Summary
Biochemical conditions regulating the 11β-hydroxysteroid dehydrogenase activity in spleen homogenate of mice have been studied. The conversion of 11-hydroxy- to 11-dehydrosteroids is a reversible reaction. The ratio of these compounds at equilibrium and the reaction rates depend on the pH and on the proportion between NADP and NADPH (or NAD and NADH) in the incubation medium. Although having identical maximal reaction velocities, the conversion rate below this maximal concentration is much greater for corticosterone than for cortisol or allotetrahydrocortisol.
Similar content being viewed by others
References
Bush, I., and V. Mahesh: Metabolism of 11-oxygenated steroids. I. Influence of the A/B ring junction on the reduction of 11-oxygroups. Biochem. J. 71, 705–717 (1959).
Deckx, R., K. Delaere, W. Heyns, and P. de Moor: A modified chromatographic system of the Bush type suitable for the resolution of cortisol metabolites. Clin. chim. Acta 9, 69–72 (1964).
——, and J. Raus: Effect of adrenalectomy, sham operation or ACTH on the cortisol metabolizing enzymes of rat liver homogenate. Metabolism 14, 264–270 (1965).
Dougherty, F., M. Berliner, and D. Berliner: 11β-Hydroxy dehydrogenase system activity in thymi of mice following prolonged cortisol treatment. Endocrinology 66, 550–558 (1960).
——, and M. Berliner: Corticosteroid-tissue interactions. Metabolism 10, 966–984 (1961).
Duve, C. de, B. Pressmann, R. Giawetto, R. Wattiaux, and F. Appelmans: Tissue fractionation studies. I. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 60, 604–617 (1955).
Eberlein, W., and A. Bongiovanni: New solvent systems for the resolution of corticosteroids by paperchromatography. Arch. Biochem. 59, 90–96 (1955).
Handler, P., and J. Klein: The inactivation of pyridine nucleotides by animal tissues in vitro. J. biol. Chem. 143, 49–57 (1942).
Hurlock, B., and P. Talalay: Microsomal 3α- and 11β-hydroxysteroid dehydrogenases. Arch. Biochem. 80, 468–470 (1959).
Katz, S.: The location and tentative identification of steroids on paper chromatograms by means of a system of color tests. Arch. Biochem. 91, 54–60 (1960).
——, and J. Broich: A new paper chromatographic system for the resolution of 17-ketosteroids. J. Chromatogr. 6, 514–517 (1961).
Klingenberg, M.: In Bergmeyer, H. (ed.): Methods of enzymatic analysis, p. 535. New York: Academic Press.
Koerner, O., and L. Hellman: Effect of thyroxine administration on the 11β-hydroxysteroid dehydrogenase in rat liver and kidney. Endocrinology 75, 592–601 (1964).
Mahesh, V.: In vitro metabolism of steroids in rat kidney. Fed. Proc. 20, 174 [1961).
——, and F. Ulrich: Metabolism of cortisol and cortisone by various tissues and subcellular particles. J. biol. Chem. 235, 356–360 (1960).
Moor, P. de, and O. Steeno: Influence of synthetic steroids with anabolic and progestational activity on the specific binding of cortisol. J. Endocr. 32, 123–124 (1965).
Osinski, P.: Steroid 11β-ol dehydrogenase in human placenta. Nature (Lond.) 187, 777 (1960).
Samuels, L.: In Greenberg, O. (ed.): Metabolic Pathways, Vol. I, p. 467. New York: Academic Press 1960.
Windmueller, H., and N. Kaplan: Solubilization and purification of diphosphopyridine nucleotidase from pig brain. Biochem. biophys. Acta (Amst.) 56, 388–391 (1962).
Author information
Authors and Affiliations
Additional information
The following abbreviations were used: allotetrahydrocortisol (or 5 α-H4F): 3α, 11β, 17α, 21-tetrahydroxy-5α-pregnan-20-one; 11-dehydrocorticosterone (or A): 21-hydroxypregn-4-ene-3,11,20-trione.
Supported in part by grant no 449 of the “National Fonds voor Geneeskundig Wetenschappelijk Onderzoek”.
Rights and permissions
About this article
Cite this article
Deckx, R., de Moor, P. Study of the 11 β-hydroxysteroid dehydrogenase in vitro. Pflügers Arch. 289, 59–68 (1966). https://doi.org/10.1007/BF00417644
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00417644