochelatase undergoes significant changes in secondary structure during the catalytic cycle. PMID: 17884090
43. a ferrochelatase mutation in a Chinese family with erythropoietic protoporphyria. PMID: 18160121
44. analysis of FECH mutations in patients with seasonal palmar keratoderma in erythropoietic protoporphyria PMID: 18787536
45. 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 PMID: 19691493
46. The findings show that at least in the cases of Mn, Pb, Cd, and Hg, metal "inhibition" of ferrochelatase occurs after metal insertion and results from poor or diminished product release. PMID: 19703464
47. analysis of ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase PMID: 19767646

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HGNC: 3647

OMIM: 177000

KEGG: hsa:2235

STRING: 9606.ENSP00000372326

UniGene: Hs.365365