Opiate receptors are present in the rat testis. Identification and localization in Sertoli cells.

Abstract:

:We have characterized opioid binding sites in the Sertoli cells of adult and 18-day-old rat testes. Maximal specific etorphine binding was attained after 30 min at 4 C. The binding was reversible, with association and dissociation rate constants of 0.98 X 10(5) M-1 min-1 and 0.33 min-1, respectively. Scatchard analyses and saturation curves revealed a single class of high-affinity, low-capacity binding sites. No opioid binding was observed in Leydig cell cultures. Exposure to opioids for 3 days caused a significant increase in [3H]etorphine specifically bound to the Sertoli cells that was completely prevented by naloxone, demonstrating opioid up-regulation of its own receptor. Chronic opioid treatment of the cultures significantly inhibited androgen-binding protein production, and this effect was prevented by naloxone. Since the circulating concentrations of endorphins (10(-12) M) are lower than the Kd of testis opiate receptors, it is conceivable that opioids of Leydig cell origin act on the specific high-affinity receptors of the Sertoli cells, and may play a role in modulating their function.

journal_name

Endocrinology

journal_title

Endocrinology

authors

Fabbri A,Tsai-Morris CH,Luna S,Fraioli F,Dufau ML

doi

10.1210/endo-117-6-2544

subject

Has Abstract

pub_date

1985-12-01 00:00:00

pages

2544-6

issue

6

eissn

0013-7227

issn

1945-7170

journal_volume

117

pub_type

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