Immunocytochemical study on the mechanism of steroid hormone biosynthesis.

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1.(1) Electron microscopic immunocytochemistry using specific antisera revealed that 3 beta-hydroxysteroid dehydrogenase is present on the membranes of smooth endoplasmic reticulum of the bovine adrenocortical cells. This result indicate that the conversion of pregnenolone to progesterone occurs on the smooth endoplasmic reticulum of the adrenocortical cells. (2) Electron microscopic immunocytochemistry revealed that ATP synthase is present on the inner mitochondrial membranes.2. Light microscopic immunocytochemistry demonstrated that aromatase (estrogen synthesizing enzyme) is present in the granulosa cells of preovulatory large follicles and in the some cells of corpus luteum, and that 17 betahydroxysteroid dehydrogenase which converts androstenedione to testosterone is present in the cells of theca interna and interstitial glands.3. Cytochrome p-450 which is involved in the detoxication of some chemical compounds could be localized immunocyotchemically in the steroid-secreting cells of the ovary and testis of 3-methylcholanthrene-treated mice.4. Calspectin which undercoats the plasma membrane is shown immunocytochemically at the baso-lateral plasma membrane of thyroid follicle epithelial cells of normal rats. In the follicle epithelial cells of TSH-treated rats, calspectin is demonstrated at the apical plasma membrane in addtion to the baso-lateral plasma membrane.5. Aromatage (estrogen synthesizing enzyme) is demonstrated in the corpus luteum cells of pregnant rats. This result indicate that the corpus luteum cells of the pregnant rats may have the capacity of estrogen synthesis.