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Volumn 29, Issue 1, 2005, Pages 63-77

Thyroid hormone availability and activity in avian species: A review

Author keywords

Deiodination; Fasting; Sulfation; TH; TR

Indexed keywords

DNA; LIOTHYRONINE; THYROID HORMONE; THYROID HORMONE RECEPTOR; THYROXINE;

EID: 20144368112     PISSN: 07397240     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.domaniend.2005.02.028     Document Type: Conference Paper
Times cited : (113)

References (91)
  • 1
    • 0002214636 scopus 로고
    • Importance of deiodination and conjugation in the hepatic metabolism of thyroid hormone
    • M.A. Greer Raven Press New York
    • T.J. Visser Importance of deiodination and conjugation in the hepatic metabolism of thyroid hormone M.A. Greer The thyroid gland 1990 Raven Press New York 255 283
    • (1990) The Thyroid Gland , pp. 255-283
    • Visser, T.J.1
  • 2
    • 0025093836 scopus 로고
    • Thyroid hormone regulates type I deiodinase messenger RNA in rat liver
    • M.J. Berry, A.-L. Kates, and P.R. Larsen Thyroid hormone regulates type I deiodinase messenger RNA in rat liver Mol Endocrinol 4 1990 743 748
    • (1990) Mol Endocrinol , vol.4 , pp. 743-748
    • Berry, M.J.1    Kates, A.-L.2    Larsen, P.R.3
  • 3
    • 0026648810 scopus 로고
    • Growth hormone acutely decreases type III iodothyronine deiodinase in chicken liver
    • V.M. Darras, L.R. Berghman, A. Vanderpooten, and E.R. Kühn Growth hormone acutely decreases type III iodothyronine deiodinase in chicken liver FEBS Lett 310 1992 5 8
    • (1992) FEBS Lett , vol.310 , pp. 5-8
    • Darras, V.M.1    Berghman, L.R.2    Vanderpooten, A.3    Kühn, E.R.4
  • 4
    • 0027352981 scopus 로고
    • Endogenous growth hormone controls high plasma levels of 3,3′,5-triiodothyronine (T3) in growing chickens by decreasing the T3-degrading type III deiodinase activity
    • V.M. Darras, P. Rudas, T.J. Visser, T.R. Hall, L.M. Huybrechts, and A. Vanderpooten Endogenous growth hormone controls high plasma levels of 3,3′,5-triiodothyronine (T3) in growing chickens by decreasing the T3-degrading type III deiodinase activity Domestic Anim Endocrinol 10 1993 55 65
    • (1993) Domestic Anim Endocrinol , vol.10 , pp. 55-65
    • Darras, V.M.1    Rudas, P.2    Visser, T.J.3    Hall, T.R.4    Huybrechts, L.M.5    Vanderpooten, A.6
  • 6
    • 0030298014 scopus 로고    scopus 로고
    • Evidence of a thyrotropin (TSH)-releasing activity of ovine corticotropin-releasing factor (oCRF) in the domestic fowl (Gallus domesticus)
    • K.L. Geris, S.P. Kotanen, L.R. Berghman, E.R. Kühn, and V.M. Darras Evidence of a thyrotropin (TSH)-releasing activity of ovine corticotropin- releasing factor (oCRF) in the domestic fowl (Gallus domesticus) Gen Comp Endocrinol 104 1996 139 146
    • (1996) Gen Comp Endocrinol , vol.104 , pp. 139-146
    • Geris, K.L.1    Kotanen, S.P.2    Berghman, L.R.3    Kühn, E.R.4    Darras, V.M.5
  • 7
    • 0033485518 scopus 로고    scopus 로고
    • Adrenal inhibition of corticotropin-releasing hormone-induced thyrotropin release: A comparative study in pre- and posthatch chicks
    • K.L. Geris, A. Laheye, L.R. Berghman, E.R. Kühn, and V.M. Darras Adrenal inhibition of corticotropin-releasing hormone-induced thyrotropin release: a comparative study in pre- and posthatch chicks J Exp Zool 284 1999 776 782
    • (1999) J Exp Zool , vol.284 , pp. 776-782
    • Geris, K.L.1    Laheye, A.2    Berghman, L.R.3    Kühn, E.R.4    Darras, V.M.5
  • 8
    • 0020638855 scopus 로고
    • Effects of glucocorticoids on circulating concentrations of thyroxine (T4) and triiodothyronine (T3) and on peripheral monodeiodination in pre- and post-hatching chickens
    • E. Decuypere, C.G. Scanes, and E.R. Kühn Effects of glucocorticoids on circulating concentrations of thyroxine (T4) and triiodothyronine (T3) and on peripheral monodeiodination in pre- and post-hatching chickens Horm Metab Res 15 1983 233 236
    • (1983) Horm Metab Res , vol.15 , pp. 233-236
    • Decuypere, E.1    Scanes, C.G.2    Kühn, E.R.3
  • 9
    • 0030298015 scopus 로고    scopus 로고
    • Plasma thyroid hormone levels and iodothyronine-deiodinase activity following an acute glucocorticoid challenge in embryonic compared with posthatch chickens
    • V.M. Darras, S.P. Kotanen, K.L. Geris, L.R. Berghman, and E.R. Kühn Plasma thyroid hormone levels and iodothyronine-deiodinase activity following an acute glucocorticoid challenge in embryonic compared with posthatch chickens Gen Comp Endocrinol 104 1996 203 212
    • (1996) Gen Comp Endocrinol , vol.104 , pp. 203-212
    • Darras, V.M.1    Kotanen, S.P.2    Geris, K.L.3    Berghman, L.R.4    Kühn, E.R.5
  • 10
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases
    • M.W.H. Coughtrie, S. Sharp, K. Maxwell, and N.P. Innes Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases Chem Biol Interact 109 1998 3 27
    • (1998) Chem Biol Interact , vol.109 , pp. 3-27
    • Coughtrie, M.W.H.1    Sharp, S.2    Maxwell, K.3    Innes, N.P.4
  • 12
    • 0041404965 scopus 로고    scopus 로고
    • Thyroid hormone sulfation in chicken and axolotl
    • G.E. Reyns, E.R. Kühn, and V.M. Darras Thyroid hormone sulfation in chicken and axolotl Netherlands J Zool 50 2000 329 341
    • (2000) Netherlands J Zool , vol.50 , pp. 329-341
    • Reyns, G.E.1    Kühn, E.R.2    Darras, V.M.3
  • 13
    • 0022382758 scopus 로고
    • Transcellular and transnuclear transport of 3,5,3′-triiodothyronine in isolated hepatocytes
    • A.D. Mooradian, H.L. Schwartz, C.N. Mariash, and J.H. Oppenheimer Transcellular and transnuclear transport of 3,5,3′-triiodothyronine in isolated hepatocytes Endocrinology 117 1985 2449 2456
    • (1985) Endocrinology , vol.117 , pp. 2449-2456
    • Mooradian, A.D.1    Schwartz, H.L.2    Mariash, C.N.3    Oppenheimer, J.H.4
  • 14
    • 0025073307 scopus 로고
    • The triiodothyronine carrier of rat erythrocytes: Asymmetry and mechanisms of trans-inhibition
    • J. Osty, Y. Zhou, F. Chantoux, J. Francon, and J.P. Blondeau The triiodothyronine carrier of rat erythrocytes: asymmetry and mechanisms of trans-inhibition Biochim Biophys Acta 1051 1990 46 51
    • (1990) Biochim Biophys Acta , vol.1051 , pp. 46-51
    • Osty, J.1    Zhou, Y.2    Chantoux, F.3    Francon, J.4    Blondeau, J.P.5
  • 15
    • 0025347918 scopus 로고
    • The transport of thyroxine into mouse neuroblastoma cells, NB41A3: The effect of L-system amino acids
    • M. Lakshmanan, E. Goncalves, G. Lessly, D. Foti, and J. Robbins The transport of thyroxine into mouse neuroblastoma cells, NB41A3: the effect of L-system amino acids Endocrinology 126 1990 3245 3250
    • (1990) Endocrinology , vol.126 , pp. 3245-3250
    • Lakshmanan, M.1    Goncalves, E.2    Lessly, G.3    Foti, D.4    Robbins, J.5
  • 18
    • 84995825964 scopus 로고
    • Thyroid hormone potentiates the antiviral action of interferon-γ in cultured human cells
    • H.Y. Lin, H.R. Thacore, P.J. Davis, and F.B. Davis Thyroid hormone potentiates the antiviral action of interferon-γ in cultured human cells J Clin Endocrinol Metab 79 1994 62 65
    • (1994) J Clin Endocrinol Metab , vol.79 , pp. 62-65
    • Lin, H.Y.1    Thacore, H.R.2    Davis, P.J.3    Davis, F.B.4
  • 19
    • 0019194637 scopus 로고
    • Rapid effect of triiodothyronine on the mitochondrial pathway in rat liver in vivo
    • K. Sterling, M.A. Brenner, and T. Sakurada Rapid effect of triiodothyronine on the mitochondrial pathway in rat liver in vivo Science 210 1980 340 342
    • (1980) Science , vol.210 , pp. 340-342
    • Sterling, K.1    Brenner, M.A.2    Sakurada, T.3
  • 20
    • 0028899694 scopus 로고
    • Thyroid hormone action: Effect of triiodothyronine on mitochondrial adenine nucleotide translocase in vivo and in vitro
    • K. Sterling, and M.A. Brenner Thyroid hormone action: effect of triiodothyronine on mitochondrial adenine nucleotide translocase in vivo and in vitro Metabolism 44 1995 193 199
    • (1995) Metabolism , vol.44 , pp. 193-199
    • Sterling, K.1    Brenner, M.A.2
  • 22
    • 0035252978 scopus 로고    scopus 로고
    • An uncoupling protein homologue putatively involved in facultative muscle thermogenesis in birds
    • S. Raimbault, S. Dridi, F. Denjean, J. Lachuer, E. Couplan, and F. Bouillaud An uncoupling protein homologue putatively involved in facultative muscle thermogenesis in birds Biochem J 353 2001 441 444
    • (2001) Biochem J , vol.353 , pp. 441-444
    • Raimbault, S.1    Dridi, S.2    Denjean, F.3    Lachuer, J.4    Couplan, E.5    Bouillaud, F.6
  • 23
    • 12244268660 scopus 로고    scopus 로고
    • Cold-induced enhancement of avian uncoupling protein expression, heat production, and triiodothyronine concentrations in broiler chicks
    • A. Collin, J. Buyse, P. van As, V.M. Darras, R.D. Malheiros, and V.M. Moraes Cold-induced enhancement of avian uncoupling protein expression, heat production, and triiodothyronine concentrations in broiler chicks Gen Comp Endocrinol 130 2003 70 77
    • (2003) Gen Comp Endocrinol , vol.130 , pp. 70-77
    • Collin, A.1    Buyse, J.2    Van As, P.3    Darras, V.M.4    Malheiros, R.D.5    Moraes, V.M.6
  • 25
    • 0033424373 scopus 로고    scopus 로고
    • Recent advances in the relationship between endocrine status and nutrition in chickens
    • L. Okumura, and K. Kita Recent advances in the relationship between endocrine status and nutrition in chickens Asian-Australian J Anim Sci 12 1999 1135 1141
    • (1999) Asian-Australian J Anim Sci , vol.12 , pp. 1135-1141
    • Okumura, L.1    Kita, K.2
  • 26
    • 0012551369 scopus 로고    scopus 로고
    • Nutritional regulation of the somatotrophic axis and intermediary metabolism in the chicken
    • A. Dawson C.M. Chaturvedi Narosa Publishing House New Dehli
    • J. Buyse, V.M. Darras, L. Vleurick, E.R. Kühn, and E. Decuypere Nutritional regulation of the somatotrophic axis and intermediary metabolism in the chicken A. Dawson CM. Chaturvedi Avian endocrinology 2001 Narosa Publishing House New Dehli 303 313
    • (2001) Avian Endocrinology , pp. 303-313
    • Buyse, J.1    Darras, V.M.2    Vleurick, L.3    Kühn, E.R.4    Decuypere, E.5
  • 27
    • 0036955485 scopus 로고    scopus 로고
    • Pre- and postprandial changes in plasma hormone and metabolite levels and hepatic deiodinase activities in meal-fed broiler chickens
    • J. Buyse, K. Janssens, S. Van der Geyten, P. Van As, E. Decuypere, and V.M. Darras Pre- and postprandial changes in plasma hormone and metabolite levels and hepatic deiodinase activities in meal-fed broiler chickens Br J Nutr 88 2002 641 653
    • (2002) Br J Nutr , vol.88 , pp. 641-653
    • Buyse, J.1    Janssens, K.2    Van Der Geyten, S.3    Van As, P.4    Decuypere, E.5    Darras, V.M.6
  • 28
    • 0033548632 scopus 로고    scopus 로고
    • The regulation of GH-dependent hormones and enzymes after feed restriction in dwarf and control chickens
    • E. Dewil, V.M. Darras, G.S. Spencer, T.J. Lauterio, and E. Decuypere The regulation of GH-dependent hormones and enzymes after feed restriction in dwarf and control chickens Life Sci 64 1999 1359 1371
    • (1999) Life Sci , vol.64 , pp. 1359-1371
    • Dewil, E.1    Darras, V.M.2    Spencer, G.S.3    Lauterio, T.J.4    Decuypere, E.5
  • 29
    • 0027737742 scopus 로고
    • Plasma growth hormone, insulin-like growth factor, insulin, and thyroid hormone association with body protein and fat accretion in steers undergoing compensatory gain after dietary energy restriction
    • J.M. Hayden, J.E. Williams, and R.J. Collier Plasma growth hormone, insulin-like growth factor, insulin, and thyroid hormone association with body protein and fat accretion in steers undergoing compensatory gain after dietary energy restriction J Anim Sci 71 1993 3327 3338
    • (1993) J Anim Sci , vol.71 , pp. 3327-3338
    • Hayden, J.M.1    Williams, J.E.2    Collier, R.J.3
  • 30
    • 0034153548 scopus 로고    scopus 로고
    • Food deprivation and feeding is associated with rapid and interdependent changes in the somatotropic and thyrothrophic axes
    • J. Buyse, E. Decuypere, V.M. Darras, L.M. Vleurick, E.R. Kühn, and J.D. Veldhuis Food deprivation and feeding is associated with rapid and interdependent changes in the somatotropic and thyrothrophic axes Br Poult Sci 41 2000 107 116
    • (2000) Br Poult Sci , vol.41 , pp. 107-116
    • Buyse, J.1    Decuypere, E.2    Darras, V.M.3    Vleurick, L.M.4    Kühn, E.R.5    Veldhuis, J.D.6
  • 31
    • 0026757250 scopus 로고
    • Ontogeny of type I and type III deiodinase activities in embryonic and posthatch chicks: Relationship with changes in plasma triiodothyronine and growth hormone levels
    • V.M. Darras, T.J. Visser, L.R. Berghman, and E.R. Kühn Ontogeny of type I and type III deiodinase activities in embryonic and posthatch chicks: Relationship with changes in plasma triiodothyronine and growth hormone levels Comp Biochem Physiol 103 1992 131 136
    • (1992) Comp Biochem Physiol , vol.103 , pp. 131-136
    • Darras, V.M.1    Visser, T.J.2    Berghman, L.R.3    Kühn, E.R.4
  • 32
    • 0029591447 scopus 로고
    • Partial food restriction increases hepatic inner ring deiodinating activity in the chicken and the rat
    • V.M. Darras, M. Cokelaere, E. Dewil, S. Arnouts, E. Decuypere, and E.R. Kühn Partial food restriction increases hepatic inner ring deiodinating activity in the chicken and the rat Gen Comp Endocrinol 100 1995 334 338
    • (1995) Gen Comp Endocrinol , vol.100 , pp. 334-338
    • Darras, V.M.1    Cokelaere, M.2    Dewil, E.3    Arnouts, S.4    Decuypere, E.5    Kühn, E.R.6
  • 34
    • 0025125736 scopus 로고
    • Ontogeny of the effect of purified chicken growth hormone on the liver 5′ monodeiodination activity in the chicken: Reversal of the activity after hatching
    • V.M. Darras, L.M. Huybrechts, L. Berghman, E.R. Kühn, and E. Decuypere Ontogeny of the effect of purified chicken growth hormone on the liver 5′ monodeiodination activity in the chicken: Reversal of the activity after hatching Gen Comp Endocrinol 77 1990 212 220
    • (1990) Gen Comp Endocrinol , vol.77 , pp. 212-220
    • Darras, V.M.1    Huybrechts, L.M.2    Berghman, L.3    Kühn, E.R.4    Decuypere, E.5
  • 36
    • 20144370020 scopus 로고    scopus 로고
    • New insights into the mechanism and actions of growth hormone (GH) in poultry
    • R. Vasilatos-Younken, X.H. Wang, Y. Zhou, J.R. Day, J.P. McMurtry, and R.W. Rosebrough New insights into the mechanism and actions of growth hormone (GH) in poultry B.A.S.E. 2 Special issue 1998 16 [abstract G2]
    • (1998) B.A.S.E. , vol.2 , Issue.SPECIAL ISSUE , pp. 16
    • Vasilatos-Younken, R.1    Wang, X.H.2    Zhou, Y.3    Day, J.R.4    McMurtry, J.P.5    Rosebrough, R.W.6
  • 37
    • 0025988639 scopus 로고
    • Thyrotropin-releasing hormone (TRH) is not thyrotropic but somatotropic in fed and starved adult chickens
    • E.R. Kuhn, M. Herremans, E. Dewil, A. Vanderpooten, P. Rudas, and T. Bartha Thyrotropin-releasing hormone (TRH) is not thyrotropic but somatotropic in fed and starved adult chickens Reprod Nutr Dev 31 1991 431 439
    • (1991) Reprod Nutr Dev , vol.31 , pp. 431-439
    • Kuhn, E.R.1    Herremans, M.2    Dewil, E.3    Vanderpooten, A.4    Rudas, P.5    Bartha, T.6
  • 38
    • 0025194083 scopus 로고
    • Central action of thyrotrophin-releasing hormone on growth hormone secretion in domestic fowl
    • S. Harvey, R.W. Lea, and C. Ahene Central action of thyrotrophin- releasing hormone on growth hormone secretion in domestic fowl J Endocrinol 126 1990 83 88
    • (1990) J Endocrinol , vol.126 , pp. 83-88
    • Harvey, S.1    Lea, R.W.2    Ahene, C.3
  • 39
    • 0027622510 scopus 로고
    • Study of the hepatic growth hormone (GH) receptor at different ages in chickens selected for a good feed conversion (FC) and a fast weight gain (GL)
    • A. Vanderpooten, W. Janssens, J. Buyse, F. Leenstra, L. Berghman, and E. Decuypere Study of the hepatic growth hormone (GH) receptor at different ages in chickens selected for a good feed conversion (FC) and a fast weight gain (GL) Domestic Anim Endocrinol 10 1993 199 206
    • (1993) Domestic Anim Endocrinol , vol.10 , pp. 199-206
    • Vanderpooten, A.1    Janssens, W.2    Buyse, J.3    Leenstra, F.4    Berghman, L.5    Decuypere, E.6
  • 40
    • 0035021772 scopus 로고    scopus 로고
    • Quantification of growth hormone receptor extra- and intracellular domain gene expression in chicken liver by quantitative competitive RT-PCR
    • P. Van As, W. Janssens, O.M. Onagbesan, V. Bruggeman, N. Buys, and J. Sanders Quantification of growth hormone receptor extra- and intracellular domain gene expression in chicken liver by quantitative competitive RT-PCR Gen Comp Endocrinol 122 2001 213 224
    • (2001) Gen Comp Endocrinol , vol.122 , pp. 213-224
    • Van As, P.1    Janssens, W.2    Onagbesan, O.M.3    Bruggeman, V.4    Buys, N.5    Sanders, J.6
  • 41
    • 0027220016 scopus 로고
    • A naturally occurring growth hormone receptor mutation: In vivo and in vitro evidence for the functional importance of the WS motif common to all members of the cytokine receptor superfamily
    • B. Duriez, M.L. Sobrier, P. Duquesnoy, M. Tixier-Boichard, E. Decuypere, and G. Coquerelle A naturally occurring growth hormone receptor mutation: in vivo and in vitro evidence for the functional importance of the WS motif common to all members of the cytokine receptor superfamily Mol Endocrinol 7 1993 806 814
    • (1993) Mol Endocrinol , vol.7 , pp. 806-814
    • Duriez, B.1    Sobrier, M.L.2    Duquesnoy, P.3    Tixier-Boichard, M.4    Decuypere, E.5    Coquerelle, G.6
  • 42
    • 0024824938 scopus 로고
    • Restricted feed intake influences thyroid hormone production and peripheral deiodination in chickens
    • T. Bartha, P. Rudas, S. Fekete, and G. Pethes Restricted feed intake influences thyroid hormone production and peripheral deiodination in chickens Acta Vet Hung 37 1989 241 246
    • (1989) Acta Vet Hung , vol.37 , pp. 241-246
    • Bartha, T.1    Rudas, P.2    Fekete, S.3    Pethes, G.4
  • 43
    • 0021084826 scopus 로고
    • Somatostatin inhibits rat hepatic T4-5′-deiodinase. the effect is independent of the associated hypoinsulinemia
    • L.A. Gavin, and M. Moeller Somatostatin inhibits rat hepatic T4-5′-deiodinase. The effect is independent of the associated hypoinsulinemia J Clin Invest 72 1983 2020 2030
    • (1983) J Clin Invest , vol.72 , pp. 2020-2030
    • Gavin, L.A.1    Moeller, M.2
  • 44
    • 0025724889 scopus 로고
    • Glucose regulation of growth hormone receptors in primary cultured rat hepatocytes
    • S. Niimi, T. Hayakawa, A. Tanaka, and A. Ichihara Glucose regulation of growth hormone receptors in primary cultured rat hepatocytes Endocrinology 129 1991 2734 2739
    • (1991) Endocrinology , vol.129 , pp. 2734-2739
    • Niimi, S.1    Hayakawa, T.2    Tanaka, A.3    Ichihara, A.4
  • 45
    • 0032975166 scopus 로고    scopus 로고
    • Glucose and amino acids interact with hormones to control expression of insulin-like growth factor-I and growth hormone receptor mRNA in cultured pig hepatocytes
    • J.M. Brameld, R.S. Gilmour, and P.J. Buttery Glucose and amino acids interact with hormones to control expression of insulin-like growth factor-I and growth hormone receptor mRNA in cultured pig hepatocytes J Nutr 129 1999 1298 1306
    • (1999) J Nutr , vol.129 , pp. 1298-1306
    • Brameld, J.M.1    Gilmour, R.S.2    Buttery, P.J.3
  • 46
    • 0032454409 scopus 로고    scopus 로고
    • Thyroid hormones are involved in insulin-like growth factor-I (IGF-I) production by stimulating hepatic growth hormone receptor (GHR) gene expression in the chicken
    • A. Tsukada, T. Ohkubo, K. Sakaguchi, M. Tanaka, K. Nakashima, and Y. Hayashida Thyroid hormones are involved in insulin-like growth factor-I (IGF-I) production by stimulating hepatic growth hormone receptor (GHR) gene expression in the chicken Growth Horm IGF Res 8 1998 235 242
    • (1998) Growth Horm IGF Res , vol.8 , pp. 235-242
    • Tsukada, A.1    Ohkubo, T.2    Sakaguchi, K.3    Tanaka, M.4    Nakashima, K.5    Hayashida, Y.6
  • 49
    • 0026694923 scopus 로고
    • Transport of 3,5,3′-triiodothyronine into the perfused rat liver and subsequent metabolism are inhibited by fasting
    • M. De Jong, R. Docter, H.J. Van Der Hoek, R.A. Vos, E.P. Krenning, and G. Hennemann Transport of 3,5,3′-triiodothyronine into the perfused rat liver and subsequent metabolism are inhibited by fasting Endocrinology 131 1992 463 470
    • (1992) Endocrinology , vol.131 , pp. 463-470
    • De Jong, M.1    Docter, R.2    Van Der Hoek, H.J.3    Vos, R.A.4    Krenning, E.P.5    Hennemann, G.6
  • 50
    • 0029780650 scopus 로고    scopus 로고
    • Different regulation of thyroid hormone transport in liver and pituitary: Its possible role in the maintenance of low T3 production during nonthyroidal illness and fasting in man
    • M.E. Everts, M. de Jong, C.F. Lim, R. Docter, E.P. Krenning, and T.J. Visser Different regulation of thyroid hormone transport in liver and pituitary: its possible role in the maintenance of low T3 production during nonthyroidal illness and fasting in man Thyroid 6 1996 359 368
    • (1996) Thyroid , vol.6 , pp. 359-368
    • Everts, M.E.1    De Jong, M.2    Lim, C.F.3    Docter, R.4    Krenning, E.P.5    Visser, T.J.6
  • 51
    • 0023025178 scopus 로고
    • The c-erbA protein is a high affinity receptor for thyroid hormone
    • J. Sap, A. Munoz, K. Damm, Y. Goldberg, J. Ghysdael, and A. Leutz The c-erbA protein is a high affinity receptor for thyroid hormone Nature 324 1986 635 640
    • (1986) Nature , vol.324 , pp. 635-640
    • Sap, J.1    Munoz, A.2    Damm, K.3    Goldberg, Y.4    Ghysdael, J.5    Leutz, A.6
  • 52
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • M. Beato, P. Herrlich, and G. Schutz Steroid hormone receptors: many actors in search of a plot Cell 83 1995 851 857
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schutz, G.3
  • 53
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • P.M. Yen Physiological and molecular basis of thyroid hormone action Physiol Rev 81 2001 1097 1142
    • (2001) Physiol Rev , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 54
    • 0023691049 scopus 로고
    • Identification of a rat c-erbAa-related protein which binds deoxyribonucleic acid and does not bind thyroid hormone
    • M.A. Lazar, R.A. Hodin, D.S. Darling, and W.W. Chin Identification of a rat c-erbAa-related protein which binds deoxyribonucleic acid and does not bind thyroid hormone Mol Endocrinol 2 1989 893 901
    • (1989) Mol Endocrinol , vol.2 , pp. 893-901
    • Lazar, M.A.1    Hodin, R.A.2    Darling, D.S.3    Chin, W.W.4
  • 55
    • 0024522826 scopus 로고
    • A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbAa transcriptional unit
    • M.A. Lazar, R.A. Hodin, D.S. Darling, and W.W. Chin A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbAa transcriptional unit Mol Cell Biol 9 1989 1128 1136
    • (1989) Mol Cell Biol , vol.9 , pp. 1128-1136
    • Lazar, M.A.1    Hodin, R.A.2    Darling, D.S.3    Chin, W.W.4
  • 56
    • 0024511936 scopus 로고
    • Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus
    • N. Miyajima, R. Horiuchi, Y. Shibuya, S. Fukushige, K. Matsubara, and K. Toyoshima Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus Cell 57 1989 31 39
    • (1989) Cell , vol.57 , pp. 31-39
    • Miyajima, N.1    Horiuchi, R.2    Shibuya, Y.3    Fukushige, S.4    Matsubara, K.5    Toyoshima, K.6
  • 57
    • 0024538351 scopus 로고
    • Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicing
    • R.J. Koenig, M.A. Lazar, R.A. Hodin, G.A. Brent, P.R. Larsen, and W.W. Chin Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicing Nature 337 1989 659 661
    • (1989) Nature , vol.337 , pp. 659-661
    • Koenig, R.J.1    Lazar, M.A.2    Hodin, R.A.3    Brent, G.A.4    Larsen, P.R.5    Chin, W.W.6
  • 58
    • 0025324403 scopus 로고
    • Gene expression from the c-erbAa/Rev-erbAa genomic locus: Potential regulation of alternative splicing by complementary transcripts from opposite DNA strands
    • M.A. Lazar, R.A. Hodin, G.R. Cardona, and W.W. Chin Gene expression from the c-erbAa/Rev-erbAa genomic locus: potential regulation of alternative splicing by complementary transcripts from opposite DNA strands J Biol Chem 265 1990 12859 12863
    • (1990) J Biol Chem , vol.265 , pp. 12859-12863
    • Lazar, M.A.1    Hodin, R.A.2    Cardona, G.R.3    Chin, W.W.4
  • 60
    • 0026471556 scopus 로고
    • Assignment of the beta-thyroid hormone receptor to 3,5,3′- triiodothyronine-dependent inhibition of transcription from thyrotropin- releasing hormone promoter in chick hypothalamic neurons
    • F. Lezoualc'h, A.H. Hassan, P. Giraud, J.P. Loeffler, S.L. Lee, and B.A. Demeneix Assignment of the beta-thyroid hormone receptor to 3,5,3′- triiodothyronine-dependent inhibition of transcription from thyrotropin- releasing hormone promoter in chick hypothalamic neurons Mol Endocrinol 6 1992 1797 1804
    • (1992) Mol Endocrinol , vol.6 , pp. 1797-1804
    • Lezoualc'H, F.1    Hassan, A.H.2    Giraud, P.3    Loeffler, J.P.4    Lee, S.L.5    Demeneix, B.A.6
  • 61
    • 0032720491 scopus 로고    scopus 로고
    • Divergent roles for thyroid hormone receptor beta isoforms in the endocrine axis and auditory system
    • E.D. Abel, M.E. Boers, C. Pazos-Moura, E. Moura, H. Kaulbach, and M. Zakaria Divergent roles for thyroid hormone receptor beta isoforms in the endocrine axis and auditory system J Clin Invest 104 1999 291 300
    • (1999) J Clin Invest , vol.104 , pp. 291-300
    • Abel, E.D.1    Boers, M.E.2    Pazos-Moura, C.3    Moura, E.4    Kaulbach, H.5    Zakaria, M.6
  • 62
    • 0030851716 scopus 로고    scopus 로고
    • A unique role of the beta-2 thyroid hormone receptor isoform in negative regulation by thyroid hormone, Mapping of a novel amino-terminal domain important for ligand-independent activation
    • M.F. Langlois, K. Zanger, T. Monden, J.D. Safer, A.N. Hollenberg, and F.E. Wondisford A unique role of the beta-2 thyroid hormone receptor isoform in negative regulation by thyroid hormone, Mapping of a novel amino-terminal domain important for ligand-independent activation J Biol Chem 272 1997 24927 24933
    • (1997) J Biol Chem , vol.272 , pp. 24927-24933
    • Langlois, M.F.1    Zanger, K.2    Monden, T.3    Safer, J.D.4    Hollenberg, A.N.5    Wondisford, F.E.6
  • 63
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • F. Rastinejad, T. Perlmann, R.M. Evans, and P.B. Sigler Structural determinants of nuclear receptor assembly on DNA direct repeats Nature 375 1995 203 211
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 64
    • 0025186267 scopus 로고
    • Interactions among a subfamily of nuclear hormone receptors: The regulatory zipper model
    • B.M. Forman, and H.H. Samuels Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model Mol Endocrinol 4 1990 1293 1301
    • (1990) Mol Endocrinol , vol.4 , pp. 1293-1301
    • Forman, B.M.1    Samuels, H.H.2
  • 65
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • R.M. Evans The steroid and thyroid hormone receptor superfamily Science 240 1988 889 895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 66
    • 0025260972 scopus 로고
    • In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
    • F.C. Dalman, R.J. Koenig, G.H. Perdew, E. Massa, and W.B. Pratt In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90 J Biol Chem 265 1990 3615 3618
    • (1990) J Biol Chem , vol.265 , pp. 3615-3618
    • Dalman, F.C.1    Koenig, R.J.2    Perdew, G.H.3    Massa, E.4    Pratt, W.B.5
  • 67
    • 0029097233 scopus 로고
    • A transcriptional corepressor that interacts with nuclear hormone receptors
    • J.D. Chen, and R.M. Evans A transcriptional corepressor that interacts with nuclear hormone receptors Nature 377 1995 454 457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 68
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear co-repressor
    • A.J. Horlein, A.M. Naar, T. Heinzel, J. Torchia, B. Gloss, and R. Kurokawa Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear co-repressor Nature 377 1995 397 404
    • (1995) Nature , vol.377 , pp. 397-404
    • Horlein, A.J.1    Naar, A.M.2    Heinzel, T.3    Torchia, J.4    Gloss, B.5    Kurokawa, R.6
  • 69
    • 0034695689 scopus 로고    scopus 로고
    • Thyroid hormone-independent interaction between the thyroid hormone receptor beta2 amino terminus and coactivators
    • C. Oberste-Berghaus, K. Zanger, K. Hashimoto, R.N. Cohen, A.N. Hollenberg, and F.E. Wondisford Thyroid hormone-independent interaction between the thyroid hormone receptor beta2 amino terminus and coactivators J Biol Chem 275 2000 1787 1792
    • (2000) J Biol Chem , vol.275 , pp. 1787-1792
    • Oberste-Berghaus, C.1    Zanger, K.2    Hashimoto, K.3    Cohen, R.N.4    Hollenberg, A.N.5    Wondisford, F.E.6
  • 70
    • 0025317798 scopus 로고
    • A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements
    • J. Burnside, D.S. Darling, and W.W. Chin A nuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements J Biol Chem 265 1990 2500 2504
    • (1990) J Biol Chem , vol.265 , pp. 2500-2504
    • Burnside, J.1    Darling, D.S.2    Chin, W.W.3
  • 71
    • 0024458145 scopus 로고
    • Identification of nuclear factors that enhance binding of the thyroid hormone receptor to a thyroid hormone response element
    • M. Murray, and H. Towle Identification of nuclear factors that enhance binding of the thyroid hormone receptor to a thyroid hormone response element Mol Endocrinol 3 1989 1434 1442
    • (1989) Mol Endocrinol , vol.3 , pp. 1434-1442
    • Murray, M.1    Towle, H.2
  • 72
    • 0025683224 scopus 로고
    • Thyroid hormone receptors form distinct nuclear protein-dependent and independent complexes with a thyroid hormone response element
    • M.A. Lazar, and T.J. Berrodin Thyroid hormone receptors form distinct nuclear protein-dependent and independent complexes with a thyroid hormone response element Mol Endocrinol 4 1990 1627 1635
    • (1990) Mol Endocrinol , vol.4 , pp. 1627-1635
    • Lazar, M.A.1    Berrodin, T.J.2
  • 73
    • 0027248681 scopus 로고
    • Characterization and tissue expression of multiple triiodothyronine (T3) receptor-auxiliary proteins (TRAPs) and their relationship to the retinoid X receptors (RXRs)
    • A. Sugawara, P.M. Yen, D.S. Darling, and W.W. Chin Characterization and tissue expression of multiple triiodothyronine (T3) receptor-auxiliary proteins (TRAPs) and their relationship to the retinoid X receptors (RXRs) Endocrinology 133 1993 965 971
    • (1993) Endocrinology , vol.133 , pp. 965-971
    • Sugawara, A.1    Yen, P.M.2    Darling, D.S.3    Chin, W.W.4
  • 74
    • 0026317212 scopus 로고
    • Dopaminergic and ligand-independent activation of steroid hormone receptors
    • R.F. Power, S. Main, J. Codina, O.M. Coneely, and B.W. O'Malley Dopaminergic and ligand-independent activation of steroid hormone receptors Science 254 1991 1636 1639
    • (1991) Science , vol.254 , pp. 1636-1639
    • Power, R.F.1    Main, S.2    Codina, J.3    Coneely, O.M.4    O'Malley, B.W.5
  • 75
    • 0026480387 scopus 로고
    • Kindred S thyroid hormone receptor is an active and constitutive silencer and a repressor for thyroid hormone and retinoic acid responses
    • A. Baniahmad, S.Y. Tsai, B.W. O'Malley, and M.J. Tsai Kindred S thyroid hormone receptor is an active and constitutive silencer and a repressor for thyroid hormone and retinoic acid responses Proc Natl Acad Sci USA 89 1992 10633 10637
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10633-10637
    • Baniahmad, A.1    Tsai, S.Y.2    O'Malley, B.W.3    Tsai, M.J.4
  • 76
    • 0024833706 scopus 로고
    • Mutations of the rat growth hormone promoter which increase and decrease response to thyroid hormone promoter which increase and decrease response to thyroid hormone define a consensus thyroid hormone response element
    • G.A. Brent, J.W. Harney, Y. Chen, R.L. Warne, D.D. Moore, and P.R. Larsen Mutations of the rat growth hormone promoter which increase and decrease response to thyroid hormone promoter which increase and decrease response to thyroid hormone define a consensus thyroid hormone response element Mol Endocrinol 3 1989 1996 2004
    • (1989) Mol Endocrinol , vol.3 , pp. 1996-2004
    • Brent, G.A.1    Harney, J.W.2    Chen, Y.3    Warne, R.L.4    Moore, D.D.5    Larsen, P.R.6
  • 77
    • 0027435514 scopus 로고
    • Interaction of human thyroid hormone receptor b with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone
    • A. Baniahmad, I. Ha, D. Reinberg, M.J. Tsai, S.Y. Tsai, and B.W. O'Malley Interaction of human thyroid hormone receptor b with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone Proc Natl Acad Sci USA 90 1993 8832 8836
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8832-8836
    • Baniahmad, A.1    Ha, I.2    Reinberg, D.3    Tsai, M.J.4    Tsai, S.Y.5    O'Malley, B.W.6
  • 78
    • 0028913188 scopus 로고
    • Tissue- and cell-specific distributions of protein interactions that interact with human b-thyroid hormone receptor
    • K.J. Petty Tissue- and cell-specific distributions of protein interactions that interact with human b-thyroid hormone receptor Mol Cell Endocrinol 108 1994 131 142
    • (1994) Mol Cell Endocrinol , vol.108 , pp. 131-142
    • Petty, K.J.1
  • 79
    • 0028970198 scopus 로고
    • Ligand modulates the interaction of thyroid hormone receptor beta with the basal transcription machinery
    • G.X. Tong, M.R. Tanen, and M.K. Bagchi Ligand modulates the interaction of thyroid hormone receptor beta with the basal transcription machinery J Biol Chem 270 1995 10601 10611
    • (1995) J Biol Chem , vol.270 , pp. 10601-10611
    • Tong, G.X.1    Tanen, M.R.2    Bagchi, M.K.3
  • 80
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
    • J.W. Lee, H.S. Choi, J. Gyuris, R. Brent, and D.D. Moore Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor Mol Endocrinol 9 1995 243 254
    • (1995) Mol Endocrinol , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4    Moore, D.D.5
  • 81
    • 0029657787 scopus 로고    scopus 로고
    • Identification of TRACs, a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors
    • S. Sande, and M.L. Privalsky Identification of TRACs, a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors Mol Endocrinol 10 1996 813 825
    • (1996) Mol Endocrinol , vol.10 , pp. 813-825
    • Sande, S.1    Privalsky, M.L.2
  • 82
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression
    • L. Alland, R. Muhle, H. Hou Jr., J. Potes, L. Chin, and N. Schreiber-Agus Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression Nature 387 1997 49 55
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou Jr., H.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6
  • 84
    • 0029060144 scopus 로고
    • Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon on their distinct amino terminal
    • A.N. Hollenberg, T. Monden, and F.E. Wondisford Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon on their distinct amino terminal J Biol Chem 270 1995 14272 14280
    • (1995) J Biol Chem , vol.270 , pp. 14272-14280
    • Hollenberg, A.N.1    Monden, T.2    Wondisford, F.E.3
  • 85
    • 0033562967 scopus 로고    scopus 로고
    • Mice devoid of all known thyroid hormone receptors are viable but exhibit disorders of the pituitary-thyroid axis, growth, and bone maturation
    • S. Gothe, Z. Wang, L. Ng, J.M. Kindblom, A.C. Barros, and C. Ohlsson Mice devoid of all known thyroid hormone receptors are viable but exhibit disorders of the pituitary-thyroid axis, growth, and bone maturation Genes Dev 13 1999 1329 1341
    • (1999) Genes Dev , vol.13 , pp. 1329-1341
    • Gothe, S.1    Wang, Z.2    Ng, L.3    Kindblom, J.M.4    Barros, A.C.5    Ohlsson, C.6
  • 86
    • 0029758906 scopus 로고    scopus 로고
    • Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
    • J.D. Fondell, J. Ge, and R.G. Roeder Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex Proc Natl Acad Sci USA 93 1996 8329 8333
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8329-8333
    • Fondell, J.D.1    Ge, J.2    Roeder, R.G.3
  • 87
    • 0033614417 scopus 로고    scopus 로고
    • Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
    • C. Rachez, B.D. Lemon, Z. Suldan, V. Bromleigh, M. Gamble, and A.M. Naar Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex Nature 398 1999 824 828
    • (1999) Nature , vol.398 , pp. 824-828
    • Rachez, C.1    Lemon, B.D.2    Suldan, Z.3    Bromleigh, V.4    Gamble, M.5    Naar, A.M.6
  • 88
    • 0032493455 scopus 로고    scopus 로고
    • The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
    • C.X. Yuan, M. Ito, J.D. Fondell, Z.Y. Fu, and R.G. Roeder The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion Proc Natl Acad Sci USA 95 1998 7939 7944
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7939-7944
    • Yuan, C.X.1    Ito, M.2    Fondell, J.D.3    Fu, Z.Y.4    Roeder, R.G.5
  • 89
    • 0025950381 scopus 로고
    • Cross-coupling of signal transduction pathways: Zinc finger meets leucine zipper
    • R. Schule, and R.M. Evans Cross-coupling of signal transduction pathways: zinc finger meets leucine zipper Trends Genet 7 1991 377 381
    • (1991) Trends Genet , vol.7 , pp. 377-381
    • Schule, R.1    Evans, R.M.2
  • 90
    • 0028037369 scopus 로고
    • Molecular mechanisms of dominant negative activity by nuclear hormone receptors
    • P.M. Yen, and W.W. Chin Molecular mechanisms of dominant negative activity by nuclear hormone receptors Mol Endocrinol 8 1994 1450 1454
    • (1994) Mol Endocrinol , vol.8 , pp. 1450-1454
    • Yen, P.M.1    Chin, W.W.2
  • 91
    • 0027461832 scopus 로고
    • Inhibition of estrogen-responsive gene activation by the retinoid X receptor beta: Evidence for multiple inhibitory pathways
    • J.H. Segars, M.S. Marks, S. Hirschfeld, P.H. Driggers, E. Martinez, and J.F. Grippo Inhibition of estrogen-responsive gene activation by the retinoid X receptor beta: evidence for multiple inhibitory pathways Mol Cell Biol 13 1993 2258 2268
    • (1993) Mol Cell Biol , vol.13 , pp. 2258-2268
    • Segars, J.H.1    Marks, M.S.2    Hirschfeld, S.3    Driggers, P.H.4    Martinez, E.5    Grippo, J.F.6


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