Sexual patterns of monooxygenase function in the liver of marine teleosts and the regulation of activity by estradiol
Sexual patterns of monooxygenase function in the liver of marine teleosts and the regulation of activity by estradiol
Date
1988-05
Authors
Gray, Elisabeth S.
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DOI
10.1575/1912/4753
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Keywords
Osteichthyes
Sex differentiation
Sex differentiation
Abstract
Sex differences in hepatic microsomal cytochrome P-450 and monooxygenase
activities were investigated in the marine teleosts scup
(Stenotomus chrysops) and winter flounder (Pseudopleuronectes americanus).
Microsomal cytochrome P-450 content per unit proteln was 3-6
tlmes lower in gonadally mature females than males. Ethoxyresorufin
O-deethylase (EROD) activity in microsomes from females of both
species was less than or equal to activity in males, reflecting
sexually differentiated levels of the responsible isozyme, P-450E.
Estradiol (E2) 2-hydroxylation, demonstrated here for the first time
in teleost microsomes, was measured via 3H20 release from
[2- 3H]E2' Microsomal E2 2-hydroxylase activity in scup was
P-450-mediated, although not by P-450E, and was 2-fold lower per unit
protein in females than in males. Testosterone 6s-hydroxylase and
aminopyrine N-demethylase (APDM) activities in scup were not sexually
differentiated. In winter flounder microsomes, E2 2-hydroxylase,
testosterone 6s-hydroxylase, and APDM activities were all sexually
differentiated. These three activities were decreased 2-3 fold per
unit protein and increased 2-4 fold per unit P-450 in gonadally mature
female winter flounder.
Levels of microsomal P-450E and P-450A were quantified by
immunoblot. Specific P-450E content was lower in females than in
males of both species, but P-450E per nmol P-45O was sexually
differentiated only in winter flounder, where it was decreased in
females. P-450A per unit protein was not sexually differentiated in
either species, and in scup was not differentiated per nmol P-450.
However, in winter flounder P-450A per nmol P-450 was five times
greater in females than in males. Previously, reconstituted scup
P-450A catalyzed both testosterone 6s-hydroxylase and E2
2-hydroxylase activities (Klotz et al., Arch. Biochem. Biophys., 249
(1986): 326). P-450A levels were positlvely correlated to some
extent with these two activities and APDM, suggesting co-regulation
with or catalysis by P-450A.
E2 injections suppressed microsomal monooxygenase activities
and P-450E levels per unit protein in gonadally regressed winter
flounder. Qualitatively, this change was like the decreased
activities in female winter flounder. Other characteristics of the
female-type pattern of monooxygenases were not reproduced by E2
treatment. This suggests that E2 could regulate monooxygenase
activities in gonadally mature female winter flounder, but indicates
that additional factors are also involved. It is speculated that
testosterone or 17a,20S-dihydroxyprogesterone, which are elevated in
plasma of spawning female teleosts, may also be regulatory. In rats
and mice, sex differences in cytochrome P-450 are imparted by
pituitary growth hormone and by the male sex steroid testosterone. In
teleosts, sex differences in hepatic monooxygenases could be effected
by means other than those known to function in mammals.
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Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy at the Massachusetts Institute of Technology and the Woods Hole Oceanographic Institution May 1988
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Citation
Gray, E. S. (1988). Sexual patterns of monooxygenase function in the liver of marine teleosts and the regulation of activity by estradiol [Doctoral thesis, Massachusetts Institute of Technology and Woods Hole Oceanographic Institution]. Woods Hole Open Access Server. https://doi.org/10.1575/1912/4753