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Erythropoietic protoporphyria (EPP) is an inherited disorder caused by a partial deficiency of the enzyme ferrochelatase. Ferrochelatase catalyzes the insertion of ferrous ions into protoporphyrin IX, the last step in heme biosynthesis. As a result of ferrochelatase deficiency, protoporphyrin is accumulated in various tissues; this accumulation is responsible for the clinical symptoms of light sensitivity and, in rare cases, liver damage (1). Several mutations have been identified in the human ferrochelatase (FECH) gene among EPP patients (2). The results indicate a possible link between the “null-allele” mutations (i.e., mutations that lead to the formation of a truncated enzyme) in the FECH gene and liver complications in EPP (3). Although EPP is considered an autosomal dominant disorder, only ∼10% of individuals with a defective enzyme develop clinical symptoms. A recent study suggested that symptomatic patients differ from asymptomatic gene carriers by the amount of mRNA output from the nonmutated allele. This so-called “low expressed” wild-type FECH allele, identified in EPP patients, is highly associated with a specific haplotype at two single nucleotide polymorphism (SNP) sites in the FECH gene namely, a G at the −251 position in the promoter region and a T at IVS1-23 (4). These latest developments in the pathogenesis of EPP allow prediction of the …

clinical chemistry

New Missense Mutation in the Human Ferrochelatase Gene in a Family with Erythropoietic Protoporphyria: Functional Studies and Correlation of Genotype and Phenotype