Formation and metabolism of progesterone by the mouse placenta in vitro

Rembiesa, R; Marchut, M; Warchol, Amella

doi:10.1016/0022-4731(71)90049-5

Cited by 17 publications

(3 citation statements)

References 12 publications

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“…Additionally, incubation of placentae obtained on day 10 with 1 µ [7-3H]pregnenolone/ml Ci/mmol; New England Nuclear) followed by extraction of the media with 10 vol. diethyl ether and thin-layer chromatography with the above solvent systems provided further evidence for the synthesis of androgen and progesterone by the mouse placenta as previously reported (Rembiesa et al 1971;Okker-Reitsma, 1972, 1976Salomon & Sherman, 1975). Preliminary experiments indicated that it was not necessary to extract incubation media before assaying for androgen and progesterone.…”

Section: Animalssupporting

confidence: 57%

“…Studies on placental function in the mouse have demonstrated the presence of steroid enzymatic activity (Deane, Rubin, Driks, Lobel & Leipsner, 1962;Vinson & Jones, 1964;Chew & Sherman, 1975), in-vitro synthesis and release of progesterone and androgens (Rembiesa, Marchut & Warchol, 1971;Okker-Reitsma, 1972, 1976Salomon & Sherman, 1975;OkkerReitsma & Wilson, 1980) and the presence of a prolactin-like hormone (Cerruti & Lyons, 1960;Kohmoto & Bern, 1970;Talamantes, 1975; Kelly, Tsushima, Shiu & Friesen, 1976). The relationships between patterns of serum steroid and prolactin-like hormone activity and the in-vitro placental secretion profiles of these hormones have not been described in the mouse.…”

Section: Introductionmentioning

confidence: 97%

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Gestational effects on placental and serum androgen, progesterone and prolactin-like activity in the mouse

Soares¹,

Talamantes²

1982

Journal of Endocrinology

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The concentrations of androgen, progesterone and prolactin-like activity in serum, placentae and media from placental incubations during the second half of pregnancy in the C3H mouse were evaluated. Serum concentrations, placental content and in-vitro placental release of androgen were raised on day 10 of pregnancy. Serum progesterone levels showed minor fluctuations during the second half of gestation, whereas placenta content and in-vitro release of progesterone were increased on day 10 of gestation. The serum profile of prolactin-like activity showed a significant mid-pregnancy increase on day 10 which did not correlate with placental content or in-vitro placental release of prolactin-like activity. The placental content and in-vitro release of prolactin-like activity were low during mid-pregnancy and increased during the latter days of gestation when serum prolactin-like activity was reduced.

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Section: Animalssupporting

confidence: 57%

Section: Introductionmentioning

confidence: 97%

Gestational effects on placental and serum androgen, progesterone and prolactin-like activity in the mouse

Soares¹,

Talamantes²

1982

Journal of Endocrinology

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“…This is consonant with differences in the physiological functions of human and mouse placentae. While human placenta plays a prominent role in producing progesterone and estrogens, mouse placenta is not able to synthesize estrogen as a result of a lack of aromatase activity (Rembiesa et al, 1971 ;Vinson and Chester-Jones, 1964). Instead, mouse placenta produces androgens, androstenedione and testosterone, which are essential precursors for estrogen synthesis in the ovaries of pregnant inice (Soares and Talamantes, 1983) and, consequently, for the maintenance of pregnancy.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning of Mouse 17β‐Hydroxysteroid Dehydrogenase Type 1 and Characterization of Enzyme Activity

Nokelainen

Puranen

Peltoketo

et al. 1996

European Journal of Biochemistry

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The biological activity of certain estrogens and androgens is modulated by enzymes called 17p-hydroxysteroid dehydrogenases (I~P-HSDS), which catalyze the interconversion between less active 17-oxosteroid and more active 17P-hydroxysteroid forms. In the present report, we describe cloning of mouse 17P-HSD type-I cDNA from an ovarian library generated from 4,4'-( 1,2-diethyl-I ,2-ethenediyl)bisphenol-(diethylstiIbestro1)-treated mice, and characterization of the corresponding enzyme. The open reading frame of the mouse 17P-HSD type-1 cDNA encodes a peptide of 344 amino acid residues with a predicted molecular mass of 3678.5 Da. The mouse 17P-HSD type-1 enzyme shares 63 % and 93 % overall identity with human and rat 17P-HSD type-I enzymes, respectively, and the most striking differences between the mouse and human type-1 enzymes are between the amino acid residues 197 and 230 and in the carboxy terminus of the enzymes. Similarly to the human 17P-HSD type-I enzyme, the mouse type-I enzyme primarily catalyzes reductive reactions from 17-0x0 forms to 17P-hydroxy forms in intact cultured cells, but unlike the human type-I enzyme, the mouse enzyme does not prefer phenolic over neutral substrates. Thus, mouse 17P-HSD type 1 catalyzes reduction of androst-4-ene-3,17-dione (androstenedione) to 17P-hydroxyandrost-4-en-3-one (testosterone) as efficiently as 3P-hydroxyestra-l,3,.5(10)-trien-17-one (estrone) to estra-1,3,5(10)-triene-3~,17~-diol (estradiol). 17P-HSD type 1 is predominantly expressed in mouse ovaries, in which it is located in granulosa cells.Keywords: 17-hydroxysteroid dehydrogenases ; cloning ; mouse; estrogen ; B1 repetitive sequence.17P-Hydroxysteroid dehydrogenases (17p-HSDs) catalyze the conversion of neutral and phenolic 17-oxosteroids to 17P-hydroxysteroids and vice versa. Both androgens and estrogens are biologically more active in their l7P-hydroxy configurations, such as 17P-hydroxyandrost-4-en-3-one (testosterone) and estra-1,3,S(10)-triene-3~,17~-diol (estradiol), than in their 17-0x0 configuration. Thus, 17P-HSDs, along with other steroidogenic enzymes such as 3P-hydroxysteroid dehydrogenases and Sa-reductases, modulate the biological activity of the sex steroids.

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