Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones

Joab, Irène; Radanyi, Christine; Renoir, Michel; Buchou, Thierry; Catelli, Maria-Grazia; Binart, Nadine; Mešter, Ján; Baulieu, Étienne-Émile

doi:10.1038/308850a0

Cited by 437 publications

(152 citation statements)

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“…The function of this 90-kDa antigen is not yet understood. Moreover, recent studies have shown that the molybdate-stabilized 8-S forms of the estrogen and androgen receptors from chick oviduct cytosol, as well, interact with BF4 monoclonal antibody [16]. However, when gradient ultracentrifugation was performed in the presence of 0.5 M KCl, all steroid hormone receptors sedimented at z 4 S, irrespective of the presence of BF4 monoclonal antibody.…”

Section: Discussionmentioning

confidence: 95%

Chick oviduct glucocorticosteroid receptor

Groyer

Bouc

Joab

et al. 1985

European Journal of Biochemistry

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The glucocorticosteroid receptor (GR) has been studied in oviduct cytosol prepared from estrogen-primed, 4-week-withdrawn chicken. The equilibrium dissociation constant was 6 nM for dexamethasone, and 18 300 receptor sites/cell were measured assuming that all cells contain identical concentrations of GR. Dexamethasone, used in most studies investigating glucocorticosteroid action, was found not to be the best GR ligand. The affinities of several natural and synthetic glucocorticosteroids for GR increased in the following order: cortisol < deoxycorticosterone < dexamethasone < corticosterone < triamcinolone acetonide. The synthetic steroid RU 486 was the most specific ligand of GR (its affinity was 10-fold higher than that of triamcinolone acetonide), while it did not bind either to plasma transcortin (which binds dexamethasone nor, surprisingly, to progesterone receptor (PR), contrary to what occurs in mammalian species.The molybdate-stabilized, 8-S form of GR was prepared from withdrawn chick oviduct, whole chick embryo or cultured chick embryo fibroblasts (which do not contain PR), and was labeled with either [3H]dexamethasone or [3H]RU 486. The sedimentation coefficient of radioactive ligand -8-S GR complexes was shifted towards heavier forms after incubation with polyclonal (IgG-G3) or monoclonal (BF,) antibodies generated against the molybdate-stabilized, 8-S form of the chick oviduct PR. Since neither IgG-G3 nor BF4 interacted with the steroid binding 4-S form of GR, it is suggested that these antibodies recognized a non-steroid binding protein common to molybdate-stabilized, 8-S forms of GR and PR.The administration of sex steroid hormones to withdrawn chickens has been shown to stimulate egg-white protein synthesis [l -61. Moreover, it has been recently demonstrated that ovalbumin and conalbumin synthesis can be induced by glucocorticosteroids either in vitro or in vivo ([7, 81 Le Bouc et al., unpublished). Our results allowed us to exclude the possibility that glucocorticosteroids acted through either progesterone or estrogen pathways, and led to postulation of the existence of a glucocorticosteroid-specific mechanism for the induction of egg-white protein synthesis. We now report the characterization and the binding specificity of chick glucocorticosteroid receptor (GR), with emphasis on the unique binding properties of the synthetic steroid RU 486.Correspondence to A. Groyer, INSERM U 33 and CNRS ER 125, Laboratoire des Hormones, H6pital de BicCtre, F-94270 Le Kremlin Bicetre, FranceAbbreviations and Trivial Names. GR, glucocorticosteroid receptor; PR, progesterone receptor; corticosterone, 1 18,21-dihydroxypregn-4-ene-3,20-dione; cortisol, 118,17a,21 -trihydroxy-pregn-4-ene-3,20-dione; deoxycorticosterone, 21-hydroxy-pregn-4-ene-3,20-dione; dexamethasone, 9a-fluoro-1 1~,17a,21-trihydroxy-16a-methylpregn-l,4-diene-3,20-dione; estradiol benzoate, 1,3,5(10)-estratrien-3,17B-diol-3-benzoate; progesterone, pregn-4-ene-3,20-dione; R 5020, 17a,21-dimethyl-pregn-4,9(lO)-diene-3,20-dione; RU 486, 178-hydrox...

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Section: Discussionmentioning

confidence: 95%

Chick oviduct glucocorticosteroid receptor

Groyer

Bouc

Joab

et al. 1985

European Journal of Biochemistry

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“…It is one of the most abundant cellular proteins found even under nonstress conditions. It has been found to be associated with a number of other intracellular proteins, including actin [28,29], pp60"-"', pp140fp", ~~94~"" [30,31], and steroid hormone receptors [32]. It is suggested that HSP90 plays several important roles in cells, one being to act as a chaperon.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an endogenous inhibitor specific to the Z‐Leu‐Leu‐Leu‐MCA degrading activity in proteasome and its identification as heat‐shock protein 90

1994

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We previously identified a benzyloxycarbonyl(Z)-Leu-Leu-Leu-4-methylcoumaryl-7-amide (ZLLL-MCA) degrading activity in proteasome as a candidate for the regulator of neurite outgrowth. As its counterpart, we purified a protein from bovine brain that specifically inhibits the ZLLL-MCA degrading activity in proteasome. This protein is heat stable and has no effect on the other catalytic activities in proteasome, or on the activities of trypsin, chymotrypsin, or m-and p-calpains either. The molar ratio ofinhibitor-to-proteasome that inhibits 50% of the ZLLL-MCA degrading activity of proteasome is 1:1. The inhibitory mechanism of the inhibitor against proteasome is non-competitive. Finally, the inhibitor was identified as heat-shock protein 90 (HSP90) by partial amino acid sequencing and immunodetection. The results suggest that HSP90 initiates neurite outgrowth through the inhibition of the ZLLL-MCA degrading activity in proteasome.

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“…Later, Hsp90 was found to be associated with several different clients such as protein kinases and nuclear steroid receptors (e.g. glucocorticoid receptor) (Joab et al, 1984;Schuh et al, 1985;Smith, 1993;Smith et al, 1992). Since then, Hsp90 clients have grown tremendously owing to genome-wide high throughput studies.…”

Section: Ii41122 the Hsp90 Chaperone Systemmentioning

confidence: 99%