Uterine Progesterone Metabolism and Progestational Response: Effects of Estrogens and Prolactin

Armstrong, David T.; King, Elizabeth R.

doi:10.1210/endo-89-1-191

Cited by 95 publications

(25 citation statements)

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“…In laboratory animals the circulating levels of oestradiol also influence the uterine metabolism of oestradiol and progesterone in vivo and in vitro (Martin and Stone 1965;Pack and Brooks 1970;Armstrong and King 1971;Clark 1973;Saffron et al 1974;Holtermann and Lisboa 1975). In view of this the generally low level of metabolism of these two steroids, particularly to less active compounds, and the lack of influence of steroid treatment, in the present study, is rather surprising.…”

Section: Discussionmentioning

confidence: 50%

Oestradiol and Progesterone: Soluble Receptor Levels and Metabolism in the Uterus of the Ovariectomized Ewe

Murphy¹,

Stone²,

Miller³

et al. 1977

Aust. Jnl. Of Bio. Sci.

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Ovariectomized ewes received injections designed to mimic to some extent oestradiol and progesterone secretion during early pregnancy (maintenance progesterone), during oestrus (oestrous oestradiol) and during the luteal phase of the previous cycle (priming progesterone). The animals were killed at times equivalent to 1, 4 or 7 days after oestrus in those animals which had received oestrous oestradiol. The level of soluble oestradiol and progesterone receptors in whole uterus, and [3Hloestradiol and [3Hlprogesterone metabolism by uterus minces were measured.Oestradiol receptor level was highest on day 1 in those animals receiving oestrous oestradiol with no significant effect at any stage of the inclusion or omission of priming or maintenance progesterone. Progesterone receptor level was also high on day 1 in those animals receiving oestrous oestradiol with high levels maintained to day 4. Again, inclusion of priming or maintenance progesterone was without effect. In animals not receiving oestrous oestradiol the level of both receptors was uniformly low.Metabolism of [3Hloestradiol was low and not affected by treatment. [3HIProgesterone metabolism, although more variable, was also low and not affected by treatment.

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Section: Discussionmentioning

confidence: 50%

Oestradiol and Progesterone: Soluble Receptor Levels and Metabolism in the Uterus of the Ovariectomized Ewe

Murphy¹,

Stone²,

Miller³

et al. 1977

Aust. Jnl. Of Bio. Sci.

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“…Ovariectomy resulted in a significant (P < 0-05) decrease in the concentration of cytosolic and nuclear progesterone receptors ( (Kennedy & Armstrong, 1972), to accelerate oestradiol binding to uterine tissue (Leung & Sasaki, 1973) and to enhance progesterone metabolism by uterine homogenates (Armstrong & King, 1971). The mechanisms for some of these responses have been presumed to relate to changes in dopamine receptors or gonadotrophinreleasing factors.…”

Section: Resultsmentioning

confidence: 99%

Prolactin as a factor in the uterine response to progesterone in rabbits

Daniel¹,

Jetton²,

Chilton³

1984

Reproduction

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Summary. The direct effect of prolactin on uteroglobin production and on uterine endometrial oestrogen and progesterone receptor concentrations was tested by using ovariectomized rabbits (at least 12 weeks) treated with prolactin; prolactin + progesterone; prolactin + oestradiol + progesterone; oestradiol + progesterone; or progesterone alone. Prolactin treatment produced a significant (P < 0\m=.\05) increase in the concentration of cytosolic oestrogen and progesterone receptors, restoring the concentrations to values found at oestrus. However, the concentration of nuclear receptors remained low. In the remaining treatment categories there was no significant (P > 0\m=.\05) increase in the concentration of oestrogen and progesterone receptors compared with those in ovariectomized controls. However, the sequential treatment of ovariectomized animals with prolactin + progesterone stimulated uteroglobin production to a concentration equal to that found in intact rabbits on the 5th day of pregnancy. This was not achieved by prolactin or progesterone alone or with oestradiol. These results suggest that prolactin acts as an essential factor in the rabbit uterine response to progesterone, perhaps by the modulation of progesterone receptor activity.

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“…It has been suggested that the enzyme is a T-cell differentiation marker (Ihle et al 1981). In addition to being present in thymic-derived lymphocytes, 20 -HSD activity has been found in many steroidogenic tissues such as the liver, ovary, testis, adrenal and placenta (Wiest 1959, Matthijssen et al 1964, Armstrong & King 1971, Pineda et al 1985, Nakajin et al 1989 and also in haemopoietic cells, erythrocytes and certain micro-organisms (Weinstein 1977, Sharaf & Sweet 1982, Hapel et al 1985, Rimsay et al 1988. While 20 -HSD has been shown to play a major role in the termination of pregnancy in the rat and rabbit, the role of 20 -HSD in the human is still ill-defined.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a human 20alpha-hydroxysteroid dehydrogenase

Zhang

Dufort²,

Rheault³

et al. 2000

Journal of Molecular Endocrinology

100

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It has been suggested that 20 -hydroxysteroid dehydrogenase (20 -HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17 -HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20 -HSDs are members of the aldoketo reductase superfamily, which also includes the 3 -HSD family. In this study, we report the cloning, from a human skin cDNA library, of a cDNA that shows, after transfection into human embryonic kidney (HEK-293) cells, high 20 -HSD activity but negligible 3 -and 17 -hydroxysteroid dehydrogenase activities. A comparison of the amino acid sequence of the human 20 -HSD with those of other related 20 -and 3 -HSDs indicates that the human 20 -HSD shares 79·9, 68·7 and 52·3% identity with rabbit, rat and bovine 20 -HSDs, whereas it shows 97, 84 and 65% identity with human type 3, type 1 and rat 3 -HSDs. In contrast, the enzyme shares only 15·2 and 15·0% identity with type 1 and type 2 human 17 -HSDs. DNA analysis predicts a protein of 323 amino acids, with a calculated molecular weight of 36 767 Da. In intact transfected cells, the human 20 -HSD preferentially catalyzes the reduction of progesterone to 20 -hydroxyprogesterone with a K m value of 0·6 µM, the reverse reaction (oxidation) being negligible. In a cell cytosolic preparation, the enzyme could use both NADPH and NADH as cofactors, but NADPH, which gave 4-fold lower K m values, was preferred. We detected the expression of 20 -HSD mRNA in liver, prostate, testis, adrenal, brain, uterus and mammary-gland tissues and in human keratinocyte (HaCaT) cells. The present study clearly indicates that the genuine human 20 -HSD belongs to the aldoketo reductase family, like the 20 -HSDs from other species.

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Uterine Progesterone Metabolism and Progestational Response: Effects of Estrogens and Prolactin

Cited by 95 publications

References 0 publications

Oestradiol and Progesterone: Soluble Receptor Levels and Metabolism in the Uterus of the Ovariectomized Ewe

Oestradiol and Progesterone: Soluble Receptor Levels and Metabolism in the Uterus of the Ovariectomized Ewe

Prolactin as a factor in the uterine response to progesterone in rabbits

Characterization of a human 20alpha-hydroxysteroid dehydrogenase

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