Conversion of progesterone to deoxycorticosterone in guinea pig spleen: an animal model for the study of steroid 21-hydroxylase activity in extra adrenal sites.
Steroid 21-hydroxylase activity has been demonstrated, previously, in microsome-enriched fractions prepared from a number of human fetal tissues. The finding that this enzyme activity was present in thymus and spleen is suggestive of the possibility that deoxycorticosterone is important in regulation of immunological processes. In the present investigation, we characterized steroid 21-hydroxylase activity in microsome-enriched preparations of guinea pig spleen. The activity of the enzyme was linear with time for 40 min and with protein concentrations up to 4.8 mg X ml-1 incubation mixture. The apparent Km of the enzyme for progesterone was 0.405 microM. Thus, the potential exists for the biosynthesis of DOC from progesterone in the spleen of the guinea pig as well as in the spleen of the human fetus. Therefore, the guinea pig may be an appropriate animal model for the study of the regulation of steroid 21-hydroxylase activity in the spleen as well as a model for the study of the role of this enzyme in immunologic processes.
D000818:Animals; D003900:Desoxycorticosterone / Q000096:biosynthesis*; D005260:Female; D006168:Guinea Pigs; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D011374:Progesterone / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology*; D013255:Steroid 21-Hydroxylase / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000378:metabolism*; D014316:Tritium
D014316:Tritium; D003900:Desoxycorticosterone; D011374:Progesterone; D013250:Steroid Hydroxylases; D013255:Steroid 21-Hydroxylase