Abstract
Gonadotropins have a controlling effect on gonadal steroid hormone production. In vivo investigations on Xenopus laevis and Rana pipiens indicate that increased activity of the steroidogenic enzyme, Δ 5-3 β-hydroxysteroid dehydrogenase (3β-HSD), which results from gonadotropin administration may be oreceded by protein synthesis and may involve a second messenger (cyclic AMP). Incubations of testicular homogenates also respond to gonadotropin treatment with increased 3β-HSD activity. Incubations of testicular microsomal fractions in recombination with either nuclei or mitochondria show that in Rana the stimulation of 3β-HSD due to gonadotropic hormone will occur in the presence of the mitochondrial fraction; growth hormone (STH), thyrotropic hormone (TSH), and ATP do not result in increased activity in this system, and the nuclear fraction also appears to be without effect. Puromycin inhibits the increase in 3β-HSD activity. In the rat, increased 3β-HSD activity due to gonadotropin stimulation occurs if the microsomal fraction is incubated together with the nuclei. Gonadotropin regulation of steroid dehydrogenase activity via the mitochondrial genome is discussed.
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