Cellular Action of Thyroid Hormone

作者: Rohit Sinha , Paul M Yen

DOI:

关键词: BiologyThyroid hormone receptor betaThyroid hormone receptorCell biologyTranscription factorPromoterCorepressorNuclear receptorEpigeneticsCoactivator

摘要: Thyroid hormones (THs) regulate growth, development, metabolism. This chapter aims to provide a comprehensive overview of the molecular and cellular mechanism(s) for intracellular signaling by TH. At level, THs bind thyroid hormone receptors (TRs) that are members nuclear receptor family. TRs act as ligand-activated transcription factors their cognate response elements (TREs) in promoters target genes. gene employing TR-interacting protein complexes containing coactivators (CoAs) or corepressors (CoRs). Coactivator corepressor include histone modifying enzymes known acetyltransferases (HATs) deacetylases (HDACs), respectively, induce epigenetic changes chromatin structure enhance repress transcriptional efficiency RNA polymerase on TH-responsive also can mediate effects indirectly binding other activating cell cascades. Additionally, emerging evidence suggests may membrane proteins than activate pathways. The important role TH metabolism, has spawned interest pharmacological use its analogs/metabolites treatment metabolic diseases such hypercholestronemia, hypertriglycerimia obesity, non-alcoholic fatty liver disease (NAFLD).

参考文章(211)
Michael K Hansen, Thomas M Connolly, Nuclear receptors as drug targets in obesity, dyslipidemia and atherosclerosis. Current opinion in investigational drugs. ,vol. 9, pp. 247- 255 ,(2008)
P.M. Yen, M. Ikeda, E.C. Wilcox, J.H. Brubaker, R.A. Spanjaard, A. Sugawara, W.W. Chin, Half-site arrangement of hybrid glucocorticoid and thyroid hormone response elements specifies thyroid hormone receptor complex binding to DNA and transcriptional activity. Journal of Biological Chemistry. ,vol. 269, pp. 12704- 12709 ,(1994) , 10.1016/S0021-9258(18)99933-3
D. Forrest, E. Hanebuth, R. J. Smeyne, N. Everds, C. L. Stewart, J. M. Wehner, T. Curran, Recessive resistance to thyroid hormone in mice lacking thyroid hormone receptor beta: evidence for tissue-specific modulation of receptor function. The EMBO Journal. ,vol. 15, pp. 3006- 3015 ,(1996) , 10.1002/J.1460-2075.1996.TB00664.X
P.M. Yen, D.S. Darling, R.L. Carter, M Forgione, P.K. Umeda, W.W. Chin, Triiodothyronine (T3) decreases binding to DNA by T3-receptor homodimers but not receptor-auxiliary protein heterodimers. Journal of Biological Chemistry. ,vol. 267, pp. 3565- 3568 ,(1992) , 10.1016/S0021-9258(19)50559-2
T Nagaya, J.L. Jameson, Distinct dimerization domains provide antagonist pathways for thyroid hormone receptor action. Journal of Biological Chemistry. ,vol. 268, pp. 24278- 24282 ,(1993) , 10.1016/S0021-9258(20)80522-5
J. J. Voegel, M. J. Heine, C. Zechel, P. Chambon, H. Gronemeyer, TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors The EMBO Journal. ,vol. 15, pp. 3667- 3675 ,(1996) , 10.1002/J.1460-2075.1996.TB00736.X
R.W. Katz, R.J. Koenig, Nonbiased identification of DNA sequences that bind thyroid hormone receptor alpha 1 with high affinity. Journal of Biological Chemistry. ,vol. 268, pp. 19392- 19397 ,(1993) , 10.1016/S0021-9258(19)36527-5
A.J. Perlman, F. Stanley, H.H. Samuels, Thyroid hormone nuclear receptor. Evidence for multimeric organization in chromatin. Journal of Biological Chemistry. ,vol. 257, pp. 930- 938 ,(1982) , 10.1016/S0021-9258(19)68289-X