FECH Antibody

1. FECH mRNA expression was significantly lower in colon adenocarcinomas compared to normal colon tissues. PMID: 28075030
2. Using a forward chemical genetic approach, FECH was identified as essential for angiogenesis in vitro and in vivo. FECH is overexpressed in wet age-related macular degeneration eyes and murine choroidal neovascularization. PMID: 28377496
3. Quantum mechanical thermodynamic cycle perturbation free energy calculations suggest a plausible pathway for porphyrin metalation in human ferrochelatase. The pathway involves ferrous iron approaching the site coordinated with Met76, while His263 accepts a proton. PMID: 27801584
4. This study indicates that homozygous polymorphism of the FECH gene is associated with a slight elevation of protoporphyrin levels in erythrocytes, resulting in a mild Erythropoietic Protoporphyria (EPP) phenotype. PMID: 26280465
5. This report describes a novel mutation, c.84G>A, in the FECH gene, identified in four individuals with Erythropoietic Protoporphyria. PMID: 26789144
6. High ferrochelatase expression correlates with the growth of malarial parasites in erythropoietic protoporphyria patients. PMID: 25414439
7. Inhibition of FECH mRNA synthesis by ASO-V1 in developing human erythroblasts from an EPP subject significantly increased the production of wild-type FECH mRNA and reduced protoporphyrin IX accumulation to levels similar to 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, along with the common FECH IVS3-48 polymorphism in erythropoietic protoporphyria. PMID: 23600449
9. The study highlights loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and X-linked protoporphyria in North American patients, revealing novel mutations and a high prevalence of X-linked protoporphyria. PMID: 23364436
10. Mutation analysis in the FECH gene identified different genotypes, including t/t, t/M, c/t, and c/M genotypes, from various EPP families. PMID: 19656458
11. Sequencing of the ferrochelatase gene did not reveal any mutations in the patients studied. Additionally, the hypomorphic allele IVS3-48C was absent in all individuals. PMID: 19656459
12. Molecular dynamic simulations provided insights into the conformational movements and functional activity of the active site residues of human ferrochelatase. PMID: 23446439
13. This study investigates the function of solvent-filled channels in human ferrochelatase. PMID: 22712763
14. This research reports ferrochelatase functional variants resulting in erythropoietic protoporphyria in an Ashkenazi Jewish family. PMID: 18758989
15. Both erythropoietic protoporphyria patients and their mother exhibited heterozygosity for a novel mutation (c.1052delA) in the FECH gene of both children, and heterozygosity for the hypomorphic allele IVS3-48T>C in all of them. PMID: 21659066
16. This study explores the role of the 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. Over 96% of unrelated EPP patients exhibit ferrochelatase deficiency. Inheritance of a common hypomorphic IVS3-48C FECH allele trans to a deleterious FECH mutation reduces FECH activity below a critical threshold. PMID: 20850938
19. This study analyzes 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 the phenotypic symptoms observed in this family. PMID: 19888946
21. The stability of newly formed ferrochelatase protein was significantly decreased during iron deficiency. PMID: 19965627
22. This study analyzes skin ferrochelatase and photosensitivity in mice and humans. PMID: 19657351
23. Mutations in the FECH gene were not found to be responsible for the development of liver disease in the severe phenotype of erythropoietic protoporphyria (EPP). PMID: 11929052
24. This research indicates 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. Mutations in ferrochelatase are associated with erythropoietic porphyria. PMID: 15046047
27. This study analyzes 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 a higher risk of severe liver disease in the United Kingdom. PMID: 15286165
29. Data on 12 ferrochelatase wild-type/EPP mutant heterodimers suggest that certain mutations lead to heterodimers with anticipated residual activity, while others result in heterodimers with significantly lower activity than predicted. PMID: 15831704
30. This research demonstrates that a mutation in the FECH gene promoter affects the binding of a transcription factor and causes the erythropoietic protoporphyria phenotype. PMID: 15850836
31. A common single-nucleotide polymorphism of the FECH gene contributes to the genetic predisposition for erythropoietic protoporphyria. PMID: 16385445
32. Erythropoietic protoporphyria patients typically carry a mutation in one FECH allele that alters enzyme structure/function, along with a polymorphism in the nonmutant allele leading to low gene expression. PMID: 16819399
33. These findings suggest that the first 62 amino acids of ferrochelatase enable targeting to mitochondria but do not contain sufficient information for efficient protein processing. 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 by cutaneous photosensitivity. PMID: 17196862
35. This study demonstrates that the substrate is bound deep within an enclosed pocket, and the binding sites with protoporphyrin IX are mapped in detail. PMID: 17261801
36. This research highlights a novel, profilin2-dependent pathway regulating synaptic physiology, neuronal excitability, and complex behavior. PMID: 17566985
37. This study 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 similarly to what is observed in ferrochelatase with bound porphyrin substrate. PMID: 17567154
38. Large deletions of the FECH gene are a significant cause of erythropoietic protoporphyria. PMID: 17597821
39. This study describes a mutation associated with erythropoietic protoporphyria in a Chinese family. PMID: 17723290
40. This research demonstrates that in malignant tissue, a transcriptional down-regulation of FECH occurs, causing endogenous protoporphyrin-IX accumulation. PMID: 17875605
41. The majority of EPP cases arise from the coinheritance of IVS3-48C and a mutation in the FECH gene. The study also documents the existence of patients with mutations in homozygosity, potentially presenting a more severe form of the disease. PMID: 17875872
42. This research indicates that ferrochelatase undergoes significant changes in secondary structure during the catalytic cycle. PMID: 17884090
43. This study describes a ferrochelatase mutation in a Chinese family with erythropoietic protoporphyria. PMID: 18160121
44. This research analyzes FECH mutations in patients with seasonal palmar keratoderma in erythropoietic protoporphyria. PMID: 18787536
45. Ferrochelatase localizes to both the mitochondrial outer and inner membranes. The change in the equilibrium position of the forward and reverse activities may be regulated by the phosphorylation of ferrochelatase. PMID: 19691493
46. This study demonstrates 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. This study analyzes 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