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Department of Endocrinology and Diabetes Mellitus, St Vincent’s University Hospital, Elm Park, Dublin, Ireland
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Department of Endocrinology and Diabetes Mellitus, St Vincent’s University Hospital, Elm Park, Dublin, Ireland
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Department of Endocrinology and Diabetes Mellitus, St Vincent’s University Hospital, Elm Park, Dublin, Ireland
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enzyme genes is the recruitment by nuclear receptors of coregulators (coactivators and corepressors) which interact with and effect transactivation ( McKenna et al. 1999 a ). It has been suggested that cofactors serve as a bridging apparatus between the
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et al . 2011 ). Primary coactivators interact directly with active TRs through the nuclear receptor (NR) recognition motif (NR box) ‘ LxxLL ’ ( Savkur & Burris 2004 ). This allows the recruitment of secondary coactivators to ultimately form a
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Introduction Peroxisome proliferator-activated receptors (PPARs) are a group of nuclear receptors that were initially identified as targets of compounds that increase peroxisome proliferation. Three PPAR genes have been identified – NR1C1, NR1
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Estrogen signaling Estrogens exert their physiological effects through two estrogen receptor (ER) subtypes, ERα and ERβ that belong to the nuclear receptor family of ligand-activated transcription factors. ERα is mainly expressed in reproductive
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The present paper describes studies conducted to detect and characterize the nuclear receptor for oestrogen in the baboon endometrium. Only 10% of the [3H]oestradiol nuclear receptor complexes were extracted with a 0·5 m-KCl solution. This solubilized receptor migrated as a 4·4S peak during 5–20% sucrose gradient centrifugation. The oestrogen receptor was not bound to oestrogen in the nuclei under normal physiological conditions. Using an unlabelled competitor addition technique with intact nuclei the variation in oestrogen-receptor concentration of baboon endometrium during the menstrual cycle was measured. This concentration increased slightly during the first week of the cycle, being maximal on day 7 before ovulation (2500 molecules/cell), then decreasing gradually, reaching the lowest level (300 molecules/cell) on day 5 after ovulation, where it remained until the end of the cycle.
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ABSTRACT
Retinoids and thyroid hormones exert profound effects on the development, growth and homeostasis of vertebrates. The receptor proteins which bind retinoic acid, tri-iodothyronine (T3) or steroid hormones and, as a result of this binding, interact with DNA to stimulate expression of specific genes, belong to the same recently discovered superfamily. The functionality of thyroid and steroid hormone receptors is thought to be related to a phosphorylation-dephosphorylation cycle. In the present work, the action of two retinoids (retinol and retinoic acid) was studied on the properties of T3-nuclear receptors and on protein kinase C (PKC) activity in the rat liver (PKC is known to be a phosphorylating enzyme for various proteins). The influence of 12-O-tetradecanoyl phorbol-13-acetate (TPA; known to enhance PKC activity) on the properties of T3-nuclear receptors was also investigated. Measurements of binding characteristics and enzyme activity were performed 4 or 12 h after a single i.p. injection of retinol or retinoic acid (6 mg/kg body weight) or 1 h after a single i.p. injection of TPA (0·7 mg/kg). The activity of PKC was increased 4 h after administration of the retinoids, and the affinity of the T3-nuclear receptor protein was increased markedly after 12 h. The activity of PKC and the affinity of the nuclear T3 receptor were both increased 1 h after administration of TPA. These observations provide indirect evidence that retinoids, particularly retinoic acid, induce an increase in PKC activity and a subsequent increase in the affinity of the T3-nuclear receptor protein.
Journal of Endocrinology (1991) 128, 245–251
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The orphan nuclear receptor TR2 and its truncated isoform deleted in the ligand binding domain (LBD) were localized exclusively in the nuclei as revealed by two methods of detection. An anti-hemagglutinin (HA) antibody detected specific nuclear localization of HA-tagged receptors and the green fluorescent protein (GFP)-tagged receptors were found to be distributed in the nuclei of living cells. By deletion analyses, the sequence responsible for targeting this receptor into the nucleus was defined. A stretch of 20 amino acid residues (KDCVINKHHRNRCQYCRLQR) within the second zinc-finger of this receptor is required for its nuclear localization and this signal is constitutively active. No nuclear localization signal was found in the N-terminus or the LBD. The GFP-tagged receptor remained biologically active, as evidenced by its repressive activity on the reporter that carried a binding site for this receptor, a direct repeat-5 (DR5). An electrophoretic mobility shift assay was performed to characterize the binding property of TR2 and its truncated isoform. TR2 bound to the DR5 as dimers whereas its truncated isoform bound as monomers.
Université Paris Descartes, Sorbonne Paris Cité, Paris, France
Assistance Publique-Hôpitaux de Paris, Hôpital Européen Georges Pompidou, Service de Génétique, Paris, France
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Université Paris Descartes, Sorbonne Paris Cité, Paris, France
Assistance Publique-Hôpitaux de Paris, Hôpital Européen Georges Pompidou, Service de Génétique, Paris, France
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potassium secretion in the distal tubule of the kidney, the colon, salivary and sweat glands via binding to the MR ( Pearce et al. 2003 ). The MR is a member of the steroid hormone receptor subgroup of the nuclear receptor superfamily ( Nuclear Receptor
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Cytokines and steroid hormones use different sets of signal transduction pathways, which seem to be unrelated. Interleukin-6 (IL-6) uses JAK tyrosine kinase and STAT (signal transducer and activator of transcription) transcription factor. Glucocorticoid binds glucocorticoid receptor (GR), which is a member of the steroid receptor superfamily. We have studied the crosstalk between the IL-6-JAK-STAT and glucocorticoid-nuclear receptor pathways. IL-6 and glucocorticoid synergistically activated the IL-6 response element on the rat alpha2-macroglobulin promoter (APRE)-driven luciferase gene. The exogenous expression of GR enhanced the synergism. The exogenous expression of dominant negative STAT3 completely abolished the IL-6 plus glucocorticoid-induced activation of the APRE-luciferase gene. Tyrosine phosphorylation of STAT3 stimulated by IL-6 alone was not different from that by IL-6 plus glucocorticoid. The protein level of STAT3 was also not increased by glucocorticoid stimulation. The time course of STAT3 tyrosine phosphorylation by IL-6 plus glucocorticoid was not different from that by IL-6 alone. The synergism was studied on the two other IL-6 response elements, the junB promoter (JRE-IL-6) and the interferon regulatory factor-1 (IRF-1) promoter (IRF-GAS) which could be activated by STAT3. The synergistic activation by glucocorticoid on the IL-6-activated JRE-IL-6 and the IRF-GAS-driven luciferase gene was not detected. Glucocorticoid did not change the mobility of IL-6-induced APRE-binding proteins in a gel shift assay. These results suggest that the synergism was through the GR and STAT3, and the coactivation pathway which was specific for APRE was the target of glucocorticoid.
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Introduction Estrogen (E) control of cell proliferation is a complex process that is subject to regulation at many levels. The nuclear receptor/transcription factor estrogen receptor-α (ESR1) is the key regulatory participant, transducing E action
