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Specific Progesterone Receptors in the Hypothalamus and Anterior Hypophysis of the Rat^*

Department of Obstetrics and Gynecology, Teikyo University School of Medicine Kaga, Itabashi, Tokyo, 173 Japan

Abstract

Progesterone-binding components were detected in hypothalamic and anterior hypophysial cytosols from estrogen-primed immature and mature female rats. These components were labeled in vitro with a tritiated synthetic progestin, R5020, which binds specifically to progesterone receptors. The radioactive complex sediments in the 7S region in sucrose density gradients containing 10% glycerol. Little 7S binding was detected in similar preparations from the cerebral cortex, amygdala or reticular formation. In contrast with the marked effects by the estrogen-priming, very low or no 7S binding was found in the hypothalamus and hypophysis from intact nonprimed immature female rats.

The dissociation constants (Kd) and the number of binding sites (NBS) of the hypothalamic components in immature rats were 3.3 x 10^–9M and 1.0 x 10^–14 moles\mg cytosol protein, respectively. These values for the adult rat anterior hypophysis were 3.8 x 10^–9M and 3.1 x 10^–14 moles/mg cytosol protein, respectively. The 7S binding components in the hypothalamus and hypophysis were specific for progestational compounds. It is noteworthy that 5β-dihydroprogesterone greatly lowered the 7S binding in both the tissues, but its 5\3-isomer was without effect. Among steroid competitors tested, only estradiol competed weakly. Incubation with pronase abolished the 7S R5020 binding. Heat experiments revealed the thermolabile nature of the components. In addition to the 7S binding component, a 4S complex of bound R5020 was evident in the hypothalamus and cerebral cortex but not in the hypophysis. This binding seemed to be mostly nonspecific in nature. We conclude from these results that the cytosols from the hypothalamus and anterior hypophysis of estrogen-primed female rats contain specific progesterone receptors.

Footnotes

^* A preliminary report of this study was presented at the 3rd International of the J. Steroid Biochemistry, Helsinki, Finland, June 1976, and the Vth International Congress of Endocrinology, Hamburg, Germany, July, 1976. Supported in part by an Aid in Research from The Ministry of Education, Culture and Art, and by a grant from The Naito Research Foundation, Tokyo.

Received August 30, 1976.

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