Untersuchungen zur famili�ren, protoporphyrin�mischen Lichturticaria

Langhof, H; Mueller, H; Rietschel, Liz

doi:10.1007/bf00483032

Cited by 60 publications

(17 citation statements)

References 10 publications

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“…EPP is characterized by the accumulation of protoporphyrin and by acute solar photosensitivity, established by Mangus et al (1961) and Langhof et al (1961). The disease is generally known to be inherited in an autosomal dominant characteristic with partial penetrance.…”

Section: Molecular Basis Of Erythropoietic Protoporphyriamentioning

confidence: 99%

Molecular and Genetic Characterization of Ferrochelatase.

Taketani

1993

Tohoku J. Exp. Med.

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Section: Molecular Basis Of Erythropoietic Protoporphyriamentioning

confidence: 99%

Molecular and Genetic Characterization of Ferrochelatase.

Taketani

1993

Tohoku J. Exp. Med.

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“…Of the recognized inherited disorders of porphyrin metabolism, the last to be described (3,4) has been called "erythropoietic protoporphyria. "1 The biochemical hallmark of this disorder is an increase in protoporphyrin concentration in red cells, stool, or both (6).…”

Section: Introductionmentioning

confidence: 99%

Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts.

Bonkowsky¹,

Bloomer²,

Ebert³

et al. 1975

J. Clin. Invest.

211

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“…EPP is characterized by the accumulation of protoporphyrin and by acute solar photosensitivity, established by Mangus [Y4] and Langhofet al [95]. The disease is known to be inherited as an autosomal dominant trait with variable clinical expression.…”

Section: Molecular Basis Of Erythropoietic Protoporphyriamentioning

confidence: 99%

Molecular and genetic characterization of ferrochelatase

Taketani

1994

Stem Cells

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Abstract. Ferrochelatase (heme synthase, protoheme ferrolyase [EC 4.99.1.1]), the final enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous ion into protoporphyrin IX to produce protoheme IX. The thorough understanding of the enzyme is prerequisite to elucidating the regulation of iron and heme metabolism. The enzyme's activity is found on the inner mitochondria1 membrane of a variety of mammalian cells. The enzyme catalyzes the chelation not only of iron but also of divalent metal ions including cobalt and zinc, and the activity is affected by various metals and lipids. The molecular weights of eukaryotic ferrochelatases are 40,000-42,000 daltons. Complementary DNA (cDNA) encoding ferrochelatase from mouse, human, yeast and bacteria have been isolated, and the derived amino acid sequences show 27438% homologies among species. The expression of ferrochelatase seems to occur in all living cells, and to play an important role in the regulation of heme biosynthesis. Ferrochelatase is markedly induced at the transcriptional level during erythroid differentiation when iron uptake by cells and hemoglobin synthesis are upregulated. This induction can be explained by the existence of sequences characteristic of erythroid-related genes. The gene has been mapped to human chromosome 18q21.3 and contains 11 exons with a size of about 45 kilobases. Once the gene for human ferrochelatase is cloned, the molecular basis and clinical diagnosis of erythropoietic protoporphyria, caused by a deficiency of ferrochelatase, will become possible. This review summarizes recent advances in ferrochelatase research and suggests important subjects for future research.

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Untersuchungen zur famili�ren, protoporphyrin�mischen Lichturticaria

Cited by 60 publications

References 10 publications

Molecular and Genetic Characterization of Ferrochelatase.

Molecular and Genetic Characterization of Ferrochelatase.

Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts.

Molecular and genetic characterization of ferrochelatase

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