Description:
PROTOPORPHYRIA, ERYTHROPOIETIC
FERROCHELATASE; FECH
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Repository
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NIGMS Human Genetic Cell Repository
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| Subcollection |
Heritable Diseases |
| Class |
Other Disorders of Known Biochemistry |
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Cell Type
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Fibroblast
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Transformant
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Untransformed
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Race
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White
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Relation to Proband
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proband
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Confirmation
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Clinical summary/Case history
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Species
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Homo sapiens
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Common Name
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Human
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Remarks
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| Passage Frozen |
22 |
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| IDENTIFICATION OF SPECIES OF ORIGIN |
Species of Origin Confirmed by Nucleoside Phosphorylase Isoenzyme Electrophoresis |
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| ferrochelatase |
Brenner et al (Am J Hum Genet 50:1203-1210 1992) reported that this fibroblast culture from a patient with protoporphyria had deficient ferrochelatase activity. Ferrochelatase mRNA levels measured by northern blotting were found to be equal to those found in normal controls. Sequence analysis of ferrochelatase cDNA showed a single point mutation a conversion of a T to a C resulting in replacement of phenylalanine (TTC) by a serine (TCC) at amino acid position 417 in the carboxy-terminal end of the protein. EC Number: 4.99.1.1 |
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| ferrochelatase |
According to the submitter, biochemical test results for this subject showed decreased enzyme activity. EC Number: 4.99.1.1 |
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| Gene |
FECH |
| Chromosomal Location |
18q21.31 |
| Allelic Variant 1 |
612386.0004; PROTOPORPHYRIA, ERYTHROPOIETIC |
| Identified Mutation |
PHE417SER; In a case of protoporphyria, Brenner et al. (1992) identified a point mutation resulting in the conversion of codon 417 from phenylalanine (TTC) to serine (TCC) in the carboxy-terminal portion of the protein. Expression of recombinant ferrochelatase in Escherichia coli demonstrated a marked deficiency in activity of the mutant protein.
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| Remarks |
Photosensitivity since infancy; def heme synthetase activity; normal delta-aminolevulinic acid synthetase activity; sim aff sister; fibro show normal ferrochelatase mRNA levels & def enzyme activity; T>C (Phe>Ser) at amino acid #417 |
| Lanzafame M, Branca G, Landi C, Qiang M, Vaz B, Nardo T, Ferri D, Mura M, Iben S, Stefanini M, Peverali FA, Bini L, Orioli D, Cockayne syndrome group A and ferrochelatase finely tune ribosomal gene transcription and its response to UV irradiation Nucleic acids research: 2021 |
| PubMed ID: 34581821 |
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| Brenner DA, Didier JM, Frasier F, Christensen SR, Evans GA, Dailey HA, A molecular defect in human protoporphyria American journal of human genetics50:1203-10 1992 |
| PubMed ID: 1376018 |
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| Bloomer JR, Bonkowsky HL, Ebert PS, Mahoney MJ, Inheritance in protoporphyria. Comparison of haem synthetase activity in skin fibroblasts with clinical features. Lancet2:226-228 1976 |
| PubMed ID: 59242 |
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| Bonkowsky HL, Bloomer JR, Ebert PS, Mahoney MJ, Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts. J Clin Invest56:1139-48 1975 |
| PubMed ID: 1184741 |
| Passage Frozen |
22 |
| Split Ratio |
1:2 |
| Temperature |
37 C |
| Percent CO2 |
5% |
| Percent O2 |
AMBIENT |
| Medium |
Eagle's Minimum Essential Medium with Earle's salts and non-essential amino acids with 2mM L-glutamine or equivalent |
| Serum |
15% fetal bovine serum Not inactivated |
| Substrate |
None specified |
| Subcultivation Method |
trypsin-EDTA |
| Supplement |
- |
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