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. 1973 Aug;134(4):847–857. doi: 10.1042/bj1340847

A model for the regulation of δ-aminolaevulinate synthetase induction in rat liver

Govindarajan Padmanaban 1, Manchanahalli R Satyanarayana Rao 1, Krishnamachari Malathi 1
PMCID: PMC1177892  PMID: 4762758

Abstract

A reciprocal relationship exists between the cytochrome P-450 content and δ-aminolaevulinate synthetase activity in adult rats. In young rats the basal δ-aminolaevulinate synthetase activity is higher and the cytochrome P-450 content is lower compared with the adult rat liver. Administration of allylisopropylacetamide neither induces the enzyme nor causes degradation of cytochrome P-450 in the young rat liver, unlike adult rat liver. Allylisopropylacetamide fails to induce δ-aminolaevulinate synthetase in adrenalectomized–ovariectomized animals or intact animals pretreated with successive doses of the drug, in the absence of cortisol. The cortisol-mediated induction of the enzyme is sensitive to actinomycin D. Allylisopropylacetamide administration degrades microsomal haem but not nuclear haem. Haem does not counteract the decrease in cytochrome P-450 content caused by allylisopropylacetamide administration, but there is evidence for the formation of drug-resistant protein-bound haem in liver microsomal material under these conditions. Phenobarbital induces δ-aminolaevulinate synthetase under conditions when there is no breakdown of cytochrome P-450. On the basis of these results and those already published, a model is proposed for the regulation of δ-aminolaevulinate synthetase induction in rat liver.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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