메뉴 건너뛰기




Volumn 149, Issue 9, 2008, Pages 4702-4709

Functional significance of a truncated thyroid receptor subtype lacking a hormone-binding domain in goldfish

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; DEIODINASE TYPE 3; LIOTHYRONINE; RECEPTOR SUBTYPE; SMALL INTERFERING RNA; THYROID HORMONE; THYROID HORMONE RECEPTOR ALPHA; THYROID HORMONE RECEPTOR ALPHA 1; THYROID HORMONE RECEPTOR ALPHA T; THYROID HORMONE RECEPTOR BETA; THYROXINE DEIODINASE; UNCLASSIFIED DRUG;

EID: 50449089994     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2008-0107     Document Type: Article
Times cited : (26)

References (43)
  • 1
    • 25144507562 scopus 로고    scopus 로고
    • Thyroid hormone deiodination in fish
    • Orozco A, Valverde RC 2005 Thyroid hormone deiodination in fish. Thyroid 15:799-813
    • (2005) Thyroid , vol.15 , pp. 799-813
    • Orozco, A.1    Valverde, R.C.2
  • 2
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM 1988 The steroid and thyroid hormone receptor superfamily. Science 240:889-895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 4
    • 0026714849 scopus 로고
    • Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein
    • Berrodin TJ, Marks MS, Ozato K, Linney E, Lazar MA 1992 Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein. Mol Endocrinol 6:1468-1478
    • (1992) Mol Endocrinol , vol.6 , pp. 1468-1478
    • Berrodin, T.J.1    Marks, M.S.2    Ozato, K.3    Linney, E.4    Lazar, M.A.5
  • 5
    • 0028307070 scopus 로고
    • A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor
    • Bogazzi F, Hudson LD, Nikodem VM 1994 A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor. J Biol Chem 269:11683-11686
    • (1994) J Biol Chem , vol.269 , pp. 11683-11686
    • Bogazzi, F.1    Hudson, L.D.2    Nikodem, V.M.3
  • 6
    • 0025317798 scopus 로고
    • Anuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements
    • Burnside J, Darling DS, Chin WW 1990 Anuclear factor that enhances binding of thyroid hormone receptors to thyroid hormone response elements. J Biol Chem 265:2500-2504
    • (1990) J Biol Chem , vol.265 , pp. 2500-2504
    • Burnside, J.1    Darling, D.S.2    Chin, W.W.3
  • 7
    • 0025936209 scopus 로고
    • Differential DNA binding by monomeric, homodimeric, and potentially heteromeric forms of the thyroid hormone receptor
    • Lazar MA, Berrodin TJ, Harding HP 1991 Differential DNA binding by monomeric, homodimeric, and potentially heteromeric forms of the thyroid hormone receptor. Mol Cell Biol 11:5005-5015
    • (1991) Mol Cell Biol , vol.11 , pp. 5005-5015
    • Lazar, M.A.1    Berrodin, T.J.2    Harding, H.P.3
  • 8
    • 11244280002 scopus 로고    scopus 로고
    • Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: Thyroid hormone receptor β-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites
    • Mengeling BJ, Pan F, Privalsky ML 2005 Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: thyroid hormone receptor β-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites. Mol Endocrinol 19:35-51
    • (2005) Mol Endocrinol , vol.19 , pp. 35-51
    • Mengeling, B.J.1    Pan, F.2    Privalsky, M.L.3
  • 9
    • 0033400343 scopus 로고    scopus 로고
    • Nuclear receptors: Coactivators, corepressors and chromatin remodeling in the control of transcription
    • Collingwood TN, Urnov FD, Wolffe AP 1999 Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription. J Mol Endocrinol 23:255-275
    • (1999) J Mol Endocrinol , vol.23 , pp. 255-275
    • Collingwood, T.N.1    Urnov, F.D.2    Wolffe, A.P.3
  • 10
    • 0032977486 scopus 로고    scopus 로고
    • Recent advances in understanding thyroid hormone receptor coregulators
    • Lee H, Yen PM 1999 Recent advances in understanding thyroid hormone receptor coregulators. J Biomed Sci 6:71-78
    • (1999) J Biomed Sci , vol.6 , pp. 71-78
    • Lee, H.1    Yen, P.M.2
  • 11
    • 0036018266 scopus 로고    scopus 로고
    • Mechanism of thyroid hormone action
    • Harvey CB, Williams GR 2002 Mechanism of thyroid hormone action. Thyroid 12:441-446
    • (2002) Thyroid , vol.12 , pp. 441-446
    • Harvey, C.B.1    Williams, G.R.2
  • 12
    • 0027416347 scopus 로고
    • Thyroid hormone receptors: Multiple forms, multiple possibilities
    • Lazar MA 1993 Thyroid hormone receptors: multiple forms, multiple possibilities. Endocr Rev 14:184-193
    • (1993) Endocr Rev , vol.14 , pp. 184-193
    • Lazar, M.A.1
  • 13
    • 0031475026 scopus 로고    scopus 로고
    • Identification of transcripts initiated from an internal promoter in the c-erbA α locus that encode inhibitors of retinoic acid receptor-α and triiodothyronine receptor activities
    • Chassande O, Fraichard A, Gauthier K, Flamant F, Legrand C, Savatier P, Laudet V, Samarut J 1997 Identification of transcripts initiated from an internal promoter in the c-erbA α locus that encode inhibitors of retinoic acid receptor-α and triiodothyronine receptor activities. Mol Endocrinol 11:1278-1290
    • (1997) Mol Endocrinol , vol.11 , pp. 1278-1290
    • Chassande, O.1    Fraichard, A.2    Gauthier, K.3    Flamant, F.4    Legrand, C.5    Savatier, P.6    Laudet, V.7    Samarut, J.8
  • 16
    • 0023691049 scopus 로고
    • Identification of a rat c-erbA α-related protein which binds deoxyribonucleic acid but does not bind thyroid hormone
    • Lazar MA, Hodin RA, Darling DS, Chin WW 1988 Identification of a rat c-erbA α-related protein which binds deoxyribonucleic acid but does not bind thyroid hormone. Mol Endocrinol 2:893-901
    • (1988) Mol Endocrinol , vol.2 , pp. 893-901
    • Lazar, M.A.1    Hodin, R.A.2    Darling, D.S.3    Chin, W.W.4
  • 17
    • 0006850898 scopus 로고
    • Alternative splicing generates messages encoding rat c-erbA proteins that do not bind thyroid hormone
    • Mitsuhashi T, Tennyson GE, Nikodem VM 1988 Alternative splicing generates messages encoding rat c-erbA proteins that do not bind thyroid hormone. Proc Natl Acad Sci USA 85:5804-5808
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5804-5808
    • Mitsuhashi, T.1    Tennyson, G.E.2    Nikodem, V.M.3
  • 20
    • 0033762445 scopus 로고    scopus 로고
    • Cloning and characterization of two novel thyroid hormone receptor β isoforms
    • Williams GR 2000 Cloning and characterization of two novel thyroid hormone receptor β isoforms. Mol Cell Biol 20:8329-8342
    • (2000) Mol Cell Biol , vol.20 , pp. 8329-8342
    • Williams, G.R.1
  • 21
    • 33749262129 scopus 로고    scopus 로고
    • Isolation of the alligator (Alligator mississippiensis) thyroid hormone receptor α and β transcripts and their responsiveness to thyroid stimulating hormone
    • Helbing CC, Crump K, Bailey CM, Kohno S, Veldhoen N, Bryan T, Bermudez D, Guillette Jr LJ 2006 Isolation of the alligator (Alligator mississippiensis) thyroid hormone receptor α and β transcripts and their responsiveness to thyroid stimulating hormone. Gen Comp Endocrinol 149:141-150
    • (2006) Gen Comp Endocrinol , vol.149 , pp. 141-150
    • Helbing, C.C.1    Crump, K.2    Bailey, C.M.3    Kohno, S.4    Veldhoen, N.5    Bryan, T.6    Bermudez, D.7    Guillette Jr, L.J.8
  • 22
    • 33745386929 scopus 로고    scopus 로고
    • Molecular characterization and sex-related seasonal expression of thyroid receptor subtypes in goldfish
    • Nelson ER, Habibi HR 2006 Molecular characterization and sex-related seasonal expression of thyroid receptor subtypes in goldfish. Mol Cell Endocrinol 253:83-95
    • (2006) Mol Cell Endocrinol , vol.253 , pp. 83-95
    • Nelson, E.R.1    Habibi, H.R.2
  • 23
    • 34547894673 scopus 로고    scopus 로고
    • Homologous regulation of estrogen receptor subtypes in goldfish (Carassius auratus)
    • Nelson ER, Wiehler WB, Cole WC, Habibi HR 2007 Homologous regulation of estrogen receptor subtypes in goldfish (Carassius auratus). Mol Reprod Dev 74:1105-1112
    • (2007) Mol Reprod Dev , vol.74 , pp. 1105-1112
    • Nelson, E.R.1    Wiehler, W.B.2    Cole, W.C.3    Habibi, H.R.4
  • 24
    • 0023281221 scopus 로고
    • Increased gonadotropin levels in goldfish do not result in alterations in circulating thyroid hormone levels
    • MacKenzie DS, Sokolowska M, Peter RE, Breton B 1987 Increased gonadotropin levels in goldfish do not result in alterations in circulating thyroid hormone levels. Gen Comp Endocrinol 67:202-213
    • (1987) Gen Comp Endocrinol , vol.67 , pp. 202-213
    • MacKenzie, D.S.1    Sokolowska, M.2    Peter, R.E.3    Breton, B.4
  • 25
    • 0344177520 scopus 로고    scopus 로고
    • Seasonal changes in mRNA levels of gonadotropin and thyrotropin subunits in the goldfish, Carassius auratus
    • Sohn YC, Yoshiura Y, Kobayashi M, Aida K 1999 Seasonal changes in mRNA levels of gonadotropin and thyrotropin subunits in the goldfish, Carassius auratus. Gen Comp Endocrinol 113:436-444
    • (1999) Gen Comp Endocrinol , vol.113 , pp. 436-444
    • Sohn, Y.C.1    Yoshiura, Y.2    Kobayashi, M.3    Aida, K.4
  • 26
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung M, Brosch G, Kolle D, Scherf H, Gerhauser C, Loidl P 1999 Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J Med Chem 42:4669-4679
    • (1999) J Med Chem , vol.42 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 28
    • 10744229917 scopus 로고    scopus 로고
    • Remiszewski SW, Sambucetti LC, Bair KW, Bontempo J, Cesarz D, Chandramouli N, Chen R, Cheung M, Cornell-Kennon S, Dean K, Diamantidis G, France D, Green MA, Howell KL, Kashi R, Kwon P, Lassota P, Martin MS, Mou Y, Perez LB, Sharma S, Smith T, Sorensen E, Taplin F, Trogani N, Versace R, Walker H, Weltchek-Engler S, Wood A, Wu A, Atadja P 2003 N-hydroxy-3-phenyl- 2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2- hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]2-propenamide (NVP-LAQ824). J Med Chem 46:4609-4624
    • Remiszewski SW, Sambucetti LC, Bair KW, Bontempo J, Cesarz D, Chandramouli N, Chen R, Cheung M, Cornell-Kennon S, Dean K, Diamantidis G, France D, Green MA, Howell KL, Kashi R, Kwon P, Lassota P, Martin MS, Mou Y, Perez LB, Sharma S, Smith T, Sorensen E, Taplin F, Trogani N, Versace R, Walker H, Weltchek-Engler S, Wood A, Wu A, Atadja P 2003 N-hydroxy-3-phenyl- 2-propenamides as novel inhibitors of human histone deacetylase with in vivo antitumor activity: discovery of (2E)-N-hydroxy-3-[4-[[(2- hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]2-propenamide (NVP-LAQ824). J Med Chem 46:4609-4624
  • 30
    • 0029118148 scopus 로고
    • The type III 5-deiodinase in Rana catesbeiana tadpoles is encoded by a thyroid hormone-responsive gene
    • Becker KB, Schneider MJ, Davey JC, Galton VA 1995 The type III 5-deiodinase in Rana catesbeiana tadpoles is encoded by a thyroid hormone-responsive gene. Endocrinology 136:4424-4431
    • (1995) Endocrinology , vol.136 , pp. 4424-4431
    • Becker, K.B.1    Schneider, M.J.2    Davey, J.C.3    Galton, V.A.4
  • 31
    • 28844470877 scopus 로고    scopus 로고
    • A cDNA for a putative type III deiodinase in the trout (Oncorhynchus mykiss): Influence of holding conditions and thyroid hormone treatment on its hepatic expression
    • Bres O, Plohman JC, Eales JG 2006 A cDNA for a putative type III deiodinase in the trout (Oncorhynchus mykiss): influence of holding conditions and thyroid hormone treatment on its hepatic expression. Gen Comp Endocrinol 145:92-100
    • (2006) Gen Comp Endocrinol , vol.145 , pp. 92-100
    • Bres, O.1    Plohman, J.C.2    Eales, J.G.3
  • 32
    • 0000622698 scopus 로고    scopus 로고
    • Effects of experimental hypo-and hyperthyroidism on iodothyronine deiodinases in Nile tilapia oreochromis niloticus
    • Mol K, van der Geyton S, Kuhn E, Darras V 1999 Effects of experimental hypo-and hyperthyroidism on iodothyronine deiodinases in Nile tilapia oreochromis niloticus. Fish Physiol Biochem 20:201-207
    • (1999) Fish Physiol Biochem , vol.20 , pp. 201-207
    • Mol, K.1    van der Geyton, S.2    Kuhn, E.3    Darras, V.4
  • 33
    • 0036191639 scopus 로고    scopus 로고
    • Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases
    • Bianco AC, Salvatore D, Gereben B, Berry MJ, Larsen PR 2002 Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr Rev 23:38-89
    • (2002) Endocr Rev , vol.23 , pp. 38-89
    • Bianco, A.C.1    Salvatore, D.2    Gereben, B.3    Berry, M.J.4    Larsen, P.R.5
  • 35
    • 0024538351 scopus 로고
    • Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicing
    • Koenig RJ, Lazar MA, Hodin RA, Brent GA, Larsen PR, Chin WW, Moore DD 1989 Inhibition of thyroid hormone action by a non-hormone binding c-erbA protein generated by alternative mRNA splicing. Nature 337:659-661
    • (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    Moore, D.D.7
  • 36
    • 0345485236 scopus 로고
    • Human carboxyl-terminal variant of α-type c-erbA inhibits trans-activation by thyroid hormone receptors without binding thyroid hormone
    • Lazar MA, Hodin RA, Chin WW 1989 Human carboxyl-terminal variant of α-type c-erbA inhibits trans-activation by thyroid hormone receptors without binding thyroid hormone. Proc Natl Acad Sci USA 86:7771-7774
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7771-7774
    • Lazar, M.A.1    Hodin, R.A.2    Chin, W.W.3
  • 37
    • 0027384527 scopus 로고
    • Dominant negative activity of an endogenous thyroid hormone receptor variant (α2) is due to competition for binding sites on target genes
    • Katz D, Lazar MA 1993 Dominant negative activity of an endogenous thyroid hormone receptor variant (α2) is due to competition for binding sites on target genes. J Biol Chem 268:20904-20910
    • (1993) J Biol Chem , vol.268 , pp. 20904-20910
    • Katz, D.1    Lazar, M.A.2
  • 38
    • 0027431085 scopus 로고
    • Distinct dimerization domains provide antagonist pathways for thyroid hormone receptor action
    • Nagaya T, Jameson JL 1993 Distinct dimerization domains provide antagonist pathways for thyroid hormone receptor action. J Biol Chem 268:24278-24282
    • (1993) J Biol Chem , vol.268 , pp. 24278-24282
    • Nagaya, T.1    Jameson, J.L.2
  • 39
    • 0028819201 scopus 로고
    • The dominant negative effect of thyroid hormone receptor splicing variant α2 does not require binding to a thyroid response element
    • Liu RT, Suzuki S, Miyamoto T, Takeda T, Ozata M, DeGroot LJ 1995 The dominant negative effect of thyroid hormone receptor splicing variant α2 does not require binding to a thyroid response element. Mol Endocrinol 9:86-95
    • (1995) Mol Endocrinol , vol.9 , pp. 86-95
    • Liu, R.T.1    Suzuki, S.2    Miyamoto, T.3    Takeda, T.4    Ozata, M.5    DeGroot, L.J.6
  • 40
    • 0029854557 scopus 로고    scopus 로고
    • Thyroid hormone receptor variant α2. Role of the ninth heptad in DNA binding, heterodimerization with retinoid X receptors, and dominant negative activity
    • Yang YZ, Burgos-Trinidad M, Wu Y, Koenig RJ 1996 Thyroid hormone receptor variant α2. Role of the ninth heptad in DNA binding, heterodimerization with retinoid X receptors, and dominant negative activity. J Biol Chem 271:28235-28242
    • (1996) J Biol Chem , vol.271 , pp. 28235-28242
    • Yang, Y.Z.1    Burgos-Trinidad, M.2    Wu, Y.3    Koenig, R.J.4
  • 42
    • 0026665641 scopus 로고
    • The unique C-termini of the thyroid hormone receptor variant, c-erbA α2, and thyroid hormone receptor α1 mediate different DNA-binding and heterodimerization properties
    • Katz D, Berrodin TJ, Lazar MA 1992 The unique C-termini of the thyroid hormone receptor variant, c-erbA α2, and thyroid hormone receptor α1 mediate different DNA-binding and heterodimerization properties. Mol Endocrinol 6:805-814
    • (1992) Mol Endocrinol , vol.6 , pp. 805-814
    • Katz, D.1    Berrodin, T.J.2    Lazar, M.A.3
  • 43
    • 0029060144 scopus 로고
    • Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini
    • Hollenberg AN, Monden T, Wondisford FE 1995 Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini. J Biol Chem 270:14274-14280
    • (1995) J Biol Chem , vol.270 , pp. 14274-14280
    • Hollenberg, A.N.1    Monden, T.2    Wondisford, F.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.