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Title: Noncoordinate regulation of de novo synthesis of cytochrome P-450 cholesterol side-chain cleavage and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase in mouse Leydig cell cultures: relation to steroid production

Abstract

The role of cAMP in the regulation of the amount and synthesis of cytochrome P-450 cholesterol side-chain cleavage (P-450scc) and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase P-450(17 alpha) was investigated in mouse Leydig cell cultures. In the absence of cAMP, the amount of immunoreactive P-450(17 alpha) decreased to less than 5% by day 4 and was undetectable between days 7 and 11. In contrast, the amount of immunoreactive P-450scc remained relatively constant throughout the same period. Treatment of Leydig cell cultures for 4 days with 0.05 mM 8-bromo-cAMP initiated on day 7 increased the amount of P-450(17 alpha) with relatively little effect on the amount of P-450scc. The rate of de novo synthesis of each of the P-450 enzymes was studied by determining (35S)methionine incorporation into newly synthesized protein. In the absence of cAMP, de novo synthesis of P-450(17 alpha) ceased while the rate of de novo synthesis of P-450scc increased with time in culture between days 2 and 11. Treatment with cAMP initiated on day 7 of culture caused a time-dependent increase in the rate of de novo synthesis of P-450(17 alpha) on days 9 and 11 equivalent to 40% and 60%, respectively, of that observed in freshly isolated Leydigmore » cells. The rate of de novo synthesis of P-450scc was increased 2-fold relative to untreated cultures on days 9 and 11. De novo synthesis of P-450(17 alpha) ceased when cAMP was removed on day 11 and restored when cAMP was added again on day 13 of culture.« less

Authors:
;  [1]
  1. Univ. of Michigan, Ann Arbor (USA)
Publication Date:
OSTI Identifier:
6073358
Resource Type:
Journal Article
Journal Name:
Molecular Endocrinology; (USA)
Additional Journal Information:
Journal Volume: 1:9; Journal ID: ISSN 0888-8809
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; AMP; BIOLOGICAL FUNCTIONS; LYASES; BIOSYNTHESIS; MIXED-FUNCTION OXIDASES; ANIMAL CELLS; CELL CULTURES; CYTOCHROMES; ELECTROPHORESIS; GENE REGULATION; METHIONINE; MICE; SULFUR 35; TRACER TECHNIQUES; AMINO ACIDS; ANIMALS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBOXYLIC ACIDS; DAYS LIVING RADIOISOTOPES; DRUGS; ENZYMES; EVEN-ODD NUCLEI; FUNCTIONS; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; LIPOTROPIC FACTORS; MAMMALS; NUCLEI; NUCLEOTIDES; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; OXIDOREDUCTASES; OXYGENASES; PIGMENTS; PROTEINS; RADIOISOTOPES; RODENTS; SULFUR ISOTOPES; SYNTHESIS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Anakwe, O O, and Payne, A H. Noncoordinate regulation of de novo synthesis of cytochrome P-450 cholesterol side-chain cleavage and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase in mouse Leydig cell cultures: relation to steroid production. United States: N. p., 1987. Web. doi:10.1210/mend-1-9-595.
Anakwe, O O, & Payne, A H. Noncoordinate regulation of de novo synthesis of cytochrome P-450 cholesterol side-chain cleavage and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase in mouse Leydig cell cultures: relation to steroid production. United States. https://doi.org/10.1210/mend-1-9-595
Anakwe, O O, and Payne, A H. 1987. "Noncoordinate regulation of de novo synthesis of cytochrome P-450 cholesterol side-chain cleavage and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase in mouse Leydig cell cultures: relation to steroid production". United States. https://doi.org/10.1210/mend-1-9-595.
@article{osti_6073358,
title = {Noncoordinate regulation of de novo synthesis of cytochrome P-450 cholesterol side-chain cleavage and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase in mouse Leydig cell cultures: relation to steroid production},
author = {Anakwe, O O and Payne, A H},
abstractNote = {The role of cAMP in the regulation of the amount and synthesis of cytochrome P-450 cholesterol side-chain cleavage (P-450scc) and cytochrome P-450 17 alpha-hydroxylase/C17-20 lyase P-450(17 alpha) was investigated in mouse Leydig cell cultures. In the absence of cAMP, the amount of immunoreactive P-450(17 alpha) decreased to less than 5% by day 4 and was undetectable between days 7 and 11. In contrast, the amount of immunoreactive P-450scc remained relatively constant throughout the same period. Treatment of Leydig cell cultures for 4 days with 0.05 mM 8-bromo-cAMP initiated on day 7 increased the amount of P-450(17 alpha) with relatively little effect on the amount of P-450scc. The rate of de novo synthesis of each of the P-450 enzymes was studied by determining (35S)methionine incorporation into newly synthesized protein. In the absence of cAMP, de novo synthesis of P-450(17 alpha) ceased while the rate of de novo synthesis of P-450scc increased with time in culture between days 2 and 11. Treatment with cAMP initiated on day 7 of culture caused a time-dependent increase in the rate of de novo synthesis of P-450(17 alpha) on days 9 and 11 equivalent to 40% and 60%, respectively, of that observed in freshly isolated Leydig cells. The rate of de novo synthesis of P-450scc was increased 2-fold relative to untreated cultures on days 9 and 11. De novo synthesis of P-450(17 alpha) ceased when cAMP was removed on day 11 and restored when cAMP was added again on day 13 of culture.},
doi = {10.1210/mend-1-9-595},
url = {https://www.osti.gov/biblio/6073358}, journal = {Molecular Endocrinology; (USA)},
issn = {0888-8809},
number = ,
volume = 1:9,
place = {United States},
year = {Tue Sep 01 00:00:00 EDT 1987},
month = {Tue Sep 01 00:00:00 EDT 1987}
}