Androgen-dependence of ornithine decarboxylase in the rat epididymis
Ornithine decarboxylase (ODC) activity was measured in epididymides of 45-day-old rats. Higher ODC activity was detected in the corpus and cauda than in the caput epididymidis. Bilateral castration for 7 days caused epididymal ODC to fall to undetectable values, whereas testosterone restored activit...
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1987
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v79_n1_p9_DeLasHeras http://hdl.handle.net/20.500.12110/paper_00224251_v79_n1_p9_DeLasHeras |
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paper:paper_00224251_v79_n1_p9_DeLasHeras2023-06-08T14:50:53Z Androgen-dependence of ornithine decarboxylase in the rat epididymis androgen cyproterone acetate ornithine decarboxylase testosterone animal cell castration endocrine system epididymis male genital system nonhuman priority journal rat Animalia Caput Ornithine decarboxylase (ODC) activity was measured in epididymides of 45-day-old rats. Higher ODC activity was detected in the corpus and cauda than in the caput epididymidis. Bilateral castration for 7 days caused epididymal ODC to fall to undetectable values, whereas testosterone restored activity to normal values. The effect of the androgen was significantly inhibited by cyproterone acetate. The caput was more sensitive to the action of testosterone than were the corpus and caudal segments. Unilateral castration for 4 or 8 days did not affect ODC on the control or castrated side, but the activity fell in epididymides of both sides after removal of the remaining testis. These results show that epididymal ODC activity is androgen-dependent. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v79_n1_p9_DeLasHeras http://hdl.handle.net/20.500.12110/paper_00224251_v79_n1_p9_DeLasHeras |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
androgen cyproterone acetate ornithine decarboxylase testosterone animal cell castration endocrine system epididymis male genital system nonhuman priority journal rat Animalia Caput |
spellingShingle |
androgen cyproterone acetate ornithine decarboxylase testosterone animal cell castration endocrine system epididymis male genital system nonhuman priority journal rat Animalia Caput Androgen-dependence of ornithine decarboxylase in the rat epididymis |
topic_facet |
androgen cyproterone acetate ornithine decarboxylase testosterone animal cell castration endocrine system epididymis male genital system nonhuman priority journal rat Animalia Caput |
description |
Ornithine decarboxylase (ODC) activity was measured in epididymides of 45-day-old rats. Higher ODC activity was detected in the corpus and cauda than in the caput epididymidis. Bilateral castration for 7 days caused epididymal ODC to fall to undetectable values, whereas testosterone restored activity to normal values. The effect of the androgen was significantly inhibited by cyproterone acetate. The caput was more sensitive to the action of testosterone than were the corpus and caudal segments. Unilateral castration for 4 or 8 days did not affect ODC on the control or castrated side, but the activity fell in epididymides of both sides after removal of the remaining testis. These results show that epididymal ODC activity is androgen-dependent. |
title |
Androgen-dependence of ornithine decarboxylase in the rat epididymis |
title_short |
Androgen-dependence of ornithine decarboxylase in the rat epididymis |
title_full |
Androgen-dependence of ornithine decarboxylase in the rat epididymis |
title_fullStr |
Androgen-dependence of ornithine decarboxylase in the rat epididymis |
title_full_unstemmed |
Androgen-dependence of ornithine decarboxylase in the rat epididymis |
title_sort |
androgen-dependence of ornithine decarboxylase in the rat epididymis |
publishDate |
1987 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224251_v79_n1_p9_DeLasHeras http://hdl.handle.net/20.500.12110/paper_00224251_v79_n1_p9_DeLasHeras |
_version_ |
1768545082852507648 |