Synergistic induction of delta-aminolevulinate synthase by glutethimide and iron: relationship to the synergistic induction of heme oxygenase.

@article{Cable1991SynergisticIO,
  title={Synergistic induction of delta-aminolevulinate synthase by glutethimide and iron: relationship to the synergistic induction of heme oxygenase.},
  author={Edward Earl Cable and John F. Healey and Y J Greene and C O Evans and Herbert L. Bonkovsky},
  journal={Biochimica et biophysica acta},
  year={1991},
  volume={1080 3},
  pages={
          245-51
        }
}
Hepatic 5-aminolevulinic acid synthase mRNA stability is modulated by inhibitors of heme biosynthesis and by metalloporphyrins.
TLDR
In primary cultures of chick embryo liver cells, whether a decrease in cellular heme might increase 5-aminolevulinic acid synthase mRNA stability and whether heme or other metalloporphyrins could reverse this stabilization was tested and found it was markedly increased by inhibitors of heme biosynthesis.
Regulation of heme metabolism in rat hepatocytes and hepatocyte cell lines: delta-aminolevulinic acid synthase and heme oxygenase are regulated by different heme-dependent mechanisms.
TLDR
The results reported here demonstrate the function of the regulatory heme pool on both ALA synthase and heme oxygenase in a mammalian hepatocyte system and demonstrate that regulation of ALa synthase mRNA levels by heme in a mammals system is mediated by a change in ALA syntheses mRNA stability.
Repression of hepatic δ‐aminolevulinate synthase by heme and metalloporphyrins: Relationship to inhibition of heme oxygenase
TLDR
Low doses of zinc mesoporphyrin and heme, in combination, may be a useful treatment for patients with acute porphyria after induction of δ‐aminolevulinate synthase by exposure of gliver cells to several chemicals.
Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: Evidence against a stress-mediated response
TLDR
It is concluded that heme and other non-heme metalloporphyrins induce heme oxygenase-1 through a mechanism requiring protein synthesis, not because metalliporphyrin increase cellular oxidative or other stress.
Upregulation of Heme Pathway Enzyme ALA Synthase-1 by Glutethimide and 4,6-Dioxoheptanoic Acid and Downregulation by Glucose and Heme: A Dissertation
Aminolevulinic acid synthasel (ALASI) is the first and normally rate-controlling enzyme for hepatic heme biosynthesis. ALASl is highly inducible , especially in liver, in response to changes in
Mechanism of the synergistic induction of CYP2H by isopentanol plus ethanol: comparison to glutethimide and relation to induction of 5-aminolevulinate synthase.
TLDR
The results indicate that the alcohols and glutethimide coordinately increase ALAS and CYP2H1 mRNA, and that increases in CYP 2H1/2 protein arise from increases in its mRNA.
Repression of ALA synthase by heme and zinc‐mesoporphyrin in a chick embryo liver cell culture model of acute porphyria
TLDR
A liver cell culture model for acute hepatic porphyrias that recapitulates the biochemical features of the human syndrome is characterized and the treatment of choice of acute porphyric syndromes may be the combination of low doses of heme and zinc‐mesoporphyrin or another similarly non‐toxic inhibitor of he me oxygenase.
Effect of sodium arsenite on heme metabolism in cultured chick embryo hepatocytes.
TLDR
The results suggest that although 2.5 microM arsenite induced heme oxygenase four- to sixfold, this had no effect on degradation of exogenous heme and this did not affect the regulatory heme pool.
Molecular basis for heme-dependent induction of heme oxygenase in primary cultures of chick embryo hepatocytes. Demonstration of acquired refractoriness to heme.
TLDR
A down-regulation of the intracellular machinery required for heme-dependent induction of heme oxygenase-1 is suggested, suggesting a short-lived protein plays a key role in modulating heme Oxygenase1 mRNA levels.
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References

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Mechanism of synergistic induction of hepatic heme oxygenase by glutethimide and iron: studies in cultured chick embryo liver cells.
TLDR
This work shows that, in cultured chick embryo liver cells, synergistic induction of heme oxygenase by iron, added with the phenobarbital-like drug, glutethimide was heme-dependent, providing evidence for the heme -dependent mechanism of induction.
Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem.
TLDR
It is found that the mRNAs for ALA synthase and PB1 P-450 were rapidly and simultaneously induced by the porphyrinogenic drugs glutethimide and 2-propyl-2-isopropylacetamide, suggesting the presence of a labile repressor which modulates PB1 p-450 gene expression.
delta-Aminolaevulinate synthase in human HepG2 hepatoma cells. Repression by haemin and induction by chemicals.
TLDR
Findings indicate that the level of ALA synthase in HepG2 cells is maintained by both synthesis and degradation of the enzyme, and that the synthesis of the enzymes is regulated by the concentration of regulatory free haem in the cell.
Adrenalectomy enhances the induction of heme oxygenase and the degradation of cytochrome P-450 in liver.
TLDR
Treatment with hydrocortisone and adrenalectomy can significantly influence the extent of the induction of heme oxygenase produced by CoCl2, but that both the initial decline and the rebound induction of delta-aminolevulinate synthase associated with this metal treatment are apparently independent of these endocrine controls.
Haem control in experimental porphyria. The effect of haemin on the induction of delta-aminolaevulinate synthase in isolated chick-embryo liver cells.
TLDR
Exogenously added haemin was shown completely to inhibit 2-allyl-2-isopropylacetamide-mediated delta-aminolaevulinate synthase induction at concentrations as low as 20nm, a value that is less than the reported physiological one, and suggests that the primary effect of haemin is at the level of transcription.
Hepatic heme metabolism and its control.
TLDR
It is believed it is unlikely that iron, rather than heme itself, is a physiologic regulator of hepatic heme metabolism, although this hypothesis has lately been proposed.
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