Estradiol Receptors in the Uterus

Alberga, Audrey; Jung, Ioan; Massol, Nelly; Raynaud, Jean‐Pierre; Raynaud-Jammet, C.; Rochefort, Henri; H, Truong; Baulieu, Étienne-Émile

doi:10.1016/b978-0-08-017578-2.50008-0

Cited by 6 publications

(6 citation statements)

References 13 publications

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“…In low-salt gradients a loss of about 30 % of the activity in the 4.5 S peak was seen for extracts from oestradiol-treated and nafoxidinetreated chicks (Lazier & Alford, 1976a). No other binding species appear, in contrast with the typical aggregation of the 5 S nuclear uterine oestradiol receptor to an 8-1OS species in low-salt conditico (Alberga et al, 1970).…”

Section: Treatment and Dose (A)mentioning

confidence: 84%

Interaction of the anti-oestrogen, nafoxidine hydrochloride, with the soluble nuclear oestradiol-binding protein in chick liver

Lazier¹,

Alford²

1977

Biochemical Journal

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Nafoxidine hydrochloride (Upjohn, 11100A)injected with oestradiol into immature chicks inhibits the hormone-induced increase in [3H]oestradiol-binding activity in salt extracts of liver nuclei as well as the subsequent production by liver of egg-yolk phosphoprotein. Substantial inhibition of both oestradiol-induced responses is seen when nafoxidine is given in a dose approximately equimolar with that of oestradiol. In vitro nafoxidine competitively inhibits binding of [3H]oestradiol in nuclear extracts. The Ki for the inhibition is 43 nM, which indicates an affinity of nafoxidine for the binding protein about 4% of that of oestradiol. The inhibitory action of nafoxidine in vivo thus is more potent than the relative binding affinity determined in vitro might indicate. One possible explanation is that the primary site of nafoxidine action is at a point proximal to nuclear receptor interaction. Nafoxidine injected alone into the chick does not induce phosphoprotein synthesis, but it does increase [3H]oestradiol-binding activity in extracts of liver nuclei to a limited extent. No differences in the properties of the oestradiol-binding activity in extracts from nafoxidine-treated chicks or from oestradiol-treated chicks were detected. Chick liver cytosol does not contain detectable high-affinity oestradiol-binding activity. A low-affinity oestradiol-binding component with a sedimentation coefficient of 3.5S was found, but it was unaffected by treatment of chicks with earlier nafoxidine or oestradiol. The results suggest a difference in the mechanism of oestradiol action in the chick liver and in the widely studied rat uterus, on which the usual model for oestradiol action is largely based.

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Section: Treatment and Dose (A)mentioning

confidence: 84%

Interaction of the anti-oestrogen, nafoxidine hydrochloride, with the soluble nuclear oestradiol-binding protein in chick liver

Lazier¹,

Alford²

1977

Biochemical Journal

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“…oestradiol complex exhibited two distinct steps. Similarly to the neo-nuclear oestrogen receptor froin rat uterus [34], the chick oviduct nuclear soluble oestrogen receptor exhibits a tendency to form aggregates, possibly involving other nuclear proteins and nucleic acids. They are observed already in the presence of high salt concentration and lead to a complete disappearance of the 4.3-S peak when the sucrose gradient centrifugation is carried out in the absence of salt.…”

Section: ~-~mentioning

confidence: 99%

Oestrogen Receptors in Chick Oviduct

Best‐Belpomme

Mešter

Weintraub

et al. 1975

European Journal of Biochemistry

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Macromolecular components with properties of oestrogen receptors have been identified in the 0.5 M KCI nuclear soluble, the nuclear insoluble and the cytosol fractions of laying hen and immature (2-4 weeks, untreated by hormone) chicken oviduct.In the 0.5 M KC1 extract of laying hen oviduct nuclei, a receptor, of protein nature according to the cffects of enzymic treatments, has been identified. It exhibits high affinity for oestradiol with an apparent equilibrium association constant K, = 4 . lo9 M-' at 4 "C. The binding of [jH] oestradiol 15 abolished by 1 yM oestriol, oestrone and diethylstilboestrol, but not by the same concentration of progesterone, testosterone, and cortisol. Sucrose gradient ultracentrifugation studies in the prc'yc'nce of 0.5 M KCl indicate a sedimentation coefficient of 4.3 S, and there is partial aggregation i n low-ionic-strength medium. The estimated number of binding sites per nucleus is about 5000, as calculated from DNA content of chick diploid genome. Most of the binding sites were found to be occupied by endogenous oestrogen(s). Oestradiol dissociates from the receptor according to an apparent two-step mechanism. The half-life time for the faster dissociation step is 18 h at 0 "C, 25 min at 20 "C and 10 min at 30 "C, and for the slower one is 180 h, 115 min and 60 min, respectively.In the 0.5 M KCl extract of immature chicken oviduct nuclei, there are approximately 500 receptor sites per nucleus; their affinity for oestradiol is the same as in the case of laying hen soluble nuclear receptor.After repeated extractions of nuclei with 0.5 M KC1 medium, a substantial quantity of oestrogen binding sites remains in the residual fraction. Binding characteristics of this insoluble nuclear receptor resemble those of the soluble nuclear receptor: high affinity for oestradiol (KA = 7 . lo* M at 37 "C) and specificity for oestrogens. The estimated number of binding sites are approximately 2000/cell for laying hen, and approximately 1 000/cell for immature chicken.In the high-speed supernatant fraction of laying hen oviduct homogenates, an oestrogen receptor is also present, but its concentration is low (< 100 sites/cell) and at the limits of sensitivity of the methods used.In the cytosol of immature chicken oviduct, there are approximately 2 500 oestradiol receptor sites per cell.

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“…The existence of a distinct nuclear binding protein, present in very small amounts and with a Ka of 10-14 m, has been reported by Alberga et al (1971) who confirm that the 5 S HAR-oestradiol reaction has a a of~10-10 m.…”

mentioning

confidence: 68%

“…The complex sediments at~6 S in the presence of 0-15 m-KCI (Alberga, Jung, Massol, Raynaud, Raynaud-Jammet, Rochefort, Truong & Baulieu, 1971). Centrifugation in the absence of oestradiol followed by recentrifugation of appropriate portions of the gradient in the presence of the hormone shows that the sedimentation coefficient of the HAR itself is similar to that of the complex (Rochefort & Baulieu, 1968).…”

mentioning

confidence: 98%

Steroid Hormones and Their Receptors

Thomas¹

1973

Journal of Endocrinology

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Estradiol Receptors in the Uterus

Cited by 6 publications

References 13 publications

Interaction of the anti-oestrogen, nafoxidine hydrochloride, with the soluble nuclear oestradiol-binding protein in chick liver

Interaction of the anti-oestrogen, nafoxidine hydrochloride, with the soluble nuclear oestradiol-binding protein in chick liver

Oestrogen Receptors in Chick Oviduct

Steroid Hormones and Their Receptors

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