Mechanisms involved in the regulation of steroid receptor levels

Jungblut, P. W.; Hughes, Alun; Gaues, J.; Kallweit, Erhard; Maschler, Itzhak; Parl, Fritz F.; Sierralta, Walter; Szendro, Pablo I.; Wagner, R. K.

doi:10.1016/0022-4731(79)90308-x

Cited by 37 publications

(8 citation statements)

References 19 publications

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“…2b) proves the specificity of the reaction. The rapid disappearance of unbound estradiol was expected from previous fractionation experiments (Jungblut et al 1979). The cell-to-cell differences in estradiol-binding capacities of the glandular epithelium, however, were surprisingly extensive.…”

Section: Estradiol In Porcine Endometrium After Intraluminal Administsupporting

confidence: 62%

Identification of target cells by immunohistochemical detection of covalently rearranged estradiol in rehydrated paraffin sections

Jungblut

Sierralta

1998

Histochemistry and Cell Biology

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Section: Estradiol In Porcine Endometrium After Intraluminal Administsupporting

confidence: 62%

Identification of target cells by immunohistochemical detection of covalently rearranged estradiol in rehydrated paraffin sections

Jungblut

Sierralta

1998

Histochemistry and Cell Biology

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“…Differences observed in replenishment after the administration of dexamethasone and predonisolone were possibly due to the difference in the rate of cellular metabolism and the clearance of these steroids. As to the mechanism of receptor replenishment, new receptor synthesis was mainly attributed by Jungblut et al (1979) and by Mester and Baulieu (1975) in the estrogen receptor of rat uterus, while main role of cycling of the translocated receptor to the cytoplasm was postulated by Ishii et al (1972) and Aronow (1978) in the glucocorticoid receptor of cultured fibroblast. In the present study, the pattern of receptor depletion and replenishment after the administration of predonisolone was not modified by concomitant administration of cycloheximide in a dose where more than 95% of protein synthesis was inhibited.…”

Section: Discussionmentioning

confidence: 99%

Depletion and replenishment of glucocorticoid receptor in cytosols of rat tissues after administration of various glucocorticoids.

Ichii

1981

Endocrinol Japon

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Administration of steroid hormones evokes a rapid fall in the amount of cytoplasmic receptors in target tissues. This has been considered to be a consequence of the receptor translocation to nuclei, but the physiological significance of depletion of the cytoplasmic receptors after hormone administration has not been fully elucidated. In the present study, depletion and replenishment of the cytoplasmic glucocorticoid receptor in rat tissues were examined after the administration of glucocorticoids of different biological potencies. Dose dependent depletion was observed in all tissues examined and doses required for complete depletion of the receptor were correlated with biological potencies of steroid administered. The receptor in the heart and the skeletal muscle was relatively sensitive to hormone injection while more than 4 times the amount of steroids was required to induce a similar effect in the thymus and the spleen. The duration of the period of depletion of the receptor in cytosols was also dose dependent and correlated to the biological potency of steroid administered. Replenishment took place earlier in the thymus and the spleen than in the heart and the skeletal muscle. Significantly lower binding affinity was observed in the replenished receptors. The administration of cycloheximide in a dose which inhibits more than 95% of 3H-leucine incorporation did not influence either the depletion or the replenishment of the receptor induced by hormone injection. In conclusion, depletion and replenishment of the cytoplasmic glucocorticoid receptor appeared to be closely correlated to the physiological action of hormones.

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“…Estradiol is metabolized after nuclear passage in porcine endometrium cells by dehydrogenation to estrone (1,2), and subsequent hydroxylation at either 6a-or 7a- (3). Our previous results sug¬ gested a localization of the 17ß-ol dehydrogenase in organdíes resembling lysosomes in size and density, although the pH optimum of the enzyme was in the neutral range.…”

mentioning

confidence: 91%

Assignment of estradiol-17β dehydrogenase and of estrone reductase to cytoplasmic structures of porcine endometrium cells

Adamski¹,

Sierralta²,

Jungblut³

1989

Acta Endocrinologica

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Homogenates of porcine endometrium contain substantial activity for the dehydrogenation of estradiol-17\g=b\ but little for estrone reduction. Both activities are associated with cytoplasmic structures. The dehydrogenase is characterized by a pH 7.7 optimum, Km 2.2 \m=x\ 10\m=-\7 mol/l for estradiol and Km 4.4 \m=x\10\m=-\5mol/l for the cosubstrate NAD+. The corresponding figures for the reductase are pH 6.6, Km 1.1 \m=x\10\m=-\6mol/1 for estrone and Km 2.1 \m=x\10\m=-\5mol/l for the cosubstrate NADPH. The (mitochondrial/lysosomal) 17 000 \m=x\ g particulate fraction contains a 52-fold higher dehydrogenase than reductase activity. The (microsomal) 200 000 \m=x\ g particulate fraction is only 16-fold richer in dehydrogenase. Isopycnic centrifugations of the two fractions in Percoll gradients reveal that estrone reductase and the coequilibrating marker enzyme cytochrome c reductase occur in constant proportions, whereas the dehydrogenase/cytochrome c reductase ratios are different. Both, the kinetic data and the structural assignments speak in favour of individual enzymes catalyzing the dehydrogenation of estradiol and the reduction of estrone. All gradient fractions exhibiting dehydrogenase activity feature small, electrondense vesicles of 0.15\p=n-\0.20\g=m\min diameter as a common structural element which might harbour the dehydrogenase.Estradiol is metabolized after nuclear passage in porcine endometrium cells by dehydrogenation to estrone (1,2), and subsequent hydroxylation at either 6a-or 7a-(3). Our previous results sug¬ gested a localization of the 17ß-ol dehydrogenase in organdíes resembling lysosomes in size and density, although the pH optimum of the enzyme was in the neutral range. We re-investigated this discrepancy by employing novel techniques for homogenization and organeile separation (4). The ex¬ periments were also thought to clarify whether the prevailing oxidation of estradiol to estrone and the less prominent reversal are catalyzed by one and the same enzyme or by individual entities at differ¬ ent localizations. This might help in exploring the mechanism by which the cell terminates the hor¬ monal stimulus. Materials and MethodsThiamine pyrophosphate was bought from Sigma (Mün¬ chen, FRG); NAD+ and NADPH from Boehringer Mann¬ heim (Mannheim, FRG); Percoll from Pharmacia (Frei¬ burg, FRG); Triton X-100 from Serva (Heidelberg, FRG); xylene-based fluor, estrone, estradiol, estriol and all other grade A chemicals were from E.Merck (Darmstadt, FRG). Tritium-labelled steroids [2,4,6,7-3H]estrone,specific activity 95 Ci/mmol and [6,7-3H] estradiol, specific activity 59 Ci/mmol were from New England Nuclear (Dreieich/FRG) and purified before use. Bond Elut RP-18 (100 mg) solid-phase extraction columns were from Analytichem International (Harbor City, CA); reversed-phase columns LiChrosorb RP-18, RT 250-4, 5 um, and guard columns, RT 4-4, 10 um, were from E.Merck; acetonitrile HPLC-grade was bought from Zinsser (Frankfurt, FRG). Milli-Q H20, Millipore (Eschborn, FRG) was used for HPLC.Endometrium was ...

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Mechanisms involved in the regulation of steroid receptor levels

Cited by 37 publications

References 19 publications

Identification of target cells by immunohistochemical detection of covalently rearranged estradiol in rehydrated paraffin sections

Identification of target cells by immunohistochemical detection of covalently rearranged estradiol in rehydrated paraffin sections

Depletion and replenishment of glucocorticoid receptor in cytosols of rat tissues after administration of various glucocorticoids.

Assignment of estradiol-17β dehydrogenase and of estrone reductase to cytoplasmic structures of porcine endometrium cells

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