Abstract
GONADOTROPHIN receptor sites with high specificity and affinity for luteinizing hormone (LH) and human chorionic gonadotrophin (HCG) have been demonstrated in particulate and soluble interstitial cell fractions of rat testis1–4. Such hormone binding sites have been used in radioligand receptor assays for LH and HCG1,2, and in studies on the structural determinants of gonadotrophin binding to target tissue5–7. Other parameters of gonadotrophin action have been examined during incubation of intact rat testes with HCG by radioimmunoassay of the cyclic AMP and testosterone produced during trophic hormone stimulation in vitro8–11. Decapsulated intact rat testes are highly sensitive to gonadotrophic stimulation in vitro, responding to HCG concentrations as low as 0.1 ng ml−1 (10−12 M) with synthesis and release of testosterone and to higher concentrations with synthesis and release of cyclic AMP10. Release of cyclic AMP during incubation with HCG has been shown to reflect cyclic AMP synthesis by simultaneous measurement of 14C-adenine incorporation and radioimmunoassay of cyclic AMP9,10.
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CATT, K., DUFAU, M. Spare Gonadotrophin Receptors in Rat Testis. Nature New Biology 244, 219–221 (1973). https://doi.org/10.1038/newbio244219a0
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DOI: https://doi.org/10.1038/newbio244219a0
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