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Glucocorticoid metabolites inhibit the metabolism of androstenedione in red blood cells of ruminants.

The present work aimed to confirm that erythrocytes of ruminants, in general, are capable of converting 17-oxo to 17-hydroxysteroids. Special attention was given to 11-oxoaetiocholanolone (a cortisol metabolite) and its possible interaction with androstenedione as substrates of 17-hydroxysteroid dehydrogenases (17-OH SDH). Blood samples were taken from cattle, sheep and goats (n = 3). Aliquots (100 or 300 microl) of washed red blood cell (RBC) suspensions were incubated in triplicates with Ringer's/glucose solution (1 ml) containing either androstenedione (10 ng) or 11-oxoaetiocholanolone (100 ng) or a mixture of 10 ng of each. Incubations were performed on a shaker at 38 degrees C for 10, 20, 40 or 80 min, respectively. After centrifugation the supernatants were stored at -24 degrees C until analysis. Concentrations of added steroids were measured with enzyme-immunoassays to monitor their decrease. The 17-OH SDH activity of RBC was highest in cattle followed by goats and sheep, and 11-oxoaetiocholanolone was a better substrate than androstenedione. Concentrations of the latter decreased more pronounced, if incubated alone. High performance liquid chromatography separations of the metabolites of 17-oxosteroids revealed the presence of both, a 17beta- and 17alpha-hydroxylated product formed by erythrocytes of sheep and goats, but only the latter in cattle. The results demonstrated that 11-oxoaetiocholanolone was also a substrate of RBC 17-OH SDH and inhibited the metabolism of androstenedione. Therefore, in ruminants, there might be an interaction between cortisol metabolites and gonadal steroids on the level of peripheral steroid metabolism.