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1
Althumairy, Duaa, Xiaoping Zhang, Nicholas Baez, George Barisas, Deborah A. Roess, George R. Bousfield, and Debbie C. Crans. "Glycoprotein G-protein Coupled Receptors in Disease: Luteinizing Hormone Receptors and Follicle Stimulating Hormone Receptors." Diseases 8, no. 3 (September 15, 2020): 35. http://dx.doi.org/10.3390/diseases8030035.
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Signal transduction by luteinizing hormone receptors (LHRs) and follicle-stimulating hormone receptors (FSHRs) is essential for the successful reproduction of human beings. Both receptors and the thyroid-stimulating hormone receptor are members of a subset of G-protein coupled receptors (GPCRs) described as the glycoprotein hormone receptors. Their ligands, follicle-stimulating hormone (FSH) and luteinizing hormone (LH) and a structurally related hormone produced in pregnancy, human chorionic gonadotropin (hCG), are large protein hormones that are extensively glycosylated. Although the primary physiologic functions of these receptors are in ovarian function and maintenance of pregnancy in human females and spermatogenesis in males, there are reports of LHRs or FSHRs involvement in disease processes both in the reproductive system and elsewhere. In this review, we evaluate the aggregation state of the structure of actively signaling LHRs or FSHRs, their functions in reproduction as well as summarizing disease processes related to receptor mutations affecting receptor function or expression in reproductive and non-reproductive tissues. We will also present novel strategies for either increasing or reducing the activity of LHRs signaling. Such approaches to modify signaling by glycoprotein receptors may prove advantageous in treating diseases relating to LHRs or FSHRs function in addition to furthering the identification of new strategies for modulating GPCR signaling.
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G, Csaba. "Environmental Pollution and Non-Perinatal Faulty Hormonal Imprinting: A Critical Review." Integrative Pediatrics and Child Care 1, no. 1 (November 13, 2018): 54–62. http://dx.doi.org/10.18314/ipcc.v1i1.1419.
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The perinatal hormonal imprinting takes place perinatally, when the developing hormone receptors meet the hormones of the newborn and this suits the normal receptor-hormone connections for life. In this period the developmental window for imprinting is open and the receptors can be cheated by hormone-related exogeneous molecules, provoking faulty hormonal imprinting with lifelong consequences, as alteration of receptor binding capacity and hormone production, functional changes, altered sexual behavior, immunological alterations and inclination to or manifestation of diseases. However, there are other critical periods of life, when the window is open, as weaning, adolescence, regeneration in adults as well, as in continously dividing cells. The most sensitive non-perinatal critical period is the adolescence. In these periods hormone-like endocrine disruptors (e.g. bisphenol A, benzpyrene, pesticides and herbicides, soy isoflavones, medically used synthetic hormones etc) are provoking faulty hormonal imprinting with lifelong consequences. The hormonal imprinting is an epigenetic process, which is inherited to the progeny cells of the organism and to the offspring of the organism, by which it can chip in the evolution. The non-perinatal faulty hormonal imprinting is justified in animal experiments and seems to be likely in case of survivors of childhood cancer treatment. Similar to the faulty perinatal hormonal imprinting, the late (non-perinatal) faulty imprinting can participate in the provocation of later manifested diseases.
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Gomaa, Ihab Adel, Ahmed Sabry, Ihab Serag El-Din Allam, Sherif Ashoush, and Ahmed Reda. "Endometrial Progesterone and Estrogen Receptors in Relation to Hormonal Levels in Women with Unexplained Recurrent Miscarriage." Revista Brasileira de Ginecologia e Obstetrícia / RBGO Gynecology and Obstetrics 45, no. 11 (November 2023): e676-e682. http://dx.doi.org/10.1055/s-0043-1776030.
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Abstract Objective Recurrent miscarriage has been linked to hormonal disturbance due to dysregulation of its receptors rather than to the availability of the hormone. We aimed to investigate endometrial expression of progesterone and estrogen receptors in relation to serum and endometrial hormonal levels in unexplained recurrent miscarriage. Methods The present case control study included 20 cases with unexplained recurrent miscarriage and 20 parous women as controls. Ovulation was confirmed using an ovulation kit and 10 to 12 days after detecting the urinary luteinizing hormone surge, all women were subjected to a blood sample and to an endometrial biopsy. Progesterone and estrogen levels were measured in serum and in endometrial tissue and receptor concentrations were in the endometrial sample. Results Women with recurrent miscarriage showed significantly lower concentration of receptors in both the cytoplasm and the nucleus of endometrial tissue compared with controls. The nuclear/cytoplasm ratio of progesterone receptor was significantly higher in cases compared with controls, implicating that recurrent miscarriage is probably linked to nongenomic activity of the hormone; this was also significant for estrogen receptor. Serum progesterone and estrogen hormonal levels were comparable between groups while both hormones were significantly reduced in the endometrium of recurrent miscarriage cases. Receptors significantly correlated with endometrial hormonal level but not to serum level. Conclusion Recurrent miscarriage might be linked to reduced endometrial progesterone and estrogen receptors and appears to be more related to nongenomic activity of progesterone. Endometrial receptors expression correlates to tissue hormonal level rather than to serum hormonal level.
4
Kovács, P., Y. Nozawa, and G. Csaba. "Induction of hormone receptor formation in the unicellular tetrahymena." Bioscience Reports 9, no. 1 (February 1, 1989): 87–92. http://dx.doi.org/10.1007/bf01117514.
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Studies based on treatment with antibodies to thyrotropic hormone, luteotropic hormone, growth hormone or adrenocorticotropic hormone have shown that although the unicellular Tetrahymena does not possess sui generis receptors to all polypeptide hormones, such binding structures may arise, or become established in the membrane of the unicellular Tetrahymena in the presence of exogenous hormone. The Tetrahymena subjected to hormonal imprinting still contained an increased amount of hormone after six generation changes, which suggested that either hormone production had been induced by treatment, or the internalized hormone had not been degraded intracellularly. Thus the role of hormonal imprinting in receptor formation has also been substantiated by the immunocytochemical approach used in the present study.
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Tedeschi, Lorena, Cristina Vassalle, Giorgio Iervasi, and Laura Sabatino. "Main Factors Involved in Thyroid Hormone Action." Molecules 26, no. 23 (December 3, 2021): 7337. http://dx.doi.org/10.3390/molecules26237337.
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The thyroid hormone receptors are the mediators of a multitude of actions by the thyroid hormones in cells. Most thyroid hormone activities require interaction with nuclear receptors to bind DNA and regulate the expression of target genes. In addition to genomic regulation, thyroid hormones function via activation of specific cytosolic pathways, bypassing interaction with nuclear DNA. In the present work, we reviewed the most recent literature on the characteristics and roles of different factors involved in thyroid hormone function in particular, we discuss the genomic activity of thyroid hormone receptors in the nucleus and the functions of different thyroid hormone receptor isoforms in the cytosol. Furthermore, we describe the integrin αvβ3-mediated thyroid hormone signaling pathway and its rapid nongenomic action in the cell. We furthermore reviewed the thyroid hormone transporters enabling the uptake of thyroid hormones in the cell, and we also include a paragraph on the proteins that mediate thyroid receptors’ shuttling from the nucleus to the cytosol.
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Schulman, I. G., H. Juguilon, and R. M. Evans. "Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states." Molecular and Cellular Biology 16, no. 7 (July 1996): 3807–13. http://dx.doi.org/10.1128/mcb.16.7.3807.
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Transactivation-defective retinoid X and thyroid hormone receptors have been used to examine mechanisms of hormonal activation. Activation and repression of transcription by retinoid X and thyroid hormone receptors are shown to be mediated by physically distinct and functionally independent regions of the hormone binding domain. Nevertheless, the ability of receptors to respond to hormone requires communication between both functional domains. Deletion of the hormone-dependent transactivation function of the retinoid X receptor, the common subunit of heterodimeric nuclear receptors, significantly impairs hormone-dependent transcription by retinoic acid, thyroid hormone, and vitamin D receptors. The results indicate that receptors do not exist in static off and on conformations but that hormone alters an equilibrium between inactive and active states.
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Zarazúa, Abraham, Aliesha González-Arenas, Gabriela Ramírez-Vélez, Blanca Bazán-Perkins, Christian Guerra-Araiza, and María G. Campos-Lara. "Sexual Dimorphism in the Regulation of Estrogen, Progesterone, and Androgen Receptors by Sex Steroids in the Rat Airway Smooth Muscle Cells." International Journal of Endocrinology 2016 (2016): 1–11. http://dx.doi.org/10.1155/2016/8423192.
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The role of sex hormones in lung is known. The three main sex steroid receptors, estrogen, progesterone, and androgen, have not been sufficiently studied in airway smooth muscle cells (ASMC), and the sex hormone regulation on these receptors is unknown. We examined the presence and regulation of sex hormone receptors in female and male rat ASMC by Western blotting and flow cytometry. Gonadectomized rats were treated with 17β-estradiol, progesterone, 17β-estradiol + progesterone, or testosterone. ASMC were enzymatically isolated from tracheas and bronchi. The experiments were performed with double staining flow cytometry (anti-α-actin smooth muscle and antibodies to each hormone receptor). ERα, ERβ, tPR, and AR were detected in females or males. ERαwas upregulated by E2 and T and downregulated by P4 in females; in males, ERαwas downregulated by P4, E + P, and T. ERβwas downregulated by each treatment in females, and only by E + P and T in males. tPR was downregulated by P4, E + P, and T in females. No hormonal regulation was observed in male receptors. AR was downregulated in males treated with E + P and T. We have shown the occurrence of sex hormone receptors in ASMC and their regulation by the sex hormones in female and male rats.
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BLAND, Rosemary. "Steroid hormone receptor expression and action in bone." Clinical Science 98, no. 2 (January 31, 2000): 217–40. http://dx.doi.org/10.1042/cs0980217.
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The skeleton is a complex tissue, and hormonal control of bone remodelling is elaborate. The important role that steroid hormones play in bone cell development and in the maintenance of normal bone architecture is well established, but it is only relatively recently that it has become possible to describe their precise mechanism of action. This review focuses not only on the steroid hormones (oestrogens, corticosteroids, androgens and progesterone), but also on related hormones (vitamin D, thyroid hormone and the retinoids), all of which act via structurally homologous nuclear receptors that form part of the steroid/thyroid receptor superfamily. By examining the actions of all of these hormones in vivo and in vitro, this review gives a general overview of the current understanding of steroid hormone action in bone. In addition, a comprehensive review of steroid hormone receptor expression in bone cells is included. Finally, the role that future developments, such as steroid hormone receptor knockout mice, will play in our understanding of steroid hormone action in bone is considered.
9
Lin, B. C., S. H. Hong, S. Krig, S. M. Yoh, and M. L. Privalsky. "A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor release." Molecular and Cellular Biology 17, no. 10 (October 1997): 6131–38. http://dx.doi.org/10.1128/mcb.17.10.6131.
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Nuclear hormone receptors are ligand-regulated transcription factors that modulate gene expression in response to small, hydrophobic hormones, such as retinoic acid and thyroid hormone. The thyroid hormone and retinoic acid receptors typically repress transcription in the absence of hormone and activate it in the presence of hormone. Transcriptional repression is mediated, in part, through the ability of these receptors to physically associate with ancillary polypeptides called corepressors. We wished to understand the mechanism by which corepressors are recruited to unliganded nuclear hormone receptors and are released on the binding of hormone. We report here that an alpha-helical domain located at the thyroid hormone receptor C terminus appears to undergo a hormone-induced conformational change required for release of corepressor and that amino acid substitutions that abrogate this conformational change can impair or prevent corepressor release. In contrast, retinoid X receptors appear neither to undergo an equivalent conformational alteration in their C termini nor to release corepressor in response to cognate hormone, consistent with the distinct transcriptional regulatory properties displayed by this class of receptors.
10
Csaba, G. "Vitamin-caused faulty perinatal hormonal imprinting and its consequences in adult age." Physiology International 104, no. 3 (September 2017): 217–25. http://dx.doi.org/10.1556/2060.104.2017.3.5.
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Lipid-soluble vitamins (vitamins A, D, E, and K) are actually hormones (exohormones), as they can be directly bound by hormone receptors or are in connection with molecules, which influence hormone receptors. Vitamin D is a transition between endo- and exohormones and the possibility of similar situation in case of other lipid-soluble hormones is discussed. The perinatal exposition with these “vitamins” can cause faulty perinatal hormonal imprinting with similar consequences as the faulty imprinting by the synthetic endohormones, members of the same hormone family or industrial, communal, or medical endocrine disruptors. The faulty imprinting leads to late (lifelong) consequences with altered hormone binding by receptors, altered sexuality, brain function, immunity, bone development, and fractures, etc. In addition, as hormonal imprinting is an epigenetic process, the effect of a single exposure by fat-soluble vitamins is inherited to the progeny generations. As vitamins are handled differently from hormones; however, perinatal treatments take place frequently and sometimes it is forced, the negative late effect of faulty perinatal vitamin-caused hormonal imprinting must be considered.
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Ren, Bingtao, and Yan Zhu. "A New Perspective on Thyroid Hormones: Crosstalk with Reproductive Hormones in Females." International Journal of Molecular Sciences 23, no. 5 (February 28, 2022): 2708. http://dx.doi.org/10.3390/ijms23052708.
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Accumulating evidence has shown that thyroid hormones (THs) are vital for female reproductive system homeostasis. THs regulate the reproductive functions through thyroid hormone receptors (THRs)-mediated genomic- and integrin-receptor-associated nongenomic mechanisms, depending on TH ligand status and DNA level, as well as transcription and extra-nuclear signaling transduction activities. These processes involve the binding of THs to intracellular THRs and steroid hormone receptors or membrane receptors and the recruitment of hormone-response elements. In addition, THs and other reproductive hormones can activate common signaling pathways due to their structural similarity and shared DNA consensus sequences among thyroid, peptide, and protein hormones and their receptors, thus constituting a complex and reciprocal interaction network. Moreover, THs not only indirectly affect the synthesis, secretion, and action of reproductive hormones, but are also regulated by these hormones at the same time. This crosstalk may be one of the pivotal factors regulating female reproductive behavior and hormone-related diseases, including tumors. Elucidating the interaction mechanism among the aforementioned hormones will contribute to apprehending the etiology of female reproductive diseases, shedding new light on the treatment of gynecological disorders.
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Whitcomb, D. C., T. M. O'Dorisio, S. Cataland, and M. T. Nishikawara. "Theoretical basis for a new in vivo radioreceptor assay for polypeptide hormones." American Journal of Physiology-Endocrinology and Metabolism 249, no. 6 (December 1, 1985): E555—E560. http://dx.doi.org/10.1152/ajpendo.1985.249.6.e555.
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To date the in vivo identification and quantitation of specific hormone receptors has been difficult, time consuming, and lacking in sensitivity. We present the theory underlying a new in vivo radioreceptor assay for polypeptide hormones based on receptor theory derived from in vitro investigations and in vivo kinetic and autoradiographic studies. The assay was developed from a tissue model and a theory of hormone distribution. Measuring the labeled hormone distributed between the plasma and interstitial space in the presence or absence of excess unlabeled hormone permits the accurate determination of hormone specifically bound to receptors. This approach eliminates the problem of nonspecific binding due to free tracer, hormone degradation products, or labeled non-hormone molecules. A receptor compartment and specific binding of hormone are calculated from only four measured parameters: total tissue labeled hormone, tissue albumin, plasma labeled hormone, and plasma albumin. The method is applicable to most tissues and hormones under a variety of conditions and permits simultaneous comparison of multiple tissues in the same animal under identical conditions.
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Fannon, Stacey A., Regina M. Vidaver, and Sherry A. Marts. "Historical Perspectives: An abridged history of sex steroid hormone receptor action." Journal of Applied Physiology 91, no. 4 (October 1, 2001): 1854–59. http://dx.doi.org/10.1152/jappl.2001.91.4.1854.
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The field of steroid hormone action is well established, although it is barely more than four decades old. Pivotal experiments in the late 1950s and 1960s showed that hormone-binding components exist within nuclei of target tissues and that steroid hormones act by regulating gene expression, rather than directly influencing enzymatic processes. The understanding that steroid hormone receptors interact with the general transcription machinery and alter chromatin structure came in the 1970s and 1980s, and details of this mechanism continue to be elucidated. In addition, the discovery of rapid cellular responses to steroid hormones has led to the identification of putative membrane-bound steroid receptors that act without affecting gene transcription. As noted in the recent Institute of Medicine report Exploring the Biological Contributions to Human Health: Does Sex Matter?, the effects of steroid hormones and defects in steroid hormone receptor action have a profound impact on human health and disease. Future research directives include the development of potent, selective steroid receptor modulators, the elucidation of nongenomic steroid hormone effects, and further exploration of hormone-genome interactions.
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Kjær, Andreas. "Vasopressin as a neuroendocrine regulator of anterior pituitary hormone secretion." Acta Endocrinologica 129, no. 6 (December 1993): 489–96. http://dx.doi.org/10.1530/acta.0.1290489.
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Secretion of the anterior pituitary hormones adrenocorticotropin (ACTH), β-endorphin and prolactin (PRL) is complex and involves a variety of factors. This review focuses on the involvement of arginine-vasopressin (AVP) in neuroendocrine regulation of these anterior pituitary hormones with special reference to receptor involvement, mode of action and origin of AVP. Arginine-vasopressin may act via at least two types of receptors: V1− and V2−receptors, where the pituitary V1−receptor is designated V1b. The mode of action of AVP may be mediating, i.e. anterior pituitary hormone secretion is transmitted via release of AVP, or the mode of action may be permissive, i.e. the presence of AVP at a low and constant level is required for anterior pituitary hormones to be stimulated. Under in vivo conditions, the AVP-induced release of ACTH and β-endorphin is mainly mediated via activation of hypothalamic V1− receptors, which subsequently leads to the release of corticotropin-releasing hormone. Under in vitro conditions, the AVP-stimulated release of ACTH and β-endorphin is mediated via pituitary V1b− receptors. The mode of action of AVP in the ACTH and β-endorphin response to stress and to histamine, which is involved in stress-induced secretion of anterior pituitary hormones, is mediating (utilizing V1− receptors) as well as permissive (utilizing mainly V1− but also V2−receptors). The AVP-induced release of PRL under in vivo conditions is conveyed mainly via activation of V1−receptors but V2−receptors and probably additional receptor(s) may also play a role. In stress- and histamine induced PRL secretion the role of AVP is both mediating (utilizing V1 −receptors) and permissive (utilizing both V1− and V2− receptors). Arginine-vasopressin may be a candidate for the PRL-releasing factor recently identified in the posterior pituitary gland. Arginine-vasopressin of both magno- and parvocellular origin may be involved in the regulation of anterior pituitary hormone secretion and may reach the corticotrophs and the lactotrophs via three main routes: the peripheral circulation, the long pituitary portal vessels or the short pituitary portal vessels.
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Brooks, Charles L. "Molecular Mechanisms of Prolactin and Its Receptor." Endocrine Reviews 33, no. 4 (August 1, 2012): 504–25. http://dx.doi.org/10.1210/er.2011-1040.
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Prolactin and the prolactin receptors are members of a family of hormone/receptor pairs which include GH, erythropoietin, and other ligand/receptor pairs. The mechanisms of these ligand/receptor pairs have broad similarities, including general structures, ligand/receptor stoichiometries, and activation of several common signaling pathways. But significant variations in the structural and mechanistic details are present among these hormones and their type 1 receptors. The prolactin receptor is particularly interesting because it can be activated by three sequence-diverse human hormones: prolactin, GH, and placental lactogen. This system offers a unique opportunity to compare the detailed molecular mechanisms of these related hormone/receptor pairs. This review critically evaluates selected literature that informs these mechanisms, compares the mechanisms of the three lactogenic hormones, compares the mechanism with those of other class 1 ligand/receptor pairs, and identifies information that will be required to resolve mechanistic ambiguities. The literature describes distinct mechanistic differences between the three lactogenic hormones and their interaction with the prolactin receptor and describes more significant differences between the mechanisms by which other related ligands interact with and activate their receptors.
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Perkins, Meghan S., Renate Louw-du Toit, and Donita Africander. "Hormone therapy and breast cancer: emerging steroid receptor mechanisms." Journal of Molecular Endocrinology 61, no. 4 (November 2018): R133—R160. http://dx.doi.org/10.1530/jme-18-0094.
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Although hormone therapy is widely used by millions of women to relieve symptoms of menopause, it has been associated with several side effects such as coronary heart disease, stroke and increased invasive breast cancer risk. These side effects have caused many women to seek alternatives to conventional hormone therapy, including the controversial custom-compounded bioidentical hormone therapy suggested to not increase breast cancer risk. Historically, estrogens and the estrogen receptor were considered the principal factors promoting breast cancer development and progression; however, a role for other members of the steroid receptor family in breast cancer pathogenesis is now evident, with emerging studies revealing an interplay between some steroid receptors. In this review, we discuss examples of hormone therapy used for the relief of menopausal symptoms, highlighting the distinction between conventional hormone therapy and custom-compounded bioidentical hormone therapy. Moreover, we highlight the fact that not all hormones have been evaluated for an association with increased breast cancer risk. We also summarize the current knowledge regarding the role of steroid receptors in mediating the carcinogenic effects of hormones used in menopausal hormone therapy, with special emphasis on the influence of the interplay or crosstalk between steroid receptors. Unraveling the intertwined nature of steroid hormone receptor signaling pathways in breast cancer biology is of utmost importance, considering that breast cancer is the most prevalent cancer among women worldwide. Moreover, understanding these mechanisms may reveal novel prevention or treatment options and lead to the development of new hormone therapies that do not cause increased breast cancer risk.
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Cordeiro, Aline, Luana Lopes Souza, Marcelo Einicker-Lamas, and Carmen Cabanelas Pazos-Moura. "Non-classic thyroid hormone signalling involved in hepatic lipid metabolism." Journal of Endocrinology 216, no. 3 (January 7, 2013): R47—R57. http://dx.doi.org/10.1530/joe-12-0542.
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Thyroid hormones are important modulators of lipid metabolism because the liver is a primary hormonal target. The hypolipidaemic effects of thyroid hormones result from the balance between direct and indirect actions resulting in stimulation of lipid synthesis and lipid oxidation, which favours degradation pathways. Originally, it was believed that thyroid hormone activity was only transduced by alteration of gene transcription mediated by the nuclear receptor thyroid hormone receptors, comprising the classic action of thyroid hormone. However, the discovery of other effects independent of this classic mechanism characterised a new model of thyroid hormone action, the non-classic mechanism that involves other signalling pathways. To date, this mechanism and its relevance have been intensively described. Considering the increasing evidence for non-classic signalling of thyroid hormones and the major influence of these hormones in the regulation of lipid metabolism, we reviewed the role of thyroid hormone in cytosolic signalling cascades, focusing on the regulation of second messengers, and the activity of effector proteins and the implication of these mechanisms on the control of hepatic lipid metabolism.
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Freamat, Mihael, and Stacia A. Sower. "A sea lamprey glycoprotein hormone receptor similar with gnathostome thyrotropin hormone receptor." Journal of Molecular Endocrinology 41, no. 4 (July 30, 2008): 219–28. http://dx.doi.org/10.1677/jme-08-0030.
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The specificity of the vertebrate hypothalamic–pituitary–gonadal and hypothalamic–pituitary–thyroid axes is explained by the evolutionary refinement of the specificity of expression and selectivity of interaction between the glycoprotein hormones GpH (FSH, LH, and TSH) and their cognate receptors GpH-R (FSH-R, LH-R, and TSH-R). These two finely tuned signaling pathways evolved by gene duplication and functional divergence from an ancestral GpH/GpH-R pair. Comparative analysis of the protochordate and gnathostome endocrine systems suggests that this process took place prior or concomitantly with the emergence of the gnathostome lineage. Here, we report identification and characterization of a novel glycoprotein hormone receptor (lGpH-R II) in the Agnathan sea lamprey. This 781 residue protein was found ∼43% identical with mammalian TSH-R and FSH-R representative sequences, and similarly with these two classes of mammalian receptors it is assembled from ten exons. A synthetic ligand containing the lamprey glycoprotein hormone β-chain tethered upstream of a mammalian α-chain activated the lGpH-R II expressed in COS-7 cells but in a lesser extent than lGpH-R I. Molecular phylogenetic analysis of vertebrate GpH-R protein sequences suggests a closer relationship between lGpH-R II and gnathostome thyrotropin receptors. Overall, the presence and characteristics of the lamprey glycoprotein hormone receptors suggest existence of a primitive functionally overlapping glycoprotein hormone/glycoprotein hormone receptor system in this animal.
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Hillerns, Pablo Ibieta, Yuangang Zu, and Michael Wink. "Binding of Phytoestrogens to Rat Uterine Estrogen Receptors and Human Sex Hormone-binding Globulins." Zeitschrift für Naturforschung C 60, no. 7-8 (August 1, 2005): 649–56. http://dx.doi.org/10.1515/znc-2005-7-823.
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The interaction of phytoestrogens with the most important binding sites of steroid hormones, i.e. sex hormone-binding globulin and estrogen receptors, was investigated. Relative binding affinities and association constants for 21 compounds among them isoflavones, flavones, flavonols, flavanones, chalcones and lignans were determined. The lignan nordihydroguaiaretic acid weakly displaced 17β-[3H]-estradiol from estrogen receptor and Scatchard analysis suggests non-conformational changes. Compounds from Glycyrrhiza glabra, liquiritigenin and isoliquiritigenin, showed estrogenic affinities to both receptors. 18β-Glycyrrhetinic acid displaced 17β-[3H]-estradiol from sex hormone-binding globulin but not from the estrogen receptor. Phytoestrogens compete with 17β-estradiol much stronger than with 5α-dihydrotestosterone for binding to sex hormone-binding globulin.
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Webb, C. F., and M. Wallis. "A comparison of lactogenic receptors from rat liver and Nb2 rat lymphoma cells by using cross-linking techniques." Biochemical Journal 250, no. 1 (February 15, 1988): 215–19. http://dx.doi.org/10.1042/bj2500215.
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Lactogenic receptors were analysed with the use of the cross-linking agent disuccinimidyl suberate to attach covalently 125I-labelled ovine prolactin or human growth hormone to binding sites from (1) liver from pregnant rats and (2) the rat-derived Nb2 lymphoma cell line. Analysis by SDS/polyacrylamide-gel electrophoresis of the proteins cross-linked to labelled hormone in rat liver indicated a major specifically-labelled complex with an Mr of 68,000-72,000, when run under reducing or non-reducing conditions. With Nb2 cells a major specifically-labelled complex with an Mr of 97,000-110,000 was identified, but only when electrophoresis was run using reducing conditions. Assuming one hormone molecule (Mr 22,000-24,000) per hormone-receptor complex, then the receptor proteins have an Mr of 44,000-50,000 for rat liver and 73,000-88,000 for the Nb2 cells. For both cell types the receptors were of lactogenic specificity; lactogenic hormones competed for binding whereas somatogenic hormones did not. These studies suggest that the lactogenic receptors in rat liver membranes and Nb2 cells differ in two respects. Firstly, the Mr of the labelled receptor protein in Nb2 cells is greater than that of the corresponding receptor protein in rat liver membranes; secondly, the Nb2 cell receptor appears to exist as a disulphide-linked oligomer whereas the receptor in rat liver membranes does not.
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Honma, Naoko, Yoko Matsuda, and Tetuo Mikami. "Carcinogenesis of Triple-Negative Breast Cancer and Sex Steroid Hormones." Cancers 13, no. 11 (May 25, 2021): 2588. http://dx.doi.org/10.3390/cancers13112588.
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Triple-negative breast cancer (TNBC) lacks an effective treatment target and is usually associated with a poor clinical outcome; however, hormone unresponsiveness, which is the most important biological characteristic of TNBC, only means the lack of nuclear estrogenic signaling through the classical estrogen receptor (ER), ER-α. Several sex steroid receptors other than ER-α: androgen receptor (AR), second ER, ER-β, and non-nuclear receptors represented by G-protein-coupled estrogen receptor (GPER), are frequently expressed in TNBC and their biological and clinical importance has been suggested by a large number of studies. Despite the structural similarity between each sex steroid hormone (androgens and estrogens) or each receptor (AR and ER-β), and similarity in the signaling mechanisms of these hormones, most studies or reviews focused on one of these receptors, and rarely reviewed them in a comprehensive way. Considering the coexistence of these hormones and their receptors in TNBC in a clinical setting, a comprehensive viewpoint would be important to correctly understand the association between the carcinogenic mechanism or pathobiology of TNBC and sex steroid hormones. In this review, the carcinogenic or pathobiological role of sex steroid hormones in TNBC is considered, focusing on the common and divergent features of the action of these hormones.
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Hermann, T., X. K. Zhang, M. Tzukerman, K. N. Wills, G. Graupner, and M. Pfahl. "Regulatory functions of a non-ligand-binding thyroid hormone receptor isoform." Cell Regulation 2, no. 7 (July 1991): 565–74. http://dx.doi.org/10.1091/mbc.2.7.565.
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Gene regulation by thyroid hormones is mediated through multiple nuclear receptors. Only some of these thyroid hormone receptor (TR) isoforms become transcriptional enhancers in the presence of the thyroid hormone T3. Here we analyze the regulatory function of the human TR alpha 2 isoform. This protein does not bind T3 and is not a transcriptional activator of thyroid hormone-responsive elements (TRE). Transfected TR alpha 2 functions as a constitutive repressor of the transcriptional activators TR alpha 1 and TR beta 1 but also represses heterologous receptors, including the retinoic acid receptor and the estrogen receptor, which can activate TRE-controlled genes. TR alpha 2 protein showed strongly reduced DNA binding to a palindromic TRE when compared with the active TRs. Hybrid receptor analysis revealed that the special properties of the TR alpha 2 protein, including its repressor function and DNA binding characteristics, are intrinsic properties of its carboxyterminus and can be transferred to other receptors. Although it has been shown that the active TRs can act as repressors and silencers due to their strong DNA binding in the absence of hormone, our data show that TR alpha 2 is unlikely to inhibit TRs and other receptors through a competitive DNA binding mechanism. Antibody gel shift experiments suggest that repression by TR alpha 2 might result from interaction with active receptors. Thus, the receptor-like TR alpha 2 isoform differs from typical nuclear receptors in its DNA-binding and ligand-binding properties and appears to regulate the activity of other receptors via protein-protein interaction.
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Higa, Gerald M., and Ryan G. Fell. "Sex Hormone Receptor Repertoire in Breast Cancer." International Journal of Breast Cancer 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/284036.
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Classification of breast cancer as endocrine sensitive, hormone dependent, or estrogen receptor (ER) positive refers singularly to ERα. One of the oldest recognized tumor targets, disruption of ERα-mediated signaling, is believed to be the mechanistic mode of action for all hormonal interventions used in treating this disease. Whereas ERαis widely accepted as the single most important predictive factor (for response to endocrine therapy), the presence of the receptor in tumor cells is also of prognostic value. Even though the clinical relevance of the two other sex hormone receptors, namely, ERβand the androgen receptor remains unclear, two discordant phenomena observed in hormone-dependent breast cancers could be causally related to ERβ-mediated effects and androgenic actions. Nonetheless, our understanding of regulatory molecules and resistance mechanisms remains incomplete, further compromising our ability to develop novel therapeutic strategies that could improve disease outcomes. This review focuses on the receptor-mediated actions of the sex hormones in breast cancer.
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Vischer, Henry F., Joke C. M. Granneman, and Jan Bogerd. "Identification of Follicle-Stimulating Hormone-Selective β-Strands in the N-Terminal Hormone-Binding Exodomain of Human Gonadotropin Receptors." Molecular Endocrinology 20, no. 8 (August 1, 2006): 1880–93. http://dx.doi.org/10.1210/me.2005-0202.
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Abstract Glycoprotein hormone receptors contain large N-terminal extracellular domains (ECDs) that distinguish these receptors from most other G protein-coupled receptors. Each glycoprotein hormone receptor ECD consists of a curved leucine-rich repeat domain flanked by N- and C-terminal cysteine-rich regions. Selectivity of the different glycoprotein hormone receptors for their cognate hormones is exclusively determined by their ECDs and, in particular, their leucine-rich repeat domain. To identify human (h)FSH-selective determinants we used a gain-of-function mutagenesis strategy in which β-strands of the hLH receptor (hLH-R) were substituted with their hFSH receptor (hFSH-R) counterparts. Introduction of hFSH-R β-strand 1 into hLH-R conferred responsiveness to hFSH, whereas hLH-R mutants harboring one of the other hFSH-R β-strands displayed none or very limited sensitivity to hFSH. However, combined substitution of hFSH-R β-strand 1 and some of the other hFSH-R β-strands further increased the sensitivity of the mutant hLH-R to hFSH. The apparent contribution of multiple hFSH-R β-strands in providing a selective hormone binding interface corresponds well with their position in relation to hFSH as recently determined in the crystal structure of hFSH in complex with part of the hFSH-R ECD.
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Jayachandran, Muthuvel, and Virginia M. Miller. "Ovariectomy upregulates expression of estrogen receptors, NOS, and HSPs in porcine platelets." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 1 (July 1, 2002): H220—H226. http://dx.doi.org/10.1152/ajpheart.00950.2001.
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Platelets participate in normal and pathological thrombotic processes. Hormone replacement in postmenopausal women is associated with increase risk for thrombosis. However, little is known regarding how platelets are affected by hormonal status. Nitric oxide (NO) modulates platelet functions and is modulated by hormones. Therefore, the present study was designed to determine how loss of ovarian hormones changes expression of estrogen receptors and regulatory proteins for NO synthase (NOS) in platelets. Estrogen receptors (ERα and ERβ), NOS, heat shock proteins 70 and 90 (HSP70 and HSP90), caveolin-1, -2, and -3, calmodulin, NOS activity, and cGMP were analyzed in a lysate of platelets from gonadally intact and ovariectomized female pigs. Expression of ERβ and ERα receptors, endothelial NOS (eNOS), HSP70, and HSP90 increased with ovariectomy. NOS activity and cGMP also increased; calmodulin was unchanged. Caveolins were not detected. These results suggest that ovarian hormones influence expression of estrogen receptors and eNOS in platelets. Changes in estrogen receptors and NOS could affect platelet aggregation in response to hormone replacement.
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Dailey, M. O., J. Schreurs, and H. Schulman. "Hormone receptors on cloned T lymphocytes. Increased responsiveness to histamine, prostaglandins, and beta-adrenergic agents as a late stage event in T cell activation." Journal of Immunology 140, no. 9 (May 1, 1988): 2931–36. http://dx.doi.org/10.4049/jimmunol.140.9.2931.
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Abstract Lymphocytes have surface receptors for a variety of hormones that play an important part in modulating the immune response. Most previous studies, however, have examined the effects of hormone agonists on heterogeneous bulk populations of cells, making it difficult to precisely identify the responding target cells. We have therefore studied a set of well characterized T cell clones for a series of adenylate cyclase-linked hormone receptors and examined changes in receptor expression that occur after cell activation. All clones tested had receptors for histamine, isoproterenol, and PGE1, but not for several other cAMP-active hormone agonists. The apparent receptor affinities and their specificities were characteristic of typical histamine H2, beta 2-adrenergic, and PGE receptors. The cAMP response to PG was higher and longer lasting than that to histamine or isoproterenol, both of which appear to undergo receptor desensitization. After activation of quiescent cells in IL-2-containing media, the cAMP response to all three ligands increased, peaking 4 to 5 days after stimulation, and then returned to basal levels as the cells ceased proliferating. Inasmuch as this effect did not require Ag, it appears that the coordinate regulation of responsiveness to these ligands is a direct result of lymphocyte activation. This increase in hormone receptor activity is functionally analogous to the up-regulation of receptors for other ligands that occurs after lymphocyte activation and further demonstrates the important immunoregulatory role played by the changing repertoire of surface receptors that is associated with activation.
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Kanyicska, B., and M. E. Freeman. "Characterization of endothelin receptors in the anterior pituitary gland." American Journal of Physiology-Endocrinology and Metabolism 265, no. 4 (October 1, 1993): E601—E608. http://dx.doi.org/10.1152/ajpendo.1993.265.4.e601.
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To characterize endothelin (ET) receptors modulating pituitary hormone secretion, potencies of ET-like agonists were compared on prolactin (PRL), thyrotropin (TSH), luteinizing hormone (LH), and follicle-stimulating hormone (FSH) secretion from primary cultures of female rat pituitary cells. ET-1 was more potent than ET-3 in all cases. Sarafotoxin (SRTX) S6b an ETA agonist, was also more potent than ET-3 in all cases. SRTX-c, an ETB receptor agonist, was inactive. The ET-1-to-ET-3 potency ratio was three orders of magnitude higher on PRL or TSH secretion than on LH and FSH secretion, whereas SRTX-b-to-ET-3 potency ratios were similar on all four hormones. The ETA antagonist BQ-123 caused a parallel dextral displacement of dose-response curves of ET-1 and ET-3 on all four hormones. Schild regressions for BQ-123 on ET-1-induced PRL, TSH, LH, and FSH secretion indicated that BQ-123 has a similar affinity for the receptors mediating ET-1's effects. When BQ-123 was assessed against ET-3, Schild regressions indicated greater affinity for ET-3 on lactotrophs and thyrotrophs than gonadotrophs. Thus changes in pituitary hormone secretion are mediated by ETA-like receptors. ET receptors in lactotrophs and thyrotrophs are clearly distinguishable from gonadotrophs. We suggest the existence of distinct ETA receptor subtypes (ETA1 and ETA2) on these differing pituitary cells.
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Kudo, Masataka, Thomas Chen, Koji Nakabayashi, Sheau Yu Hsu, and Aaron J. W. Hsueh. "The Nematode Leucine-Rich Repeat-Containing, G Protein-Coupled Receptor (LGR) Protein Homologous to Vertebrate Gonadotropin and Thyrotropin Receptors is Constitutively Activated in Mammalian Cells." Molecular Endocrinology 14, no. 2 (February 1, 2000): 272–84. http://dx.doi.org/10.1210/mend.14.2.0422.
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Abstract The receptors for LH, FSH, and TSH belong to the large G protein-coupled, seven-transmembrane (TM) protein family and are unique in having a large N-terminal extracellular (ecto-) domain containing leucine-rich repeats important for interactions with the large glycoprotein hormone ligands. Recent studies indicated the evolution of an expanding family of homologous leucine-rich repeat-containing, G protein-coupled receptors (LGRs), including the three known glycoprotein hormone receptors; mammalian LGR4 and LGR5; and LGRs in sea anemone, fly, and snail. We isolated nematode LGR cDNA and characterized its gene from the Caenorhabditis elegans genome. This receptor cDNA encodes 929 amino acids consisting of a signal peptide for membrane insertion, an ectodomain with nine leucine-rich repeats, a seven-TM region, and a long C-terminal tail. The nematode LGR has five potential N-linked glycosylation sites in its ectodomain and multiple consensus phosphorylation sites for protein kinase A and C in the cytoplasmic loop and C tail. The nematode receptor gene has 13 exons; its TM region and C tail, unlike mammalian glycoprotein hormone receptors, are encoded by multiple exons. Sequence alignments showed that the TM region of the nematode receptor has 30% identity and 50% similarity to the same region in mammalian glycoprotein hormone receptors. Although human 293T cells expressing the nematode LGR protein do not respond to human glycoprotein hormones, these cells exhibited major increases in basal cAMP production in the absence of ligand stimulation, reaching levels comparable to those in cells expressing a constitutively activated mutant human LH receptor found in patients with familial male-limited precocious puberty. Analysis of cAMP production mediated by chimeric receptors further indicated that the ectodomain and TM region of the nematode LGR and human LH receptor are interchangeable and the TM region of the nematode LGR is responsible for constitutive receptor activation. Thus, the identification and characterization of the nematode receptor provides the basis for understanding the evolutionary relationship of diverse LGRs and for future analysis of mechanisms underlying the activation of glycoprotein hormone receptors and related LGRs.
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Mendelsohn, Laurane G. "Growth hormone receptors." Life Sciences 43, no. 1 (January 1988): 1–5. http://dx.doi.org/10.1016/0024-3205(88)90229-9.
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Plaut, M. "Lymphocyte Hormone Receptors." Annual Review of Immunology 5, no. 1 (April 1987): 621–69. http://dx.doi.org/10.1146/annurev.iy.05.040187.003201.
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Nemere, Ilka, and Korry Hintze. "Novel hormone “receptors”." Journal of Cellular Biochemistry 103, no. 2 (2008): 401–7. http://dx.doi.org/10.1002/jcb.21437.
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Fliss, Albert E., Yifang Fang, Frank Boschelli, and Avrom J. Caplan. "Differential In Vivo Regulation of Steroid Hormone Receptor Activation by Cdc37p." Molecular Biology of the Cell 8, no. 12 (December 1997): 2501–9. http://dx.doi.org/10.1091/mbc.8.12.2501.
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The CDC37 gene is essential for the activity of p60v-src when expressed in yeast cells. Since the activation pathway for p60v-src and steroid hormone receptors is similar, the present study analyzed the hormone-dependent transactivation by androgen receptors and glucocorticoid receptors in yeast cells expressing a mutant version of the CDC37gene. In this mutant, hormone-dependent transactivation by androgen receptors was defective at both permissive and restrictive temperatures, although transactivation by glucocorticoid receptors was mildly defective only at the restrictive temperature. Cdc37p appears to function via the androgen receptor ligand-binding domain, although it does not influence receptor hormone-binding affinity. Models for Cdc37p regulation of steroid hormone receptors are discussed.
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Ji, Inhae, ChangWoo Lee, YongSang Song, P. Michael Conn, and Tae H. Ji. "Cis- and Trans-Activation of Hormone Receptors: the LH Receptor." Molecular Endocrinology 16, no. 6 (June 1, 2002): 1299–308. http://dx.doi.org/10.1210/mend.16.6.0852.
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Abstract G protein-coupled receptors (GPCRs) accommodate a wide spectrum of activators from ions to glycoprotein hormones. The mechanism of activation for this large and clinically important family of receptors is poorly understood. Although initially thought to function as monomers, there is a growing body of evidence that GPCR dimers form, and in some cases that these dimers are essential for signal transduction. Here we describe a novel mechanism of intermolecular GPCR activation, which we refer to as trans-activation, in the LH receptor, a GPCR that does not form stable dimers. The LH receptor consists of a 350-amino acid amino-terminal domain, which is responsible for high-affinity binding to human CG, followed by seven-transmembrane domains and connecting loops. This seven-transmembrane domain bundle transmits the signal from the extracellular amino terminus to intracellular G proteins and adenylyl cyclase. Here, we show that binding of hormone to one receptor can activate adenylyl cyclase through its transmembrane bundle, intramolecular activation (cis-activation), as well as trans-activation through the transmembrane bundle of an adjacent receptor, without forming a stable receptor dimer. Coexpression of a mutant receptor defective in hormone binding and another mutant defective in signal generation rescues hormone-activated cAMP production. Our observations provide new insights into the mechanism of receptor activation mechanisms and have implications for the treatment of inherited disorders of glycoprotein hormone receptors.
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Gittoes, Neil J. L., Christopher J. McCabe, Julie Verhaeg, Michael C. Sheppard, and Jayne A. Franklyn. "Thyroid Hormone and Estrogen Receptor Expression in Normal Pituitary and Nonfunctioning Tumors of the Anterior Pituitary1." Journal of Clinical Endocrinology & Metabolism 82, no. 6 (June 1, 1997): 1960–67. http://dx.doi.org/10.1210/jcem.82.6.3969.
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Abstract Nonfunctioning tumors (NFTs) of the anterior pituitary often express elevated levels of the glycoprotein hormone α-subunit, which, under normal physiological conditions, is under negative feedback control by thyroid and gonadal steroid hormones. We postulate that inappropriately elevated levels of expression of α-subunit in the face of normal levels of these target organ hormones may reflect an abnormality of thyroid hormone receptors (TRs) and/or gonadal steroid receptors in NFTs. Using immunocytochemistry and Western blotting we have examined TR and estrogen receptor (ER) protein expression in normal human anterior pituitary glands and NFTs. Pretranslational expression of these receptors was examined using semiquantitative reverse transcriptase-PCR. Expression of all TR variant and ER proteins was reduced in pituitary tumors compared with that in normal pituitaries. The expression of messenger ribonucleic acids encoding the TRβ1 and TRβ2 isoforms and ER was also significantly reduced in tumors compared with normal tissues, although there was no difference between tumors and normals in the level of expression of TRα1 and α2 messenger ribonucleic acids. We suggest that reduced expression of TRs and ER may account for inappropriate expression of the glycoprotein hormoneα -subunit gene in some NFTs and may contribute to uncontrolled tumor growth.
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Dauncey, M. J., P. White, K. A. Burton, and M. Katsumata. "Nutrition–hormone receptor–gene interactions: implications for development and disease." Proceedings of the Nutrition Society 60, no. 1 (February 2001): 63–72. http://dx.doi.org/10.1079/pns200071.
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Nutrition profoundly alters the phenotypic expression of a given genotype, particularly during fetal and postnatal development. Many hormones act as nutritional signals and their receptors play a key role in mediating the effects of nutrition on numerous genes involved in differentiation, growth and metabolism. Polypeptide hormones act on membrane-bound receptors to trigger gene transcription via complex intracellular signalling pathways. By contrast, nuclear receptors for lipid-soluble molecules such as glucocorticoids (GC) and thyroid hormones (TH) directly regulate transcription via DNA binding and chromatin remodelling. Nuclear hormone receptors are members of a large superfamily of transcriptional regulators with the ability to activate or repress many genes involved in development and disease. Nutrition influences not only hormone synthesis and metabolism but also hormone receptors, and regulation is mediated either by specific nutrients or by energy status. Recent studies on the role of early environment on development have implicated GC and their receptors in the programming of adult disease. Intrauterine growth restriction and postnatal undernutrition also induce striking differences in TH-receptor isoforms in functionally-distinct muscles, with critical implications for gene transcription of myosin isoforms, glucose transporters, uncoupling proteins and cation pumps. Such findings highlight a mechanism by which nutritional status can influence normal development, and modify nutrient utilization, thermogenesis, peripheral sensitivity to insulin and optimal cardiac function. Diet and stage of development will also influence the transcriptional activity of drugs acting as ligands for nuclear receptors. Potential interactions between nuclear receptors, including those for retinoic acid and vitamin D, should not be overlooked in intervention programmes using I or vitamin A supplementation of young and adult human populations.
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Rubio, Rafael. "The Endothelial Barrier Restricts Endocrine Actions to the Luminal Vascular Receptors: Changing the Paradigm: A Didactic Approach." European Journal of Medical and Health Sciences 3, no. 6 (November 13, 2021): 8–16. http://dx.doi.org/10.24018/ejmed.2021.3.6.1070.
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In 1849, the first list of endocrine hormones was discovered and proposed that the synthesizing gland delivers it to the circulation. The circulatory hormone reaches the target organ, physically unimpeded acts directly on the parenchymal cells. Such a simplistic view persists despite new knowledge of an endothelial wall barrier and implications for every parenchymal cell in the body. This misconception leads to inadequate interpretations of data, wrong diagnosis and therapeutic expectations, erroneous hypotheses, and misleads further research work. The quest of this review is to play down this misconception by pointing out key overlooked findings of the vascular endothelial wall: 1) The selective endothelial barrier physically separates two same-hormone-containing compartments; the endocrine and the interstitial autocrine hormone compartments, 2) the hormone concentrations values in these compartments are independent of each other, 3) in each compartment the hormone acts solely on the receptors of that particular compartment, 4) multiple intravascular endocrine hormones act solely on their corresponding luminal endothelial membrane receptor (LEMR), without directly acting on the parenchymal cells, 5) Agonist-activation of LEMR triggers the release of specific paracrine endothelial agents that in conjunction with autocrine interstitial hormone modulate parenchymal function(s) and perhaps the turnover of the interstitial autocrine hormone, 6) these hormone compartments, functionally interact via paracrine exchange signaling, and the integrated intercourse of all these events result in the final hormonal organ effect. The present challenges to achieving more rationale therapeutic effects are to design agonists or antagonists that exclusively gain access to a target compartment and have high specificity for the receptor of the cells in that compartment.
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Puzianowska-Kuznicka, Monika, Eliza Pawlik-Pachucka, Magdalena Owczarz, Monika Budzińska, and Jacek Polosak. "Small-Molecule Hormones: Molecular Mechanisms of Action." International Journal of Endocrinology 2013 (2013): 1–21. http://dx.doi.org/10.1155/2013/601246.
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Small-molecule hormones play crucial roles in the development and in the maintenance of an adult mammalian organism. On the molecular level, they regulate a plethora of biological pathways. Part of their actions depends on their transcription-regulating properties, exerted by highly specific nuclear receptors which are hormone-dependent transcription factors. Nuclear hormone receptors interact with coactivators, corepressors, basal transcription factors, and other transcription factors in order to modulate the activity of target genes in a manner that is dependent on tissue, age and developmental and pathophysiological states. The biological effect of this mechanism becomes apparent not earlier than 30–60 minutes after hormonal stimulus. In addition, small-molecule hormones modify the function of the cell by a number of nongenomic mechanisms, involving interaction with proteins localized in the plasma membrane, in the cytoplasm, as well as with proteins localized in other cellular membranes and in nonnuclear cellular compartments. The identity of such proteins is still under investigation; however, it seems that extranuclear fractions of nuclear hormone receptors commonly serve this function. A direct interaction of small-molecule hormones with membrane phospholipids and with mRNA is also postulated. In these mechanisms, the reaction to hormonal stimulus appears within seconds or minutes.
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Tetzlaff, S., S. Ponsuksili, E. Murani, K. Schellander, and K. Wimmers. "SNP analysis, genotyping and mapping of the porcine <i>PTHR1</i> gene to chromosome 13 (Brief report)." Archives Animal Breeding 50, no. 3 (October 10, 2007): 320–21. http://dx.doi.org/10.5194/aab-50-320-2007.
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Abstract. The parathyroid hormone/parathyroid hormone like hormone type I receptor (PTHR1) belongs to the family of G protein-coupled receptors for peptide hormones, including parathyroid hormone (PTH) and parathyroid hormone like hormone (PTHLH), which participate in epithelial-mesenchymal interactions during the formation and differentiation of epithelial organs (FOLEY et al., 2001; CHOMDEJ et al., 2004). The function of PTHR1 and its ligands suggest its candidacy for traits related to the development of bones and joints but also of mammary gland. The porcine gene was screened for SNPs and assigned to SSC13.
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Johnson, Jill L., and Elizabeth A. Craig. "A Role for the Hsp40 Ydj1 in Repression of Basal Steroid Receptor Activity in Yeast." Molecular and Cellular Biology 20, no. 9 (May 1, 2000): 3027–36. http://dx.doi.org/10.1128/mcb.20.9.3027-3036.2000.
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ABSTRACT In addition to its roles in translocation of preproteins across membranes, Ydj1 facilitates the maturation of Hsp90 substrates, including mammalian steroid receptors, which activate transcription in yeast in a hormone-dependent manner. To better understand Ydj1's function, we have constructed and analyzed an array of Ydj1 mutants in vivo. Both the glucocorticoid receptor and the estrogen receptor exhibited elevated activity in the absence of hormone in allydj1 mutant strains, indicating a strict requirement for Ydj1 activity in hormonal control. Glucocorticoid receptor containing a mutation in the carboxy-terminal transcriptional activation domain, AF-2, retained elevated basal activity, while mutation of the amino-terminal transactivation domain, AF-1, eliminated the elevated basal activity observed in ydj1 mutant strains. This result indicates that the source of activity is AF-1, which is normally repressed by the carboxy-terminal hormone binding domain in the absence of hormone. Chimeric proteins containing the hormone binding domain of the estrogen or glucocorticoid receptor fused to heterologous activation and DNA binding domains also exhibited elevated activity in the absence of hormone. Thus, Ydj1 mutants appear to increase basal receptor activity by altering the ability of the hormone binding domain of the receptor to repress nearby activation domains. We propose that Ydj1 functions to present steroid receptors to the Hsp90 pathway for folding and hormonal control. In the presence of Ydj1 mutants that fail to bind substrate efficiently, some receptor escapes the Hsp90 pathway, resulting in constitutive activity.
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Stossi, Fabio, Radhika D. Dandekar, Maureen G. Mancini, Guowei Gu, Suzanne A. W. Fuqua, Agostina Nardone, Carmine De Angelis, et al. "Estrogen-induced transcription at individual alleles is independent of receptor level and active conformation but can be modulated by coactivators activity." Nucleic Acids Research 48, no. 4 (January 13, 2020): 1800–1810. http://dx.doi.org/10.1093/nar/gkz1172.
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Abstract Steroid hormones are pivotal modulators of pathophysiological processes in many organs, where they interact with nuclear receptors to regulate gene transcription. However, our understanding of hormone action at the single cell level remains incomplete. Here, we focused on estrogen stimulation of the well-characterized GREB1 and MYC target genes that revealed large differences in cell-by-cell responses, and, more interestingly, between alleles within the same cell, both over time and hormone concentration. We specifically analyzed the role of receptor level and activity state during allele-by-allele regulation and found that neither receptor level nor activation status are the determinant of maximal hormonal response, indicating that additional pathways are potentially in place to modulate cell- and allele-specific responses. Interestingly, we found that a small molecule inhibitor of the arginine methyltransferases CARM1 and PRMT6 was able to increase, in a gene specific manner, the number of active alleles/cell before and after hormonal stimulation, suggesting that mechanisms do indeed exist to modulate hormone receptor responses at the single cell and allele level.
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Bishop, J. Michael. "Steroid receptors: Oncogenes as hormone receptors." Nature 321, no. 6066 (May 1986): 112–13. http://dx.doi.org/10.1038/321112a0.
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Wagner, Richard L., B. Russell Huber, Andrew K. Shiau, Alex Kelly, Suzana T. Cunha Lima, Thomas S. Scanlan, James W. Apriletti, John D. Baxter, Brian L. West, and Robert J. Fletterick. "Hormone Selectivity in Thyroid Hormone Receptors." Molecular Endocrinology 15, no. 3 (March 1, 2001): 398–410. http://dx.doi.org/10.1210/mend.15.3.0608.
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Marchand, O., R. Safi, H. Escriva, E. Van Rompaey, P. Prunet, and V. Laudet. "Molecular cloning and characterization of thyroid hormone receptors in teleost fish." Journal of Molecular Endocrinology 26, no. 1 (February 1, 2001): 51–65. http://dx.doi.org/10.1677/jme.0.0260051.
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Thyroid hormones are pleiotropic factors important for many developmental and physiological functions in vertebrates. Their effects are mediated by two specific receptors (TRalpha and TRbeta) which are members of the nuclear hormone receptor superfamily. To clarify the function of these receptors, our laboratory has started a comparative study of their role in teleost fish. This type of approach has been hampered by the isolation of specific clones for each fish species studied. In this report, we describe an efficient reverse transcription/PCR procedure that allows the isolation of large fragments corresponding to TRalpha and TRbeta of a wide range of teleost fish. Phylogenetic analysis of these receptors revealed a placement consistent with their origin, sequences from teleost fish being clearly monophyletic for both TRalpha and TRbeta. Interestingly, this approach allowed us to isolate (from tilapia and salmon) several new TRalpha or TRbeta isoforms resulting from alternative splicing. These isoforms correspond to expressed transcripts and thus may have an important physiological function. In addition, we isolated a cDNA encoding TRbeta in the Atlantic salmon (Salmo salar) encoding a functional thyroid hormone receptor which binds specific thyroid hormone response elements and regulates transcription in response to thyroid hormones.
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Eggena, P., and C. L. Ma. "Downregulation of vasopressin receptors in toad bladder." American Journal of Physiology-Cell Physiology 250, no. 3 (March 1, 1986): C453—C459. http://dx.doi.org/10.1152/ajpcell.1986.250.3.c453.
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Binding of tritium-labeled vasopressin [( 3H]AVP) to a broken epithelial cell preparation of the toad's urinary bladder has been related to hormonal action on water and urea transport across the intact tissue. Hormone binding to receptor sites and permeability changes were initiated at the same concentration of hormone (0.4 nM). Half-maximal urea and water permeability responses were observed with 3.1 and 5.6 nM AVP, respectively, although half-maximal receptor saturation required considerably higher concentrations of hormone (less than 500 nM). Because maximal permeability responses were obtained with occupation of approximately 200 fmol/mg protein receptor sites and the total receptor density was in excess of 2,000 fmol/mg protein, there is apparently a receptor reserve in this tissue. The antidiuretic hormone employed by the toad is vasotocin (AVT). This compound was 60-fold more effective than AVP in displacing [3H]AVP from receptor sites. Preincubation of bladders with AVT resulted in downregulation of receptor sites. Although the magnitude of receptor loss was equivalent in the presence or absence of a transmembrane osmotic pressure gradient, the capacity of AVT to induce permeability changes was more markedly reduced in the presence of an osmotic gradient. This observation suggests that the negative-feedback signal initiated by water flow through the hormone target cell diminishes sensitivity to hormone by a mechanism other than by a reduction in the number of surface receptors or by a decrease in their affinity for the hormone.
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Bonthuis, Paul J., James K. Patteson, and Emilie F. Rissman. "Acquisition of Sexual Receptivity: Roles of Chromatin Acetylation, Estrogen Receptor-α, and Ovarian Hormones." Endocrinology 152, no. 8 (June 7, 2011): 3172–81. http://dx.doi.org/10.1210/en.2010-1001.
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Sexually naïve, hormone-primed, C57BL/6J female mice are not receptive to mating attempts by conspecific males. Repeated experience with sexually active males and concurrent treatment with estradiol and progesterone gradually increases female receptivity over the course of five trials to maximal levels. Ovarian hormones activate their cognate nuclear steroid receptors estrogen receptor-α and progesterone receptor to induce female sexual receptivity. Nuclear receptors recruit coactivators of transcription that include histone acetyltransferases to hormone responsive genes. In this set of studies, we found that the histone deacetylase inhibitor sodium butyrate enhances the experiential acquisition of receptivity. Evidence is provided that the actions of sodium butyrate on receptivity require activated estrogen receptor-α and progesterone.
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Törmä, H., O. Rollman, and A. Vahlquist. "Detection of mRNA transcripts for retinoic acid, vitamin D3, and thyroid hormone (c/erb/A) nuclear receptors in human skin using reverse transcription and polymerase chain reaction." Acta Dermato-Venereologica 73, no. 2 (April 1, 1993): 102–7. http://dx.doi.org/10.2340/0001555573102107.
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Differentiation of keratinocytes involves both non/genomic and genomic events. The genomic effects are regulated by ligand/dependent transcription factors, e.g. the steroid/thyroid super/family of nuclear receptors. In the present study we examined mRNA expression of receptors for retinoic acid, thyroid hormone, and vitamin D3 in normal human skin and cultured keratinocytes using reverse transcription coupled to the polymerase chain reaction. The vitamin D3 receptor and the retinoic acid receptor (RAR) gamma together with the more distantly related RXR alpha were amplified extensively in skin and cultured keratinocytes. RAR alpha was amplified at a lower level, and RAR beta was almost undetectable. The thyroid hormone receptors alpha 1 and beta 1 were weakly amplified, but to comparable levels. Because receptors for retinoic acid, thyroid hormones, and vitamin D3 are all expressed in human epidermis differentiation of keratinocytes is probably regulated at transcriptional level by these molecules. It remains to be seen whether alterations in the expression of the nuclear receptors occur in certain skin disorders.
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Wei, L. L. "Transcriptional activation of the estrogen receptor." Clinical Chemistry 39, no. 2 (February 1, 1993): 341–45. http://dx.doi.org/10.1093/clinchem/39.2.341.
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Abstract Almost all breast cancer tumors progress to a hormone-resistant state. Evidence is presented that the existence of mutant estrogen receptors may explain some hormone-resistant phenotypes. Breast tumor cells bearing a mutant receptor that is constitutively active and does not bind hormone would have unregulated cell growth and thus appear to be hormone-independent. Alternatively, breast cancer cells may contain estrogen receptors that are transcriptionally inactive but when co-expressed with wild-type receptors render normal estrogen receptors inactive. These cells would be considered estrogen receptor-positive but would be hormone-resistant. The hormone-resistant phenotype could be further complicated by the finding that other nonreceptor proteins may also modulate the transcriptional activity of estrogen receptors. These findings, if substantiated in vivo, could add to the complexity of the hormone-resistant phenotype. Different strategies of treatment will need to be developed to effectively treat the various subtypes of hormone-resistant breast tumors.
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Shramko, S. V., L. F. Gulyaeva, V. N. Zorina, and T. V. Tretyakova. "Proliferative diseases of the uterus: clinical, immunological, and molecular aspects." Voprosy ginekologii, akušerstva i perinatologii 19, no. 5 (2020): 13–21. http://dx.doi.org/10.20953/1726-1678-2020-5-13-21.
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Objective. To perform comparative analysis of clinical data, serum levels of acute-phase proteins, cytokines, steroid hormones, and expression of genes encoding sex hormone receptors in tissues of patients with proliferative diseases of the uterus. Patients and methods. We analyzed clinical data of 349 patients with various proliferative diseases of the uterus. We also evaluated their serum levels of α2-macroglobulin, pregnancy-associated α2-glycoprotein, their immunocomplexes with IgG, lactoferrin, VEGF, IL-6, TNFa, IL-8, and sex hormones. Uterine tissue samples were tested for the expression of genes encoding estrogen receptors α and β (ЕRα, ЕRβ) and progesterone receptors (PGR). Data analysis was performed using the statistical packages of SAS 9.4, STATISTICA12, and IBM-SPSS Statistics 22. Results. The changes in the level of acute-phase proteins indicated inflammation. In isolated uterine fibroids, expression of genes encoding progesterone receptors prevailed, whereas in isolated adenomyosis, expression of genes encoding estrogen receptors prevailed. Patients with both uterine fibroids and adenomyosis demonstrated similar levels of expression of genes encoding sex steroid hormone receptors. Tissues of uterine leiomyosarcoma were characterized by downregulated expression of genes encoding sex steroid hormone receptors. Conclusion. Upregulation of genes encoding progesterone receptors in isolated uterine fibroids confirms that therapy with progesterone receptor blockers is appropriate in this case. The predominance of expression of genes encoding estrogen receptors in isolated adenomyosis indicates local hyperestrogenism, justifying the use of progestogens and antiestrogens. Equal expression of genes encoding estrogen and progesterone receptors in patients with combined disease, as wells as high frequency of inflammatory changes in tissues and increased serum levels of inflammatory markers, proves the need for antiinflammatory therapy. Key words: adenomyosis, inflammation, steroid receptor genes, leiomyosarcoma, uterine fibroids, gene expression
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Jensen, Elwood V. "The Contribution of “Alternative Approaches” to Understanding Steroid Hormone Action." Molecular Endocrinology 19, no. 6 (June 1, 2005): 1439–42. http://dx.doi.org/10.1210/me.2005-0154.
Full textAbstract:
Abstract In the 47 yr since the first evidence for a steroid hormone receptor was presented at an international congress to an audience of five persons, the concept of “alternative approach” has played an important role in providing new understanding. By asking not what does an estrogenic hormone do to cellular processes in responsive tissues but what do these cells do to the hormone, it was shown that rat uterus contains a characteristic protein with which the hormone associates to promote growth. In the following decade, it was established that this substance is a true receptor, involved in hormonal action. Furthermore, estradiol was found not to undergo a chemical change as it exerts its effect. Finally, estrogenic action was established as a two-step process in which association with the hormone converts the receptor from an inactive to an active form that can bind tightly in the nucleus to modify transcription. These findings, obtained by studying the fate of the hormone itself, disproved the then accepted concept that estrogens interact with enzyme systems, and opened a new field of research. Soon various laboratories identified intracellular receptors for all classes of steroid hormones, the action of which involves a similar two-step process. Several laboratories then attempted, without success, to obtain antibodies to these receptors by conventional techniques. The unconventional approach of gradient ultracentrifugation, using radioactive estradiol as a marker for the receptor, gave a means of recognizing the soluble immune complexes formed with estrogen receptor and provided the first antibodies to any steroid hormone receptor, permitting its cloning. Finally, the knowledge that estrogens act through a receptor suggested that measuring the receptor content of an excised tumor specimen could identify, in advance, two thirds of the human breast cancers that are not estrogen dependent. These patients will not benefit from endocrine ablation or antiestrogen treatment and should be placed directly on chemotherapy. This is now standard clinical practice.
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Moehren, Udo, Maren Eckey, and Aria Baniahmad. "Gene repression by nuclear hormone receptors." Essays in Biochemistry 40 (June 1, 2004): 89–104. http://dx.doi.org/10.1042/bse0400089.
Full textAbstract:
Repression by nuclear hormone receptors (NHRs) plays an important role in development, immune response and cellular function. We review mechanisms of how NHRs act as repressors of gene transcription either by direct contact with basal transcription factors or through recruitment of cofactors and enzymic activities that modulate chromatin accessibility. We describe also the role and biochemical mechanism of the cognate hormone that switches a NHR from a transcriptional silencer into an activator. This includes data from crystal structure, functional receptor domain analyses and the role of co-repressors in chromatin modification and remodelling. Furthermore, the comparison of negative response elements with classical response elements unravels the role of co-repressors in this context. We also describe the inhibition of the nuclear factor kappaB and Jun/Fos pathway by NHRs, as well as the molecular mechanism of anti-hormone therapies. Anti-hormones are commonly used in breast and prostate cancer therapy to inhibit cancer proliferation through repression of the oestrogen or androgen receptor, respectively. Here we provide a comprehensive overview of the various mechanism of NHR repression.