Specific estrogen receptors in the lactating mammary gland of the rat

Gardner, David G.; Wittliff, James L.

doi:10.1021/bi00740a023

Cited by 53 publications

(14 citation statements)

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“…Since the demonstration that the mammary gland of C3H-strain mice binds oestradiol-17,8 in vivo with high affinity (Bresciani & Puca, 1965; Puca & Bresciani, 1969), specific receptors for oestrogen have been shown to exist in the mammary gland of mice (Shyamala & Nandi, 1972;Auricchio et al, 1976) and rats (Gardner & Wittliff, 1973). In normal human breast, oestrogen receptors are barely detectable (Hanel & Twaddle, 1973).…”

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confidence: 99%

“…Mostly, mammary oestrogen receptor has been studied by sucrose-gradient centrifugation. Mammary receptor from both mouse and rat glands sediments at 8-1OS at low-salt concentrations (10mm) and at about 4S when 0.4 M-KCl is present (Shyamala & Nandi, 1972;Gardner & Wittliff, 1973;Auricchio et al, 1976). Also, after injection in vivo of [3H]oestradiol-17,8, a radioactive receptor-oestradiol complex of approx.…”

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confidence: 99%

“…Also, after injection in vivo of [3H]oestradiol-17,8, a radioactive receptor-oestradiol complex of approx. 4-5S can be extracted from the nuclear pellet of glands from pregnant and lactating mice (Gardner & Wittliff, 1973). From studies with chelating agents, it has been suggested that the mammary oestrogen receptor is a metalloprotein (Shyamala, 1975).…”

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Oestrogen receptor of mammary gland. Inhibition of aggregation and characterization of receptor from lactating gland in the presence of sodium bromide

Auricchio

Rotondi

Schiavone

et al. 1978

Biochemical Journal

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1. When NaBr, a chaotropic salt, is added, in concentrations ranging from 0.5M to 2M, to low-salt mammary cytosol, (i) age-dependent aggregation of oestrogen receptor is inhibited, (ii) the receptor sediments as a sharp peak at 4.2S on sucrose-gradient centrifugation, with complete disappearance of heavier forms, and (iii) on gel filtration with Sephadex G-200, the receptor is included in the gel matrix. On a calibrated column, the receptor has a Stokes radius of 3.7 nm (±6%). 2. Because NaBr inhibits interaction of receptor with other components of cytosol, the values of the sedimentation coefficient, measured by sucrose-gradient sedimentation, and of the Stokes radius, measured by gel filtration, can be accepted with confidence. From these values, it can be computed that the oestrogen-receptor form in NaBr has a mol.wt. of 64000, with a frictional ratio of 1.4. 3. Also, inhibition of aggregation by NaBr allows a 30-90-fold purification of oestrogen receptor. Analysis of this partially purified receptor by sucrose-gradient sedimentation and gel filtration in NaBr gives the same results as for receptor in crude cytosol. On electrofocusing on a pH5-8 gradient, the partially purified oestrogen receptor focuses at pH6.2. On removal of NaBr, receptor aggregates even in this partially purified state. It seems likely that at the protein and ionic concentrations of cytoplasm in vivo, the 64000-mol.wt. receptor form is part of higher states of self-and/or hetero-association with other cytoplasmic components. 4. NaBr up to a concentration of 2M does not inhibit binding of oestrogen by receptor, nor does it decrease the affinity of the interaction (KD 8.9 x10-1OM). The total number of binding sites in cytosol, however, decreases by approx. 10 %, but this decrease may actually be the result of elimination of lower-affinity binding by non-receptor components of cytosol. 5. NaSCN, another chaotropic salt, was also tested but gave less satisfactory results with the mammary cytosol than with uterine cytosol. EDTA was omitted from the buffers because it favours aggregation of mammary oestrogen receptor. KCl (0.4M), sucrose (15%) and ZnSO4 (3mM) did not prevent aggregation of receptor.Since the demonstration that the mammary gland of C3H-strain mice binds oestradiol-17,8 in vivo with high affinity (Bresciani & Puca,

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Oestrogen receptor of mammary gland. Inhibition of aggregation and characterization of receptor from lactating gland in the presence of sodium bromide

Auricchio

Rotondi

Schiavone

et al. 1978

Biochemical Journal

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“…In our experiments receptor could be extracted from mammary nuclei of MMTV-bearing mice and sedimented in the 5S region as does the classical rat uterine nuclear receptor [17], Whether nuclear uptake might become defective during the process of malignant transforma tion in mouse mammary awaits further study. Previous reports on the characteristics of cytosol estrogen receptor in rodent lactating mammary tissues indicated that it sediments near 8-9S for the Fischer rat [18], vole [19] and BALB/c mouse [14], Specific binding in the 8-9S region also has been reported to exist in DES-induced mammary tumors of C3H mice [20]. The ''IOS" form reported in this paper is partly due to non-specific aggregation caused by the high protein concentrations necessary to detect mammary cytosol binding peaks.…”

Section: Resultsmentioning

confidence: 95%

Estrogen Binding in Mammary Tissue of C3H Mice With or Without the Mouse Mammary Tumor Virus

Bondy¹,

Okey²

1978

Oncology

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Substrains of C3H mice, with and without the milk-transmitted form of the mouse mammary tumor virus (MMTV)¹, were compared to determine if the presence of MMTV altered estrogen action. Uterine weight response to oral diethylstilbestrol was the same for both substrains, (MMTV⁺ and MMTV^-). The concentration of high-affinity estrogen binding sites ("receptors") in lactating mammary tissue did not differ significantly for MMTV⁺ versus MMTV^- mice; the affinity of the estradiol-receptor interaction appeared higher, however, in cytosol from MMTV^- mice. Sucrose density gradient analysis revealed no significant differences in sedimentation properties of cytosol receptor from the two substrains.

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“…Estrogen-binding was measured by the modification [25] of the charcoal adsorption assay originally described by Korenman [26]. Protein concentrations were measured by the method of Lowry et al [29] using bovine serum albumin as standard.…”

Section: Estrogen-binding Assaymentioning

confidence: 99%

Cyclic AMP‐Binding Proteins: Inverse Relationship with Estrogen‐Receptors in Hormone‐Dependent Mammary Tumor Regression

Cho‐Chung

Bodwin

Clair

1978

European Journal of Biochemistry

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Dimethylbenzanthracene-induced rat mammary carcinomas possess activities binding cyclic adenosine 3': 5'-monophosphate (CAMP) and estrogen. When dimethylbenzanthracene-induced tumors regress after ovariectomy of the host, a change in the specific binding of CAMP and estrogen occurs in the tumors. Six days after ovariectomy, CAMP binding increases 5-fold in the nuclei and 2-fold in the cytosol of tumors, while nuclear and cytoplasmic estrogen binding decreases by 80 and 50 %, respectively. These changes in activities binding CAMP and estrogen are detectable within 1 day after ovariectomy and the changes are reversed when resumption of tumor growth is induced by the injection of 17f3-estradiol. When dimethylbenzanthracene-induced tumors fail to regress after ovariectomy, the change in activities binding CAMP and estrogen does not occur. Significant increases in the cAMP level as well as in adenylate cyclase and CAMP-phosphodiesterase activities are also found in the regressing tumors. Concomitant with the increase of CAMP-binding activity is an increase in histone kinase activity in the regressing tumor. These data suggest the involvement of cAMP in the growth control of a hormone-dependent mammary tumor.

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Specific estrogen receptors in the lactating mammary gland of the rat

Cited by 53 publications

References 16 publications

Oestrogen receptor of mammary gland. Inhibition of aggregation and characterization of receptor from lactating gland in the presence of sodium bromide

Oestrogen receptor of mammary gland. Inhibition of aggregation and characterization of receptor from lactating gland in the presence of sodium bromide

Estrogen Binding in Mammary Tissue of C3H Mice With or Without the Mouse Mammary Tumor Virus

Cyclic AMP‐Binding Proteins: Inverse Relationship with Estrogen‐Receptors in Hormone‐Dependent Mammary Tumor Regression

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