Distribution of progesterone-binding cytochrome P450 and steroid-17 alpha-hydroxylase/C-17,20-lyase within different compartments of the rat testis.
Progesterone-binding capacity of cytochrome P450 and rate of progesterone consumption by cytochrome P450-dependent hydroxylases are highest in the Leydig cell fraction but are also detectable in the non-Leydig cell fraction of interstitial cells as well as in seminiferous tubules from rat testis. The Leydig cell compartment, however, contributes only to a minor extent to the total progesterone binding and hydroxylation within the whole testis.
D000446:Aldehyde-Lyases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D007985:Leydig Cells / Q000378:metabolism; D008297:Male; D008861:Microsomes / Q000378:metabolism; D011374:Progesterone / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012671:Seminiferous Tubules / Q000378:metabolism; D013254:Steroid 17-alpha-Hydroxylase / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000378:metabolism*; D013737:Testis / Q000378:metabolism*
D011374:Progesterone; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D013254:Steroid 17-alpha-Hydroxylase; D000446:Aldehyde-Lyases