Effect of organic forms of selenium on delta-aminolevulinate dehydratase from liver, kidney, and brain of adult rats.

@article{Barbosa1998EffectOO,
  title={Effect of organic forms of selenium on delta-aminolevulinate dehydratase from liver, kidney, and brain of adult rats.},
  author={Nilda B. V. Barbosa and Jo{\~a}o Batista T Rocha and Gilson Rog{\'e}rio Zeni and Tatiana Emanuelli and Marisa C Beque and Antonio Luiz Braga},
  journal={Toxicology and applied pharmacology},
  year={1998},
  volume={149 2},
  pages={
          243-53
        }
}
The inhibitory effect of various forms of organic selenium compounds and of diphenyl ditelluride (PhTe)2 on delta-aminolevulinate dehydratase (delta-ALA-D) from liver, kidney, and brain of rats was investigated because it has been reported that organocalcogens catalyze the oxidation of thiols. Diphenyl diselenide (PhSe)2, rho-chloro-diphenyl diselenide (rho ClPhSe)2, propyl-2-2-diphenyl diselenide, and propyl-2-methoxy-2-phenyl selenide inhibited delta-ALA-D and the IC50 ranged from 2 to 32… 

Short communication Mechanisms of the inhibitory effects of selenium and mercury on the activity of d-aminolevulinate dehydratase from mouse liver, kidney and brain

TLDR
Results suggest a similar inhibitory mechanism of Se 4� and Hg 2� on d-ALA-D in which oxidation of sulfhydryl groups located at the active site of the enzyme is an essential step.

Reaction of diphenyl diselenide with hydrogen peroxide and inhibition of delta-aminolevulinate dehydratase from rat liver and cucumber leaves.

  • M. FarinaN. B. Barbosa J. Rocha
  • Biology, Chemistry
    Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas
  • 2002
TLDR
The results suggest that the interaction of (PhSe)2 with mammal delta-ALA-D requires the presence of cysteinyl residues in close proximity, and the formation of seleninic acid as a product of this reaction may increase the toxicity of organic chalcogens such as (Ph Se)2.

Inhibition of hepatic δ-aminolevulinate dehydratase activity induced by mercuric chloride is potentiated by N-acetylcysteine in vitro.

  • R. BrandãoC. W. Nogueira
  • Biology, Chemistry
    Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association
  • 2011

Association between diphenyl diselenide and cadmium chloride attenuates the toxicity of both in tissues of mice in vitro.

Delta-aminolevulinate dehydratase inhibition by phenyl selenoacetylene: effect of reaction with hydrogen peroxide.

TLDR
It is suggested that delta-aminolevulinate dehydratase is a potential molecular target for phenyl selenoacetylene, due to the oxidation of enzyme sulfhydryl groups, and that the monooxygenation of this selenocompound, which in vivo could be possibly mediated by flavin-containing monooxigenases, increases its inhibitory effect.
...

References

SHOWING 1-10 OF 45 REFERENCES

Liver microsome and flavin-containing monooxygenase catalyzed oxidation of organic selenium compounds.

TLDR
Activity measurements by this procedure indicated that the oxidation of dialkyl selenides by rat, guinea pig, or pig liver microsomes was catalyzed primarily by a monooxygenase with the properties of FMO.

Mechanism of renal lead-binding protein reversal of delta-aminolevulinic acid dehydratase inhibition by lead.

  • P. GoeringB. Fowler
  • Biology, Chemistry
    The Journal of pharmacology and experimental therapeutics
  • 1985
TLDR
Addition of semipurified PbBP to liver delta-aminolevulinic acid dehydratase (ALAD) reaction mixtures reverses inhibition of this enzyme by lead and thus provides an explanation for the relative insensitivity of renal ALAD to lead inhibition in vivo and in vitro.

Effect of mercuric chloride intoxication and dimercaprol treatment on delta-aminolevulinate dehydratase from brain, liver and kidney of adult mice.

TLDR
The present data show that dimercaprol did not acts by reactivating mercury-inhibited sulfhydryl-containing ALA-D, and that indeed it may have an inhibitory effect per se depending on the tissue, and suggested that the dimercicaprol-Hg complex may have a more toxic effect on ALa-D activity than Hg2+.

Regulation of lead inhibition of delta-aminolevulinic acid dehydratase by a low molecular weight, high affinity renal lead-binding protein.

  • P. GoeringB. Fowler
  • Biology, Chemistry
    The Journal of pharmacology and experimental therapeutics
  • 1984
TLDR
Kinetic analysis of either hepatic or renal ALAD activity at an IC50 concentration of Pb indicated a noncompetitive inhibition pattern, and if inhibition of hepatic ALAD by Pb could be reversed by addition of partially purified PbBP from kidney to liver cytosol.

Selective inhibition of Zn(2+)-glycerophosphocholine cholinephosphodiesterase by tellurium tetrachloride.

TLDR
A Zn(2+)-glycerophosphocholine cholinephosphodiesterase is proposed to be one of the target enzymes which is susceptible to the inhibitory effect of tellurium tetrachloride.

Identification of type I iodothyronine 5'-deiodinase as a selenoenzyme.

CAN SELENOAMINO ACIDS ACT AS REVERSIBLE BIOLOGICAL ANTIOXIDANTS *

TLDR
Selenium, long known for its toxic properties, was not recognized to have beneficial effects until the middle of the 20th century, when it was demonstrated that liver necrosis in rats and exudative diathesis in chickens, symptoms characteristic of vitamin E deficiency, could be prevented by small amounts of selenite.

Selenium regulation of hepatic heme metabolism: induction of delta-aminolevulinate synthase and heme oxygenase.

  • M. MainesA. Kappas
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1976
TLDR
The data from this study indicate that excess selenium can substantially inhibit microsomal drug metabolism and may mediate an increase in heme oxygenase through increased production and cellular availability of "free" heme, which results from the increased heme synthetic activity of hematocytes.