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Tetsuya Tagami, Hiroyuki Yamamoto, Kenji Moriyama, Kuniko Sawai, Takeshi Usui, Akira Shimatsu, and Mitsuhide Naruse

Introduction A subgroup of the nuclear receptor superfamily that includes the receptors for thyroid hormone (TRs), retinoic acid (RARs), and vitamin D are known to form heterodimers with retinoid X receptors (RXR) to modulate the transcription of

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Changhua Shi, Qing Meng, and David W Wood

Introduction Thyroid hormone receptors (TRs) belong to the nuclear hormone receptor (NHR) superfamily, which includes a wide variety of transcriptional regulators that respond to various small-molecule hormones. TRs specifically regulate those genes

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Michelle Mohyi and Terry J Smith

immune tolerance to the thyrotropin receptor (TSHR) and the generation of activating antibodies against that protein. Further, hyperthyroidism, a central manifestation of GD, can be easily treated with commonly used and effective anti-thyroid medications

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Yali Ling, Feng Xu, Xuedi Xia, Dexing Dai, Ruoman Sun, and Zhongjian Xie

human vitamin D receptor gene associated with hypocalcemic rickets . Science 242 1702 – 1705 . ( ) 2849209 Ito Y Nikiforov YE Schlumberger M Vigneri R 2013 Increasing incidence of thyroid cancer

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Richard Keijzer, Piet-Jan E Blommaart, Wil T Labruyère, Jacqueline L M Vermeulen, Behrouz Zandieh Doulabi, Onno Bakker, Dick Tibboel, and Wouter H Lamers

alternative splicing, four thyroid hormone-binding receptors, namely TRα 1 and TRβ 1–3 ( Williams 2000 , Chassande 2003 ). In addition, several proteins, including TRα 2 , which do not bind thyroid hormone-response elements and/or thyroid hormones, are

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D C Thijssen-Timmer, M Platvoet-Ter Schiphorst, J Kwakkel, R Emter, A Kralli, W M Wiersinga, and O Bakker

Introduction Thyroid hormone receptor α (TRα) has an important role in the regulation of physiological functions, such as the control of body temperature and heart rate ( Wikstrom et al. 1998 ). The TRα gene encodes several

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R Núñez Miguel, J Sanders, D Y Chirgadze, J Furmaniak, and B Rees Smith

molecules that could block autoantibody binding to the receptor while allowing hormone binding. Declaration of interest RSR Ltd is a developer of in vitro medical diagnostics including kits for measuring thyroid autoantibodies. RNM, JS, JF, and BRS are

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Laëtitia Schneider, Claire El-Yazidi, Alexandra Dace, Marie Maraninchi, Richard Planells, Alain Margotat, and Janine Torresani

receptor (VDR) and the T 3 receptors (TRs), which belong to the steroid/thyroid-retinoid family of nuclear hormone receptors ( Mangelsdorf & Evans 1995 ). To date, three main functional TRs have been identified (TRα1, TRβ1 and TRβ2), which are encoded by

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O Chassande

Thyroid hormone (TH) is required for the development of vertebrates and exerts numerous homeostatic functions in adults. TH acts through nuclear receptors which control the transcription of target genes. Unliganded and liganded thyroid hormone receptors (TRs) have been shown to exert opposite effects on the transcription of target genes in vitro. However, the occurance of an aporeceptor activity in vivo and its potential physiological significance has not been clearly addressed. Several data generated using experimental hypothyroidism and thyrotoxicosis in wild type and TR knockout mice support the notion that apoTRs have an intrinsic activity in several tIssues. ApoTRs, and in particular TRalpha1, are predominant during the early stages of vertebrate development and must be turned into holoTRs for post-natal development to proceed normally. However, the absence of striking alterations of embryonic and fetal development in mice devoid of TRs indicates that apoTRs do not play a fundamental role. During development, as well as in adults, apoTRs rather appears as a system which increases the range of transcriptional responses to moderate variations of T3.

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M Montiel and E Jimenez

In this study we showed, for the first time, the existence of a moderate density of specific angiotensin II (Ang II) binding sites (Kd=3.9+/-1.7 nM and Bmax=467.2 130.0 fmol/mg protein) in plasma membrane preparations from rat thyroid gland. Reverse transcriptase/polymerase chain reactions, using primers based on the cloned AT1 and AT2 receptor subtypes, and pharmacological characterization, using the Ang II receptor subtype antagonists Losartan and PD 123319, revealed that these Ang II binding sites match with the AT1 receptor subtypes. To obtain more information on the molecular structure of this Ang II receptor, immunoblotting analyses were carried out using a polyclonal rabbit anti-AT1 antiserum. Western analysis of fresh plasma membrane preparations from thyroid tissue showed three prominent bands of approximately 60, 45 and 40 kDa which appear to be related to different degrees of glycosylation of the receptor molecule. The functional significance of the Ang II receptors in thyroid gland is currently not known. Nevertheless, since Ang II receptors play a pivotal role in the co-ordinated actions of the renin-angiotensin system (RAS), our findings support a reciprocal regulation of thyroid function by the RAS.