The selective inhibition by metopirone of 11β-hydroxylation in bovine adrenal perfusion of progesterone1

Levy, Harold; Hwa, Chung; Carlo, James J.

doi:10.1016/0039-128x(65)90142-x

Cited by 8 publications

(2 citation statements)

References 4 publications

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“…Each of these enzymes is located in mitochondria and the results of several early studies suggested that adrenal microsomal hydroxylases were not affected by metyrapone. Neither 21-hydroxylase nor 17a-hydroxylase activity was inhibited by metyrapone in rat or bovine adrenals (8,9). However, the specificity of the actions of metyrapone appears to be species-dependent (10).…”

Section: April 1981mentioning

confidence: 99%

Chemical suppression of steroidogenesis.

Colby¹

1981

Environ Health Perspect

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A large number of chemicals are known to interfere with steroidogenesis in the adrenal cortex and other tissues. Many xenobiotics inhibit steroid hormone production as a result of interactions with cytochrome P-450-containing hydroxylases in adrenal mitochondria or microsomes. For example, metyrapone, a compound used clinically in the evaluation of pituitary-adrenocortical function, binds to various cytochromes P-450 in the adrenal, preventing the interactions of steroid substrates with the enzymes and inhibiting steroidogenesis. The mineralocorticoid antagonist, spironolactone, and its major circulating metabolite, canrenone, also competitively interact with adrenal steroid hydroxylases. In addition, spironolactone is converted by adrenal microsomes to an unknown metabolite which promotes the destruction of cytochromes P-450, decreasing the activities of steroid hydroxylases. Carbon tetrachloride is similarly "activated" by adrenal microsomal mixed function oxidases resulting in a decline in steroidogenic enzyme activity. Carbon tetrachloride (in the presence of NADPH) initiates lipid peroxidation in adrenal microsomes but its toxic effects on steroid hydroxylases are fully demonstrable when lipid peroxidation is inhibited by EDTA. A number of heavy metals, including cadmium, also inhibit adrenal steroid hydroxylases. When incubated with adrenal microsomes, cadmium does not affect cytochrome P-450 levels but decreases basal and substrate stimulated NADPH-cytochrome P-450 reductase activity. Although inhibitory effects of many chemicals on steroidogenesis have been described, the toxicological significance as well as definitive mechanisms of action have in most cases yet to be determined.

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Section: April 1981mentioning

confidence: 99%

Chemical suppression of steroidogenesis.

Colby¹

1981

Environ Health Perspect

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“…Neither 21-hydroxylase nor 17ot-hydroxylase activity was inhibited by metyrapone in rat or bovine adrenals (8,9). Each of these enzymes is located in mitochondria and the results of several early studies suggested that adrenal microsomal hydroxylases were not affected by metyrapone.…”

mentioning

confidence: 97%

Chemical Suppression of Steroidogenesis

Colby¹

1981

Environmental Health Perspectives

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Über die adrenale Steroid‐Biosynthese in vitro. III. Selektive Hemmung der Nebennierenrinden‐Funktion

Kahnt

Neher

1966

Helvetica Chimica Acta

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Volumen 49, Fasciculus 1 (1966) -No. 82-83 725 azides with an hexapeptide. The two latter have been obtained from the hexapeptide by the recurring method, using active trichlorophenyl esters.Comparison of the biological activities of these compounds with those of the corresponding analogues still bearing the a-amino group shows that suppression of this amino group decreases the pressoric/antidiuretic ratio of these compounds.Laboratoires de Chimie pharmaceutique SANDOZ S. A., BAle BIBLIOGRAPHIE

show abstract

The selective inhibition by metopirone of 11β-hydroxylation in bovine adrenal perfusion of progesterone1

Cited by 8 publications

References 4 publications

Chemical suppression of steroidogenesis.

Chemical suppression of steroidogenesis.

Chemical Suppression of Steroidogenesis

Über die adrenale Steroid‐Biosynthese in vitro. III. Selektive Hemmung der Nebennierenrinden‐Funktion

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