Maintenance of microsomal hemoprotein concentrations following inhibition of ferrochelatase activity by 3,5-diethoxycarbonyl-1,4-dihydrocollidine in chick embryo liver.

Rifkind, Arleen B.

doi:10.1016/s0021-9258(17)30058-3

Cited by 22 publications

(1 citation statement)

References 43 publications

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“…These data were obtained from different experiments in which pooled livers were assayed 0.75, 1.5, 2 and 2.5 h after injection of the drug (2mg per egg) or solvent (dimethyl sulphoxide). In an attempt to enhance our ability to detect a propylisopropylacetamide-mediated decrease in cytochrome P-450, ferrochelatase activity, and therefore haem synthesis, was inhibited by administering a low dose (0.15 mg/egg) of dicarbethoxydihydrocollidine 8 h before killing (Cole et al, 1979;Rifkind, 1979);…”

Section: Jursfl L Nmentioning

confidence: 99%

Induction of 5-aminolaevulinate synthase in chick embryo liver by propylisopropylacetamide does not involve destruction of cytochrome P-450

Sinclair¹,

Healey²,

Sinclair³

et al. 1981

Biochemical Journal

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Section: Jursfl L Nmentioning

confidence: 99%

Induction of 5-aminolaevulinate synthase in chick embryo liver by propylisopropylacetamide does not involve destruction of cytochrome P-450

Sinclair¹,

Healey²,

Sinclair³

et al. 1981

Biochemical Journal

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Genetic, Metabolic, and Biochemical Aspects of the Porphyrias

Sassa

Kappas

1981

Advances in Human Genetics 11

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Ferrochelatase and N-alkylated porphyrins

Cole

Marks

1984

Mol Cell Biochem

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The final step in heme synthesis is catalyzed by the mitochondrial enzyme, ferrochelatase. Characterization of this enzyme has been complicated by a number of factors including the dependence of enzyme activity on lipids. Purification of ferrochelatase from rat and bovine sources has been achieved only relatively recently using blue Sepharose CL-6B chromatography. When 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine (DDC) is given to animals, it produces a hepatic porphyria resembling human variegate porphyria thus providing an experimental system in which to study this disease. DDC has been found to cause the accumulation of a green pigment, identified as N-methyl protoporphyrin IX (N-MePP), which is a potent inhibitor of ferrochelatase. The source of the N-methyl substituent of N-MePP was found to be the 4-methyl group of DDC. Considerable evidence indicates that the protoporphyrin IX moiety of N-MePP originates from the heme moiety of cytochrome P-450 and that DDC is a suicide substrate for this hemoprotein. Some studies suggest that cytochrome P-450 isozymes differ in their susceptibility to destruction by DDC and its 4-alkyl analogues. Griseofulvin has also been reported to inhibit hepatic ferrochelatase in rodents but not in the 17-day old chick embryo nor in hepatocyte culture systems. Thus, the mechanism by which griseofulvin produces an experimental porphyria in chick embryo liver cell culture is different from that for rodents.

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Maintenance of microsomal hemoprotein concentrations following inhibition of ferrochelatase activity by 3,5-diethoxycarbonyl-1,4-dihydrocollidine in chick embryo liver.

Cited by 22 publications

References 43 publications

Induction of 5-aminolaevulinate synthase in chick embryo liver by propylisopropylacetamide does not involve destruction of cytochrome P-450

Induction of 5-aminolaevulinate synthase in chick embryo liver by propylisopropylacetamide does not involve destruction of cytochrome P-450

Genetic, Metabolic, and Biochemical Aspects of the Porphyrias

Ferrochelatase and N-alkylated porphyrins

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