메뉴 건너뛰기




Volumn 151, Issue 1-2, 1999, Pages 103-119

Local activation and inactivation of thyroid hormones: The deiodinase family

Author keywords

Binding; Deiodinases; Euthyroid sick syndrome; Low T3 syndrome; Non thyroidal illness; Selenium; Thyroid hormone; Transport and metabolism of thyroid hormones; Uptake

Indexed keywords

CELL NUCLEUS RECEPTOR; IODIDE PEROXIDASE; LEVOTHYROXINE; LIOTHYRONINE; SELENIUM; SELENOCYSTEINE; THYROID HORMONE; TRANSCRIPTION FACTOR;

EID: 0142214992     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(99)00040-4     Document Type: Article
Times cited : (298)

References (152)
  • 1
    • 15444342300 scopus 로고    scopus 로고
    • Molecular characterization and tissue distribution of a new organic anion transporter subtype (oatp3) that transports thyroid hormones and taurocholate and comparison with oatp2
    • Abe T., Kakyo M., Sakagami H., Tokui T., Nishio T., Tanemoto M., Nomura H., Hebert H., Matsuno S., Kondo H., Yawo H. Molecular characterization and tissue distribution of a new organic anion transporter subtype (oatp3) that transports thyroid hormones and taurocholate and comparison with oatp2. J. Biol. Chem. 273:1998;22395-22401.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22395-22401
    • Abe, T.1    Kakyo, M.2    Sakagami, H.3    Tokui, T.4    Nishio, T.5    Tanemoto, M.6    Nomura, H.7    Hebert, H.8    Matsuno, S.9    Kondo, H.10    Yawo, H.11
  • 2
    • 0028981175 scopus 로고
    • 17β-hydroxysteroid dehydrogenase: Isoenzymes and mutations
    • Anderson S. 17β-hydroxysteroid dehydrogenase: isoenzymes and mutations. J. Endocrinol. 147:1995;197-200.
    • (1995) J. Endocrinol. , vol.147 , pp. 197-200
    • Anderson, S.1
  • 4
    • 0025688215 scopus 로고
    • Hepatic iodothyronine 5′-deiodinase. The role of selenium
    • Arthur J.R., Nicol F., Beckett G.J. Hepatic iodothyronine 5′-deiodinase. The role of selenium. Biochem. J. 272:1990;537-540.
    • (1990) Biochem. J. , vol.272 , pp. 537-540
    • Arthur, J.R.1    Nicol, F.2    Beckett, G.J.3
  • 5
    • 0018743101 scopus 로고
    • Re-examination of the subcellular localization of thyroxine-5′-deiodination in rat liver
    • Auf dem Brinke D., Hesch R.D., Köhrle J. Re-examination of the subcellular localization of thyroxine-5′-deiodination in rat liver. Biochem. J. 180:1979;273-279.
    • (1979) Biochem. J. , vol.180 , pp. 273-279
    • Auf Dem Brinke, D.1    Hesch, R.D.2    Köhrle, J.3
  • 6
    • 0018380256 scopus 로고
    • Observations on the factors that control the generation of triiodothyronine from thyroxine in rat liver and nature of the defect induced by fasting
    • Balsam A., Ingbar S.H. Observations on the factors that control the generation of triiodothyronine from thyroxine in rat liver and nature of the defect induced by fasting. J. Clin. Invest. 63:1979;1145-1156.
    • (1979) J. Clin. Invest. , vol.63 , pp. 1145-1156
    • Balsam, A.1    Ingbar, S.H.2
  • 9
    • 0030786396 scopus 로고    scopus 로고
    • 3,5-Di-iodo-L-thyronine stimulates type I 5'- deiodinase activity in rat anterior pituitaries in vivo and in reaggregate cultures and GH3 cells in vitro
    • Baur A., Bauer K., Jarry H., Köhrle J. 3,5-Di-iodo-L-thyronine stimulates type I 5'- deiodinase activity in rat anterior pituitaries in vivo and in reaggregate cultures and GH3 cells in vitro. Endocrinology. 138:1997;3242-3248.
    • (1997) Endocrinology , vol.138 , pp. 3242-3248
    • Baur, A.1    Bauer, K.2    Jarry, H.3    Köhrle, J.4
  • 10
    • 0345260489 scopus 로고    scopus 로고
    • GX cells: A human cell model for investigations of immuno-endocrine interactions at the pituitary level
    • 1-1 (Abstract)
    • Baur, A., Köhrle, J., 1997. GX cells: a human cell model for investigations of immuno-endocrine interactions at the pituitary level. Exp. Clin. Endocrinol. Diabetes 105, 1-1 (Abstract).
    • (1997) Exp. Clin. Endocrinol. Diabetes , vol.105
    • Baur, A.1    Köhrle, J.2
  • 11
    • 0345280814 scopus 로고    scopus 로고
    • Type I 5′-deiodinase is stimulated by iodothyronines and involved in thyroid hormone metabolism in human somatomammotroph GX cells
    • (in press)
    • Baur, A., Köhrle, J., 1999. Type I 5′-deiodinase is stimulated by iodothyronines and involved in thyroid hormone metabolism in human somatomammotroph GX cells. Eur. J. Endocrinol. 140 (in press).
    • (1999) Eur. J. Endocrinol. , vol.140
    • Baur, A.1    Köhrle, J.2
  • 12
    • 0031007408 scopus 로고    scopus 로고
    • The type 2 and type 3 iodothyronine deiodinases play important roles in coordinating development in Rana catesbeiana tadpoles
    • Becker K.B., Stephens K.C., Davey J.C., Schneider M.J., Galton Y.A. The type 2 and type 3 iodothyronine deiodinases play important roles in coordinating development in Rana catesbeiana tadpoles. Endocrinology. 138:1997;2989-2997.
    • (1997) Endocrinology , vol.138 , pp. 2989-2997
    • Becker, K.B.1    Stephens, K.C.2    Davey, J.C.3    Schneider, M.J.4    Galton, Y.A.5
  • 13
    • 0028948990 scopus 로고
    • Differential control of type-I iodothyronine deiodinase expression by the activation of the cyclic AMP and phosphoinositol signalling pathways in cultured human thyrocytes
    • Beech S.G., Walker S.W., Arthur J.R., Lee D., Beckett G.J. Differential control of type-I iodothyronine deiodinase expression by the activation of the cyclic AMP and phosphoinositol signalling pathways in cultured human thyrocytes. J. Mol. Endocrinol. 14:1995;171-177.
    • (1995) J. Mol. Endocrinol. , vol.14 , pp. 171-177
    • Beech, S.G.1    Walker, S.W.2    Arthur, J.R.3    Lee, D.4    Beckett, G.J.5
  • 15
    • 0028886971 scopus 로고
    • Thyroid hormones and brain development
    • Bernal J., Nunez J. Thyroid hormones and brain development. Eur. J. Endocrinol. 133:1995;390-398.
    • (1995) Eur. J. Endocrinol. , vol.133 , pp. 390-398
    • Bernal, J.1    Nunez, J.2
  • 16
    • 0026778835 scopus 로고
    • Identification of essential histidine residues in rat type I iodothyronine deiodinase
    • Berry M.J. Identification of essential histidine residues in rat type I iodothyronine deiodinase. J. Biol. Chem. 267:1992;18055-18059.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18055-18059
    • Berry, M.J.1
  • 17
    • 0025979337 scopus 로고
    • Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
    • Berry M.J., Banu L., Larsen P.R. Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature. 349:1991;438-440.
    • (1991) Nature , vol.349 , pp. 438-440
    • Berry, M.J.1    Banu, L.2    Larsen, P.R.3
  • 18
    • 0026334925 scopus 로고
    • Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase
    • Berry M.J., Kieffer J.D., Harney J.W., Larsen P.R. Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase. J. Biol. Chem. 266:1991;14155-14158.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14155-14158
    • Berry, M.J.1    Kieffer, J.D.2    Harney, J.W.3    Larsen, P.R.4
  • 19
    • 0027856032 scopus 로고
    • Modification of thermogenic capacity in neonatal pigs by changes in thyroid status during late gestation
    • Berthon D., Herpin P., Duchamp C., Dauncey M.J., Le Dividich J. Modification of thermogenic capacity in neonatal pigs by changes in thyroid status during late gestation. J. Dev. Physiol. 19:1993;253-261.
    • (1993) J. Dev. Physiol. , vol.19 , pp. 253-261
    • Berthon, D.1    Herpin, P.2    Duchamp, C.3    Dauncey, M.J.4    Le Dividich, J.5
  • 20
    • 0029966360 scopus 로고    scopus 로고
    • Interactive effects of thermal environment and energy intake on thyroid hormone metabolism in newborn pigs
    • Berthon D., Herpin P., Le Dividich J., Dauncey M.J. Interactive effects of thermal environment and energy intake on thyroid hormone metabolism in newborn pigs. Biol. Neonate. 69:1996;51-59.
    • (1996) Biol. Neonate , vol.69 , pp. 51-59
    • Berthon, D.1    Herpin, P.2    Le Dividich, J.3    Dauncey, M.J.4
  • 21
    • 0025281913 scopus 로고
    • Iodothyronine deiodinase activities in FRTL-5 cells: Predominance of type I 5′-deiodinase
    • Borges M., Ingbar S.H., Silva J.E. Iodothyronine deiodinase activities in FRTL-5 cells: predominance of type I 5′-deiodinase. Endocrinology. 126:1990;3059-3068.
    • (1990) Endocrinology , vol.126 , pp. 3059-3068
    • Borges, M.1    Ingbar, S.H.2    Silva, J.E.3
  • 22
    • 0032509416 scopus 로고    scopus 로고
    • The 3′-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence element
    • Buettner C., Harney J.W., Larsen P.R. The 3′-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence element. J. Biol. Chem. 273:1998;33374-33378.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33374-33378
    • Buettner, C.1    Harney, J.W.2    Larsen, P.R.3
  • 23
    • 0030691866 scopus 로고    scopus 로고
    • Thyroid hormones inhibit type 2 iodothyronine deiodinase in the rat cerebral cortex by both pre- And posttranslational mechanisms
    • Burmeister L.A., Pachucki J., Germain D.L.S. Thyroid hormones inhibit type 2 iodothyronine deiodinase in the rat cerebral cortex by both pre- and posttranslational mechanisms. Endocrinology. 138:1997;5231-5237.
    • (1997) Endocrinology , vol.138 , pp. 5231-5237
    • Burmeister, L.A.1    Pachucki, J.2    Germain, D.L.S.3
  • 28
    • 0030699924 scopus 로고    scopus 로고
    • Steroid metabolism in the mammalian brain: 5-alpha-reduction and aromatization
    • Celotti F., Negri-Cesi P., Poletti A. Steroid metabolism in the mammalian brain: 5-alpha-reduction and aromatization. Brain Res. Bull. 44:1997;365-375.
    • (1997) Brain Res. Bull. , vol.44 , pp. 365-375
    • Celotti, F.1    Negri-Cesi, P.2    Poletti, A.3
  • 30
    • 0027199677 scopus 로고
    • Stimulatory effect of thyroid hormone on growth hormone gene expression in a human pituitary cell line
    • Chomczynski P., Soszynski P.A., Frohman L.A. Stimulatory effect of thyroid hormone on growth hormone gene expression in a human pituitary cell line. J. Clin. Endocrinol. Metab. 77:1993;281-285.
    • (1993) J. Clin. Endocrinol. Metab. , vol.77 , pp. 281-285
    • Chomczynski, P.1    Soszynski, P.A.2    Frohman, L.A.3
  • 31
    • 0002968699 scopus 로고    scopus 로고
    • Nature, source, and relative significance of circulating thyroid hormones
    • In: Braverman, L.E., Utiger R.D. (Eds.), Lippincott-Raven, Philadelphia
    • Chopra, I.J., 1996. Nature, source, and relative significance of circulating thyroid hormones. In: Braverman, L.E., Utiger R.D. (Eds.), Werner and Ingbar's The Thyroid, 7th ed. (7). Lippincott-Raven, Philadelphia, pp. 111-124.
    • (1996) Werner and Ingbar's the Thyroid, 7th Ed. , Issue.7 , pp. 111-124
    • Chopra, I.J.1
  • 32
    • 0032566541 scopus 로고    scopus 로고
    • Conserved cysteines in the type 1 deiodinase selenoprotein are not essential for catalytic activity
    • Croteau W., Bodwell J.E., Richardson J.M., St. Germain D.L. Conserved cysteines in the type 1 deiodinase selenoprotein are not essential for catalytic activity. J. Biol. Chem. 273:1998;25230-25236.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25230-25236
    • Croteau, W.1    Bodwell, J.E.2    Richardson, J.M.3    St. Germain, D.L.4
  • 34
    • 0001436225 scopus 로고
    • Cellular actions of thyroid hormones
    • In: Braverman, L.E., Utiger, R.D. (Eds.), Lippincott-Raven, Philadelphia
    • Davis, P.J., 1991. Cellular actions of thyroid hormones. In: Braverman, L.E., Utiger, R.D. (Eds.), Werner and Ingbar's The Thyroid, 6 ed. (9). Lippincott-Raven, Philadelphia, pp. 190-203.
    • (1991) Werner and Ingbar's the Thyroid, 6 Ed. , Issue.9 , pp. 190-203
    • Davis, P.J.1
  • 35
    • 0029907826 scopus 로고    scopus 로고
    • Nongenomic actions of thyroid hormone
    • Davis P.J., Davis F.B. Nongenomic actions of thyroid hormone. Thyroid. 6:1996;497-504.
    • (1996) Thyroid , vol.6 , pp. 497-504
    • Davis, P.J.1    Davis, F.B.2
  • 37
    • 0028903150 scopus 로고
    • The deiodination of thyroxine to triiodothyronine in the testes of patients with prostate cancer
    • Dutkiewicz S., Witeska A., Nauman A. The deiodination of thyroxine to triiodothyronine in the testes of patients with prostate cancer. Int. Urol. Nephrol. 27:1995;81-85.
    • (1995) Int. Urol. Nephrol. , vol.27 , pp. 81-85
    • Dutkiewicz, S.1    Witeska, A.2    Nauman, A.3
  • 38
    • 0029938145 scopus 로고    scopus 로고
    • Only the combined treatment with thyroxine and triiodothyronine ensures euthyroidism in all tissues of the thyroidectomized rat
    • Escobar-Morreale H.F., Escobar del Rey F., Obregón M.J., Morreale de Escobar G. Only the combined treatment with thyroxine and triiodothyronine ensures euthyroidism in all tissues of the thyroidectomized rat. Endocrinology. 137:1996;2490-2502.
    • (1996) Endocrinology , vol.137 , pp. 2490-2502
    • Escobar-Morreale, H.F.1    Escobar Del Rey, F.2    Obregón, M.J.3    Morreale De Escobar, G.4
  • 39
    • 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
    • Everts M.E., De Jong M., Lim C.-F., Docter R., Krenning E.P., Visser T.J., Hennemann G. 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    Hennemann, G.7
  • 41
    • 0029968909 scopus 로고    scopus 로고
    • Thyroid hormone deiodination pathways in brain and liver of rainbow trout, Oncorhynchus mykiss
    • Frith S.D., Eales J.G. Thyroid hormone deiodination pathways in brain and liver of rainbow trout, Oncorhynchus mykiss. Gen. Comp. Endocrinol. 101:1996;323-332.
    • (1996) Gen. Comp. Endocrinol. , vol.101 , pp. 323-332
    • Frith, S.D.1    Eales, J.G.2
  • 42
    • 0030782757 scopus 로고    scopus 로고
    • Cloning of human 25-hydroxy-vitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1
    • Fu G.K., Lin D., Zhang M.Y., Bikle D.D., Shackleton C.H., Miller W.L., Portale A.A. Cloning of human 25-hydroxy-vitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol. Endocrinol. 11:1997;1961-1970.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1961-1970
    • Fu, G.K.1    Lin, D.2    Zhang, M.Y.3    Bikle, D.D.4    Shackleton, C.H.5    Miller, W.L.6    Portale, A.A.7
  • 43
    • 0027967516 scopus 로고
    • Expression of type II thyroxine 5′-deiodinase from rat harderian gland in Xenopus laevis oocytes
    • Garcia Macias J.F., Molinero P., Guerrero J.M., Osuna C. Expression of type II thyroxine 5′-deiodinase from rat harderian gland in Xenopus laevis oocytes. FEBS Lett. 354:1994;110-112.
    • (1994) FEBS Lett. , vol.354 , pp. 110-112
    • Garcia Macias, J.F.1    Molinero, P.2    Guerrero, J.M.3    Osuna, C.4
  • 44
    • 0031635492 scopus 로고    scopus 로고
    • Molecular cloning of (25-OH-D)-1 alpha-hydroxylase: An approach to the understanding of vitamin D pseudo-deficiency
    • Glorieux F.H., St. Arnaud R. Molecular cloning of (25-OH-D)-1 alpha-hydroxylase: an approach to the understanding of vitamin D pseudo-deficiency. Recent Prog. Horm. Res. 53:1998;341-349.
    • (1998) Recent Prog. Horm. Res. , vol.53 , pp. 341-349
    • Glorieux, F.H.1    St. Arnaud, R.2
  • 46
    • 0023132959 scopus 로고
    • Brain cortex reverse triiodothyronine (rT3) and triiodothyronine concentrations under steady state infusions of thyroxine and rT3
    • Goumaz M.O., Kaiser C.A., Burger A.G. Brain cortex reverse triiodothyronine (rT3) and triiodothyronine concentrations under steady state infusions of thyroxine and rT3. Endocrinology. 120:1987;1590-1596.
    • (1987) Endocrinology , vol.120 , pp. 1590-1596
    • Goumaz, M.O.1    Kaiser, C.A.2    Burger, A.G.3
  • 47
    • 0030928654 scopus 로고    scopus 로고
    • Regional expression of 5′-deiodinase II in the rat brain as studied by in situ hybridization
    • Guadano-Ferraz A., Bernal J. Regional expression of 5′-deiodinase II in the rat brain as studied by in situ hybridization. Proc. Natl. Acad. Sci. U.S.A. 94:1997;10391-10396.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10391-10396
    • Guadano-Ferraz, A.1    Bernal, J.2
  • 48
    • 0030191799 scopus 로고    scopus 로고
    • T3 potentiates the adrenergic stimulation of type II 5′-deiodinase activity in cultured rat brown adipocytes
    • Hernandez A., Obregon M.J. T3 potentiates the adrenergic stimulation of type II 5′-deiodinase activity in cultured rat brown adipocytes. Am. J. Physiol. 271:1996;E15-E23.
    • (1996) Am. J. Physiol. , vol.271
    • Hernandez, A.1    Obregon, M.J.2
  • 49
    • 0032192485 scopus 로고    scopus 로고
    • Localization of the type 3 iodothyronine deiodinase (DIO3) gene to human chromosome 14q32 and mouse chromosome 12F1
    • Hernandez A., Park J.P., Lyon G.J., Mohandas T.K., St. Germain D.L. Localization of the type 3 iodothyronine deiodinase (DIO3) gene to human chromosome 14q32 and mouse chromosome 12F1. Genomics. 53:1998;119-121.
    • (1998) Genomics , vol.53 , pp. 119-121
    • Hernandez, A.1    Park, J.P.2    Lyon, G.J.3    Mohandas, T.K.4    St. Germain, D.L.5
  • 50
    • 0029331734 scopus 로고
    • Does thermoregulatory feeding occur in newborn infants? A novel view of the role of brown adipose tissue thermogenesis in control of food intake
    • Himms Hagen J. Does thermoregulatory feeding occur in newborn infants? A novel view of the role of brown adipose tissue thermogenesis in control of food intake. Obes. Res. 3:1995;361-369.
    • (1995) Obes. Res. , vol.3 , pp. 361-369
    • Himms Hagen, J.1
  • 51
    • 0029112354 scopus 로고
    • Defects in the synthesis and metabolism of vitamin D
    • Holick M.F. Defects in the synthesis and metabolism of vitamin D. Exp. Clin. Endocrinol. Diabetes. 103:1995;219-227.
    • (1995) Exp. Clin. Endocrinol. Diabetes , vol.103 , pp. 219-227
    • Holick, M.F.1
  • 55
    • 0011223439 scopus 로고
    • Identification of a T3 responsive element in the upstream regulatory region of the human type I 5′-deiodinase gene
    • (Abstract)
    • Jakobs, T., Schmutzler, C., Köhrle, J., 1995. Identification of a T3 responsive element in the upstream regulatory region of the human type I 5′-deiodinase gene. Thyroid 5, S130 (Abstract).
    • (1995) Thyroid , vol.5
    • Jakobs, T.1    Schmutzler, C.2    Köhrle, J.3
  • 56
    • 0030748116 scopus 로고    scopus 로고
    • The promotor of the human type I 5′-deiodinase gene: Mapping of the transcription start site and identification of a DR+4 thyroid hormone responsive element
    • Jakobs T., Schmutzler C., Meissner J., Köhrle J. The promotor of the human type I 5′-deiodinase gene: mapping of the transcription start site and identification of a DR+4 thyroid hormone responsive element. Eur. J. Biochem. 247:1997;288-297.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 288-297
    • Jakobs, T.1    Schmutzler, C.2    Meissner, J.3    Köhrle, J.4
  • 57
    • 0031172520 scopus 로고    scopus 로고
    • Structure of the human type I iodothyronine 5′-deiodinase gene and localization to chromosome 1p32-p33
    • Jakobs T.C., Koehler M.R., Schmutzler C., Glaser F., Schmid M., Köhrle J. Structure of the human type I iodothyronine 5′-deiodinase gene and localization to chromosome 1p32-p33. Genomics. 42:1997;361-363.
    • (1997) Genomics , vol.42 , pp. 361-363
    • Jakobs, T.C.1    Koehler, M.R.2    Schmutzler, C.3    Glaser, F.4    Schmid, M.5    Köhrle, J.6
  • 58
    • 0029805887 scopus 로고    scopus 로고
    • An oxysterol signalling pathway mediated by the nuclear receptor LXRα
    • Janowski B.A., Willy P.J., Devi T.R., Falck J.R., Mangelsdorf D.J. An oxysterol signalling pathway mediated by the nuclear receptor LXRα Nature. 383:1996;728-731.
    • (1996) Nature , vol.383 , pp. 728-731
    • Janowski, B.A.1    Willy, P.J.2    Devi, T.R.3    Falck, J.R.4    Mangelsdorf, D.J.5
  • 59
    • 0022466739 scopus 로고
    • In vivo inhibition of the 5′-deiodinase type II in brain cortex and pituitary by reverse triiodothyronine
    • Kaiser C.A., Goumaz M.O., Burger A.G. In vivo inhibition of the 5′-deiodinase type II in brain cortex and pituitary by reverse triiodothyronine. Endocrinology. 119:1986;762-770.
    • (1986) Endocrinology , vol.119 , pp. 762-770
    • Kaiser, C.A.1    Goumaz, M.O.2    Burger, A.G.3
  • 60
    • 0023924631 scopus 로고
    • Human epidermal keratinocytes in culture convert thyroxine to 3,5,3′-triiodothyronine by type II iodothyronine deiodination: A novel endocrine function of the skin
    • Kaplan M.M., Pan C.Y., Gordon P.R., Lee J.K., Gilchrest B.A. Human epidermal keratinocytes in culture convert thyroxine to 3,5,3′-triiodothyronine by type II iodothyronine deiodination: a novel endocrine function of the skin. J. Clin. Endocrinol. Metab. 66:1988;815-822.
    • (1988) J. Clin. Endocrinol. Metab. , vol.66 , pp. 815-822
    • Kaplan, M.M.1    Pan, C.Y.2    Gordon, P.R.3    Lee, J.K.4    Gilchrest, B.A.5
  • 61
    • 0019775180 scopus 로고
    • Autoregulation of 3,3′,5′-triiodothyronine production by rat liver microsomes
    • Kaminski T., Köhrle J., Ködding R., Hesch R.D. Autoregulation of 3,3′,5′-triiodothyronine production by rat liver microsomes. Acta Endocrinol. 98:1981;240-245.
    • (1981) Acta Endocrinol. , vol.98 , pp. 240-245
    • Kaminski, T.1    Köhrle, J.2    Ködding, R.3    Hesch, R.D.4
  • 62
    • 0031785516 scopus 로고    scopus 로고
    • Studies of the hormonal regulation of type 2 5′-iodothyronine deiodinase messenger ribonucleic aacid in pituitary tumor cells using semiquantitative reverse transcription polymerase reaction
    • Kim S.W., Harney J.W., Larsen P.R. Studies of the hormonal regulation of type 2 5′-iodothyronine deiodinase messenger ribonucleic aacid in pituitary tumor cells using semiquantitative reverse transcription polymerase reaction. Endocrinology. 139:1998;4895-4905.
    • (1998) Endocrinology , vol.139 , pp. 4895-4905
    • Kim, S.W.1    Harney, J.W.2    Larsen, P.R.3
  • 63
    • 0021281413 scopus 로고
    • Regulation of thyroxine 5′-deiodinase activity by 3,5,3′-triiodothyronine in cultured anterior pituitary cells
    • Koenig R.J., Leonard J.L., Senator D., Rappaport N., Watson A., Larsen P.R. Regulation of thyroxine 5′-deiodinase activity by 3,5,3′-triiodothyronine in cultured anterior pituitary cells. Endocrinology. 115:1984;324-329.
    • (1984) Endocrinology , vol.115 , pp. 324-329
    • Koenig, R.J.1    Leonard, J.L.2    Senator, D.3    Rappaport, N.4    Watson, A.5    Larsen, P.R.6
  • 64
    • 0024991755 scopus 로고
    • Thyrotropin (TSH) action on thyroid hormone deiodination and secretion: One aspect of thyrotropin regulation of thyroid cell biology
    • Köhrle J. Thyrotropin (TSH) action on thyroid hormone deiodination and secretion: one aspect of thyrotropin regulation of thyroid cell biology. Horm. Metab. Res. 23(Suppl.):1990;18-28.
    • (1990) Horm. Metab. Res. , vol.23 , Issue.SUPPL. , pp. 18-28
    • Köhrle, J.1
  • 65
    • 0029696059 scopus 로고    scopus 로고
    • Thyroid hormone deiodinases: A selenoenzyme family acting as gate keepers to thyroid hormone action
    • Köhrle J. Thyroid hormone deiodinases: a selenoenzyme family acting as gate keepers to thyroid hormone action. Acta Med. Austriaca. 23:1996;17-30.
    • (1996) Acta Med. Austriaca , vol.23 , pp. 17-30
    • Köhrle, J.1
  • 66
    • 0030637205 scopus 로고    scopus 로고
    • Thyroid carcinoma: Interrelationships between local thyroid hormone metabolism by the type I 5′-deiodinase and the expression of thyroid hormone receptors and other thyroid-specific (de-)differentiation markers
    • Köhrle J. Thyroid carcinoma: interrelationships between local thyroid hormone metabolism by the type I 5′-deiodinase and the expression of thyroid hormone receptors and other thyroid-specific (de-)differentiation markers. Curr. Top. Pathol. 91:1997;83-116.
    • (1997) Curr. Top. Pathol. , vol.91 , pp. 83-116
    • Köhrle, J.1
  • 67
    • 0038501459 scopus 로고    scopus 로고
    • The trace element selenium and the thyroid gland
    • (in press)
    • Köhrle, J., 1999. The trace element selenium and the thyroid gland. Biochimie (in press).
    • (1999) Biochimie
    • Köhrle, J.1
  • 68
    • 0022967239 scopus 로고
    • Rat liver iodothyronine monodeiodinase: Evaluation of the iodothyronine binding site
    • Köhrle J., Auf'mkolk M., Rokos H., Hesch R.D., Cody V. Rat liver iodothyronine monodeiodinase: evaluation of the iodothyronine binding site. J. Biol. Chem. 261:1986;11613-11622.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11613-11622
    • Köhrle, J.1    Auf'mkolk, M.2    Rokos, H.3    Hesch, R.D.4    Cody, V.5
  • 69
    • 0021728078 scopus 로고
    • Biochemical characteristics of iodothyronine monodeiodination by rat liver microsomes: The interaction between iodothyronine substrate analogues and the ligand binding site of iodothyronine deiodinase resembles that of the TBPA-iodothyronine ligand binding site Horm.
    • Köhrle, J., Hesch, R.D., 1984. Biochemical characteristics of iodothyronine monodeiodination by rat liver microsomes: the interaction between iodothyronine substrate analogues and the ligand binding site of iodothyronine deiodinase resembles that of the TBPA-iodothyronine ligand binding site Horm. Metab. Res. 14 (Suppl. Ser.), 42-55.
    • (1984) Metab. Res. , vol.14 , Issue.SUPPL. SER. , pp. 42-55
    • Köhrle, J.1    Hesch, R.D.2
  • 70
  • 71
    • 4243635583 scopus 로고    scopus 로고
    • Genetics of iodothyronine deiodinase enzymes
    • (Abstract)
    • Köhrle, J., Jakobs, T.C., Schmutzler, C., 1997. Genetics of iodothyronine deiodinase enzymes. Thyroid 7, 687-687 (Abstract).
    • (1997) Thyroid , vol.7 , pp. 687-687
    • Köhrle, J.1    Jakobs, T.C.2    Schmutzler, C.3
  • 73
    • 0028918580 scopus 로고
    • Rapid stimulation of type I 5′-deiodinase in rat pituitaries by 3,3′,5-triiodo-L-thyronine
    • Köhrle J., Schomburg L., Drescher S., Fekete E., Bauer K. Rapid stimulation of type I 5′-deiodinase in rat pituitaries by 3,3′,5-triiodo-L-thyronine. Mol. Cell. Endocrinol. 108:1995;17-21.
    • (1995) Mol. Cell. Endocrinol. , vol.108 , pp. 17-21
    • Köhrle, J.1    Schomburg, L.2    Drescher, S.3    Fekete, E.4    Bauer, K.5
  • 74
    • 0027971390 scopus 로고
    • Membrane iodothyronine transporters part I: Review of physiology
    • Kragie L. Membrane iodothyronine transporters part I: review of physiology. Endocr. Res. 20:1994;319-341.
    • (1994) Endocr. Res. , vol.20 , pp. 319-341
    • Kragie, L.1
  • 75
    • 0029884539 scopus 로고    scopus 로고
    • Membrane iodothyronine transporters part II: Review of protein biochemistry
    • Kragie L. Membrane iodothyronine transporters part II: review of protein biochemistry. Endocr. Res. 22:1996;95-119.
    • (1996) Endocr. Res. , vol.22 , pp. 95-119
    • Kragie, L.1
  • 77
    • 0019754949 scopus 로고
    • Relationships between circulating and intracellular thyroid hormones: Physiological and clinical implications
    • Larsen P.R., Silva J.E., Kaplan M.M. Relationships between circulating and intracellular thyroid hormones: physiological and clinical implications. Endocr. Rev. 2:1981;87-102.
    • (1981) Endocr. Rev. , vol.2 , pp. 87-102
    • Larsen, P.R.1    Silva, J.E.2    Kaplan, M.M.3
  • 78
    • 0018816299 scopus 로고
    • Iodothyronine release from the perfused canine thyroid
    • Laurberg P. Iodothyronine release from the perfused canine thyroid. Kopenhagen Acta Endocrinol. Suppl. 236:1980;1-50.
    • (1980) Kopenhagen Acta Endocrinol. Suppl. , vol.236 , pp. 1-50
    • Laurberg, P.1
  • 79
    • 0027319115 scopus 로고
    • The type I iodothyronine 5′-deiodinase messenger ribonucleic acid is localized to the S3 segment of the rat kidney proximal tubule
    • Lee W.S., Berry M.J., Hediger M.A., Larsen P.R. The type I iodothyronine 5′-deiodinase messenger ribonucleic acid is localized to the S3 segment of the rat kidney proximal tubule. Endocrinology. 132:1993;2136-2140.
    • (1993) Endocrinology , vol.132 , pp. 2136-2140
    • Lee, W.S.1    Berry, M.J.2    Hediger, M.A.3    Larsen, P.R.4
  • 80
    • 0002227815 scopus 로고
    • Identification and structure analysis of iodothyronine deiodinases
    • In: Greer, M.A. (Ed.), Raven Press, New York
    • Leonard, J.L., 1991. Identification and structure analysis of iodothyronine deiodinases. In: Greer, M.A. (Ed.), The Thyroid Gland (9). Raven Press, New York, pp. 285-321.
    • (1991) The Thyroid Gland , Issue.9 , pp. 285-321
    • Leonard, J.L.1
  • 81
    • 0025875494 scopus 로고
    • Localization of type I iodothyronine 5′ deiodinase to the basolateral plasma membrane of rat kidney and LLC-PK1 renal cortical cells
    • Leonard J.L., Ekenbarger D.M., Frank S.J., Farwell A.P., Köhrle J. Localization of type I iodothyronine 5′ deiodinase to the basolateral plasma membrane of rat kidney and LLC-PK1 renal cortical cells. J. Biol. Chem. 266:1991;11262-11269.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11262-11269
    • Leonard, J.L.1    Ekenbarger, D.M.2    Frank, S.J.3    Farwell, A.P.4    Köhrle, J.5
  • 82
    • 0030945125 scopus 로고    scopus 로고
    • Thyroid hormone-regulated actin polymerization in brain
    • Leonard J.L., Farwell A.P. Thyroid hormone-regulated actin polymerization in brain. Thyroid. 7:1997;147-151.
    • (1997) Thyroid , vol.7 , pp. 147-151
    • Leonard, J.L.1    Farwell, A.P.2
  • 83
    • 0001628146 scopus 로고    scopus 로고
    • Intracellular pathways of iodothyronine metabolism
    • In: Braverman, L.E., Utiger, R.D. (Eds.), Lippincott-Raven, Philadelphia
    • Leonard, J.L., Köhrle, J., 1996. Intracellular pathways of iodothyronine metabolism. In: Braverman, L.E., Utiger, R.D. (Eds.), Werner and Ingbar's The Thyroid: A Fundamental and Clinical Text, 7th ed. (8). Lippincott-Raven, Philadelphia, pp. 125-161.
    • (1996) Werner and Ingbar's the Thyroid: A Fundamental and Clinical Text, 7th Ed. , Issue.8 , pp. 125-161
    • Leonard, J.L.1    Köhrle, J.2
  • 86
    • 0024440499 scopus 로고
    • Alterations in 3,3′,5′-triiodothyronine metabolism in response to propylthiouracil, dexamethasone, and thyroxine administration in man
    • LoPresti J.S., Eigen A., Kaptein E., Anderson K.P., Spencer C.A., Nicoloff J.T. Alterations in 3,3′,5′-triiodothyronine metabolism in response to propylthiouracil, dexamethasone, and thyroxine administration in man. J. Clin. Invest. 84:1989;1650-1656.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1650-1656
    • Lopresti, J.S.1    Eigen, A.2    Kaptein, E.3    Anderson, K.P.4    Spencer, C.A.5    Nicoloff, J.T.6
  • 87
    • 0029095653 scopus 로고
    • Structural and functional differences in the dio 1 gene in mice with inherited type 1 deiodinase deficiency
    • Maia A.L., Berry M.J., Sabbag R., Harney J.W., Larsen P.R. Structural and functional differences in the dio 1 gene in mice with inherited type 1 deiodinase deficiency. Mol. Endocrinol. 9:1995;969-980.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 969-980
    • Maia, A.L.1    Berry, M.J.2    Sabbag, R.3    Harney, J.W.4    Larsen, P.R.5
  • 88
    • 0030944473 scopus 로고    scopus 로고
    • Euthyroid sick syndrome: An overview
    • McIver B., Gorman C.A. Euthyroid sick syndrome: an overview. Thyroid. 7:1997;125-132.
    • (1997) Thyroid , vol.7 , pp. 125-132
    • McIver, B.1    Gorman, C.A.2
  • 90
    • 0027138088 scopus 로고
    • Effects of thyroid and glucocorticoid hormones on the level of messenger ribonucleic acid for iodothyronine type I 5′-deiodinase in rat primary hepatocyte cultures grown as spheroids
    • Menjo M., Murata Y., Fujii T., Nimura Y., Seo H. Effects of thyroid and glucocorticoid hormones on the level of messenger ribonucleic acid for iodothyronine type I 5′-deiodinase in rat primary hepatocyte cultures grown as spheroids. Endocrinology. 133:1993;2984-2990.
    • (1993) Endocrinology , vol.133 , pp. 2984-2990
    • Menjo, M.1    Murata, Y.2    Fujii, T.3    Nimura, Y.4    Seo, H.5
  • 91
    • 0029894973 scopus 로고    scopus 로고
    • Selenoenzyme expression in thyroid and liver of second generation selenium- And iodine-deficient rats
    • Mitchell J.H., Nicol F., Beckett G.J., Arthur J.R. Selenoenzyme expression in thyroid and liver of second generation selenium- and iodine-deficient rats. J. Mol. Endocrinol. 16:1996;259-267.
    • (1996) J. Mol. Endocrinol. , vol.16 , pp. 259-267
    • Mitchell, J.H.1    Nicol, F.2    Beckett, G.J.3    Arthur, J.R.4
  • 93
    • 0029828480 scopus 로고    scopus 로고
    • Effects of ceramide and protein kinase c on the regulation of type I 5′-deiodase in FRTL-5 rat thyroid cells
    • Mori K., Stone S., Braverman L.E., DeVito W.J. Effects of ceramide and protein kinase c on the regulation of type I 5′-deiodase in FRTL-5 rat thyroid cells. Endocrinology. 137:1996;4994-4999.
    • (1996) Endocrinology , vol.137 , pp. 4994-4999
    • Mori, K.1    Stone, S.2    Braverman, L.E.3    DeVito, W.J.4
  • 94
    • 0020413589 scopus 로고
    • Effect of cycloAMP on iodothyronine metabolism in the isolated perfused rat liver
    • Müller M.J., Köhrle J., Hesch R.D., Seitz H.J. Effect of cycloAMP on iodothyronine metabolism in the isolated perfused rat liver. Biochem. Int. 5:1982;495-501.
    • (1982) Biochem. Int. , vol.5 , pp. 495-501
    • Müller, M.J.1    Köhrle, J.2    Hesch, R.D.3    Seitz, H.J.4
  • 96
    • 0342983839 scopus 로고
    • 5′-Deiodinase type I in human kidney cancer
    • (Abstract)
    • Naumann, A., Naumann, J., Witeska, A., Dutkiewicz, M., 1993. 5′-Deiodinase type I in human kidney cancer. J. Endocrinol. Invest. 16 (Suppl. 2), 76-76 (Abstract).
    • (1993) J. Endocrinol. Invest. , vol.16 , Issue.SUPPL. 2 , pp. 76-76
    • Naumann, A.1    Naumann, J.2    Witeska, A.3    Dutkiewicz, M.4
  • 97
    • 0031736678 scopus 로고    scopus 로고
    • Direct measurement of the contributions of type I and type II 5′-deiodinases to whole body steady state 3,5,3′-triiodothyronine production from thyroxione in the rat
    • Nguyen, T.T., Chapa, F., DiStefano, J.J., III, 1998. Direct measurement of the contributions of type I and type II 5′-deiodinases to whole body steady state 3,5,3′-triiodothyronine production from thyroxione in the rat. Endocrinology 139, 4626-4633.
    • (1998) Endocrinology , vol.139 , pp. 4626-4633
    • Nguyen, T.T.1    Chapa, F.2    Distefano J.J. III3
  • 98
    • 0028124526 scopus 로고
    • Characterization and postnatal development of 5′-deiodinase activity in goat perirenal fat
    • Nicol F., Lefranc H., Arthur J.R., Trayhurn P. Characterization and postnatal development of 5′-deiodinase activity in goat perirenal fat. Am. J. Physiol. 267:1994;144R-149R.
    • (1994) Am. J. Physiol. , vol.267
    • Nicol, F.1    Lefranc, H.2    Arthur, J.R.3    Trayhurn, P.4
  • 99
    • 0002718244 scopus 로고    scopus 로고
    • The molecular basis of thyroid hormone actions
    • In: Braverman, L.E., Utiger, R.D. (Eds.), Lippincott-Raven, Philadelphia
    • Oppenheimer, J.H., Schwartz, H.L., Strait, K.A., 1996. The molecular basis of thyroid hormone actions. In: Braverman, L.E., Utiger, R.D. (Eds.), Werner and Ingbar's The Thyroid, 7th ed. (9). Lippincott-Raven, Philadelphia, pp. 162-184.
    • (1996) Werner and Ingbar's the Thyroid, 7th Ed. , Issue.9 , pp. 162-184
    • Oppenheimer, J.H.1    Schwartz, H.L.2    Strait, K.A.3
  • 101
    • 0030612099 scopus 로고    scopus 로고
    • Sphingomyelinase and phospholipase A2 regulate type I deiodase expression in FRTL-5 cells
    • Pekary A.E., Chopra I.J., Berg L., Hershman J.M. Sphingomyelinase and phospholipase A2 regulate type I deiodase expression in FRTL-5 cells. Thyroid. 7:1997;647-654.
    • (1997) Thyroid , vol.7 , pp. 647-654
    • Pekary, A.E.1    Chopra, I.J.2    Berg, L.3    Hershman, J.M.4
  • 102
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • Penning T.M. Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr. Rev. 18:1997;281.
    • (1997) Endocr. Rev. , vol.18 , pp. 281
    • Penning, T.M.1
  • 103
    • 0030894299 scopus 로고    scopus 로고
    • Thyroid hormone and gene expression in the regulation of mitochondrial respiratory function
    • Pillar T.M., Seitz H.J. Thyroid hormone and gene expression in the regulation of mitochondrial respiratory function. Eur. J. Endocrinol. 136:1997;231-239.
    • (1997) Eur. J. Endocrinol. , vol.136 , pp. 231-239
    • Pillar, T.M.1    Seitz, H.J.2
  • 106
    • 0002551887 scopus 로고    scopus 로고
    • Thyroid hormone transport proteins and the physiology of hormone binding
    • In: Braverman, L.E., Utiger, R.D. (Eds.), Lippincott-Raven, Philadelphia
    • Robbins, J., 1996. Thyroid hormone transport proteins and the physiology of hormone binding. In: Braverman, L.E., Utiger, R.D. (Eds.), Werner and Ingbar's The Thyroid, 7th ed. (6). Lippincott-Raven, Philadelphia, pp. 96-110.
    • (1996) Werner and Ingbar's the Thyroid, 7th Ed. , Issue.6 , pp. 96-110
    • Robbins, J.1
  • 107
    • 0018801620 scopus 로고
    • Purification and characterization of a flavoprotein from bovine thyroid with iodotyrosine deiodinase activity
    • Rosenberg I.N., Goswami A. Purification and characterization of a flavoprotein from bovine thyroid with iodotyrosine deiodinase activity. J. Biol. Chem. 254:1979;12318-12325.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12318-12325
    • Rosenberg, I.N.1    Goswami, A.2
  • 108
    • 0027322364 scopus 로고
    • Thyroxine 5′-deiodinase type II activity in chick pineal and Harderian gland: Nyctohemeral rhythmicity and its regulation by noradrenergic input
    • Rubio A., Menendez Pelaez A., Reiter R.J. Thyroxine 5′-deiodinase type II activity in chick pineal and Harderian gland: nyctohemeral rhythmicity and its regulation by noradrenergic input. J. Pineal Res. 14:1993;53-59.
    • (1993) J. Pineal Res. , vol.14 , pp. 53-59
    • Rubio, A.1    Menendez Pelaez, A.2    Reiter, R.J.3
  • 109
    • 0030037150 scopus 로고    scopus 로고
    • Catalytic activity of type II iodothyronine 5′-deiodinase polypeptide is dependent upon a cyclic AMP activation factor
    • Safran M., Farwell A.P., Leonard J.L. Catalytic activity of type II iodothyronine 5′-deiodinase polypeptide is dependent upon a cyclic AMP activation factor. J. Biol. Chem. 271:1996;16363-16368.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16363-16368
    • Safran, M.1    Farwell, A.P.2    Leonard, J.L.3
  • 110
    • 0029938790 scopus 로고    scopus 로고
    • Molecular biological and biochemical charcterization of the human type 2 selenodeiodinase
    • Salvatore D., Bartha T., Harney J.W., Larsen P.R. Molecular biological and biochemical charcterization of the human type 2 selenodeiodinase. Endocrinology. 137:1996;3308-3315.
    • (1996) Endocrinology , vol.137 , pp. 3308-3315
    • Salvatore, D.1    Bartha, T.2    Harney, J.W.3    Larsen, P.R.4
  • 111
    • 0029832961 scopus 로고    scopus 로고
    • Type 2 iodothyronine deiodinase is highly expressed in human thyroid
    • Salvatore D., Tu H., Harney J.W., Larsen P.R. Type 2 iodothyronine deiodinase is highly expressed in human thyroid. J. Clin. Invest. 98:1996;962-968.
    • (1996) J. Clin. Invest. , vol.98 , pp. 962-968
    • Salvatore, D.1    Tu, H.2    Harney, J.W.3    Larsen, P.R.4
  • 114
    • 0029955143 scopus 로고    scopus 로고
    • Effects of retinoids and role of retinoic acid receptors in human thyroid carcinomas and cell lines derived therefrom
    • Schmutzler C., Brtko J., Bienert K., Köhrle J. Effects of retinoids and role of retinoic acid receptors in human thyroid carcinomas and cell lines derived therefrom. Exp. Clin. Endocrinol. Diabetes. 104:1996;16-19.
    • (1996) Exp. Clin. Endocrinol. Diabetes , vol.104 , pp. 16-19
    • Schmutzler, C.1    Brtko, J.2    Bienert, K.3    Köhrle, J.4
  • 115
    • 0042945030 scopus 로고    scopus 로고
    • Regulation of type I 5′-deiodinase (5′DI) by proinflammatory cytokines in the human hepatocarcinoma cell line HepG2
    • 2-2 (Abstract)
    • Schmutzler, C., Jakobs, T.C., Dreher, I., Glaser, F., Köhrle, J., 1998a. Regulation of type I 5′-deiodinase (5′DI) by proinflammatory cytokines in the human hepatocarcinoma cell line HepG2. J. Endocrinol. Invest. 21, 2-2 (Abstract).
    • (1998) J. Endocrinol. Invest. , vol.21
    • Schmutzler, C.1    Jakobs, T.C.2    Dreher, I.3    Glaser, F.4    Köhrle, J.5
  • 116
    • 0345692156 scopus 로고    scopus 로고
    • RA- and T3-dependent activation of the human type I 5′-deiodinase promoter is mediated by bifunctional hormone responsive elements in a cell type-specific manner (submitted)
    • Schmutzler, C., Jakobs, T.C., Wagner, C., Glaser, F., Meissner-Weigl, J., Köhrle, J., 1998b. RA- and T3-dependent activation of the human type I 5′-deiodinase promoter is mediated by bifunctional hormone responsive elements in a cell type-specific manner (submitted).
    • (1998)
    • Schmutzler, C.1    Jakobs, T.C.2    Wagner, C.3    Glaser, F.4    Meissner-Weigl, J.5    Köhrle, J.6
  • 117
    • 0028136191 scopus 로고
    • Retinoids stimulate type I iodothyronine 5′-deiodinase activity in human follicular thyroid carcinoma cell lines
    • Schreck R., Schnieders F., Schmutzler C., Köhrle J. Retinoids stimulate type I iodothyronine 5′-deiodinase activity in human follicular thyroid carcinoma cell lines. J. Clin. Endocrinol. Metab. 79:1994;791-798.
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 791-798
    • Schreck, R.1    Schnieders, F.2    Schmutzler, C.3    Köhrle, J.4
  • 118
    • 0030945339 scopus 로고    scopus 로고
    • The evolution of gene expression, structure and function of transthyretin
    • Schreiber G., Richardson S.J. The evolution of gene expression, structure and function of transthyretin. Comp. Biochem. Physiol. B. 116:1997;137-160.
    • (1997) Comp. Biochem. Physiol. B , vol.116 , pp. 137-160
    • Schreiber, G.1    Richardson, S.J.2
  • 119
    • 2042442587 scopus 로고    scopus 로고
    • Different tissue distribution, elimination, and kinetics of thyroxine and its conformational analog, the synthetic flavonoid EMD 49209 in the rat
    • Schröder van der Elst J.P., Van der Heide D., Rokos H., Köhrle J., Morreale de Escobar G. Different tissue distribution, elimination, and kinetics of thyroxine and its conformational analog, the synthetic flavonoid EMD 49209 in the rat. Endocrinology. 138:1997;79-84.
    • (1997) Endocrinology , vol.138 , pp. 79-84
    • Schröder Van Der Elst, J.P.1    Van Der Heide, D.2    Rokos, H.3    Köhrle, J.4    Morreale De Escobar, G.5
  • 120
    • 0031764259 scopus 로고    scopus 로고
    • Iodothyronine deiodinase activities in fetal rat tissues at several levels of iodine deficiency: A role for the skin in 3,5,3′-triiodothyronine economy?
    • Schröder van der Elst J.P., Van der Heide D., Morreale de Escobar G., Obregón M.J. Iodothyronine deiodinase activities in fetal rat tissues at several levels of iodine deficiency: a role for the skin in 3,5,3′-triiodothyronine economy? Endocrinology. 139:1998;2229-2234.
    • (1998) Endocrinology , vol.139 , pp. 2229-2234
    • Schröder Van Der Elst, J.P.1    Van Der Heide, D.2    Morreale De Escobar, G.3    Obregón, M.J.4
  • 122
    • 0029982310 scopus 로고    scopus 로고
    • Analysis of the functional state of T3 nuclear receptors expressed in thyroid cells
    • Selmi-Ruby S., Rousset B. Analysis of the functional state of T3 nuclear receptors expressed in thyroid cells. Mol. Cell. Endocrinol. 119:1996;95-104.
    • (1996) Mol. Cell. Endocrinol. , vol.119 , pp. 95-104
    • Selmi-Ruby, S.1    Rousset, B.2
  • 124
    • 0029561581 scopus 로고
    • Thyroid hormone control of thermogenesis and energy balance
    • Silva J.E. Thyroid hormone control of thermogenesis and energy balance. Thyroid. 5:1995;481-492.
    • (1995) Thyroid , vol.5 , pp. 481-492
    • Silva, J.E.1
  • 125
    • 0031794371 scopus 로고    scopus 로고
    • Metabolism of retinoic acid: Implications for development and cancer
    • Sonneveld E., Van der Saag P.T. Metabolism of retinoic acid: implications for development and cancer. Int. J. Vitam. Nutr. Res. 68:1998;404-410.
    • (1998) Int. J. Vitam. Nutr. Res. , vol.68 , pp. 404-410
    • Sonneveld, E.1    Van Der Saag, P.T.2
  • 126
    • 0029656213 scopus 로고    scopus 로고
    • Beta- And alpha-adrenergic mechanisms are involved in regulating type II thyroxine 5′-deiodinase in rat thymus
    • Soutto M., Guerrero J.M., Molinero P. Beta- and alpha-adrenergic mechanisms are involved in regulating type II thyroxine 5′-deiodinase in rat thymus. Life Sci. 58:1996;1-8.
    • (1996) Life Sci. , vol.58 , pp. 1-8
    • Soutto, M.1    Guerrero, J.M.2    Molinero, P.3
  • 127
    • 0025231546 scopus 로고
    • 5′-Deiodination in rat hepatocytes: Effects of specific flavonoid inhibitors
    • Spanka M., Hesch R.-D., Irmscher K., Köhrle J. 5′-Deiodination in rat hepatocytes: effects of specific flavonoid inhibitors. Endocrinology. 126:1990;1660-1667.
    • (1990) Endocrinology , vol.126 , pp. 1660-1667
    • Spanka, M.1    Hesch, R.-D.2    Irmscher, K.3    Köhrle, J.4
  • 129
    • 0024462651 scopus 로고
    • Ligand-induced inactivation of type I iodothyronine 5′-deiodinase: Protection by propylthiouracil in vivo and reversibility in vitro
    • St. Germain D.L., Croteau W. Ligand-induced inactivation of type I iodothyronine 5′-deiodinase: protection by propylthiouracil in vivo and reversibility in vitro. Endocrinology. 125:1989;2735-2744.
    • (1989) Endocrinology , vol.125 , pp. 2735-2744
    • St. Germain, D.L.1    Croteau, W.2
  • 130
    • 0030770801 scopus 로고    scopus 로고
    • The deiodinase family of selenoproteins
    • St. Germain D.L., Galton V.A. The deiodinase family of selenoproteins. Thyroid. 7:1997;655-668.
    • (1997) Thyroid , vol.7 , pp. 655-668
    • St. Germain, D.L.1    Galton, V.A.2
  • 131
    • 0032566136 scopus 로고    scopus 로고
    • Placental iodothyronine deiodinase III and II ratios, mRNA expression compared to enzyme activity
    • Stulp M.R., De Vijlder J.J.M., Ris-Stalpers C. Placental iodothyronine deiodinase III and II ratios, mRNA expression compared to enzyme activity. Mol. Cell Endocrinol. 142:1998;67-73.
    • (1998) Mol. Cell Endocrinol. , vol.142 , pp. 67-73
    • Stulp, M.R.1    De Vijlder, J.J.M.2    Ris-Stalpers, C.3
  • 132
    • 0030724860 scopus 로고    scopus 로고
    • The role of the active site cysteine in catalysis by type1 iodothyronine deiodinase
    • Sun B.C., Harney J.W., Marla J.B., Larsen P.R. The role of the active site cysteine in catalysis by type1 iodothyronine deiodinase. Endocrinology. 138:1997;5452-5458.
    • (1997) Endocrinology , vol.138 , pp. 5452-5458
    • Sun, B.C.1    Harney, J.W.2    Marla, J.B.3    Larsen, P.R.4
  • 133
    • 0028003654 scopus 로고
    • Identification of critical amino acids for 3,5,3′-triiodothyronine deiodination by human type 1 deiodinase based on comparative functional-structural analyses of the human, dog, and rat enzymes
    • Toyoda N., Harney J.W., Berry M.J., Larsen P.R. Identification of critical amino acids for 3,5,3′-triiodothyronine deiodination by human type 1 deiodinase based on comparative functional-structural analyses of the human, dog, and rat enzymes. J. Biol. Chem. 269(32):1994;20329-20334.
    • (1994) J. Biol. Chem. , vol.269 , Issue.32 , pp. 20329-20334
    • Toyoda, N.1    Harney, J.W.2    Berry, M.J.3    Larsen, P.R.4
  • 134
    • 0031015952 scopus 로고    scopus 로고
    • Structure-activity relationships for thyroid hormone deiodination by mammalian type I iodothyronine deiodinases
    • Toyoda N., Kaptein E., Berry M.J., Harney J.W., Larsen P.R., Visser T.J. Structure-activity relationships for thyroid hormone deiodination by mammalian type I iodothyronine deiodinases. Endocrinology. 138:1997;213-219.
    • (1997) Endocrinology , vol.138 , pp. 213-219
    • Toyoda, N.1    Kaptein, E.2    Berry, M.J.3    Harney, J.W.4    Larsen, P.R.5    Visser, T.J.6
  • 136
    • 0026683591 scopus 로고
    • Thyrotropin and triiodothyronine regulate iodothyronine 5′-deiodinase messenger ribonucleic acid levels in FRTL-5 rat thyroid cells
    • Toyoda N., Nishikawa M., Mori Y., Gondou A., Ogawa Y., Yonemoto T., Yoshimura M., Masaki H., Inada M. Thyrotropin and triiodothyronine regulate iodothyronine 5′-deiodinase messenger ribonucleic acid levels in FRTL-5 rat thyroid cells. Endocrinology. 131:1992;389-394.
    • (1992) Endocrinology , vol.131 , pp. 389-394
    • Toyoda, N.1    Nishikawa, M.2    Mori, Y.3    Gondou, A.4    Ogawa, Y.5    Yonemoto, T.6    Yoshimura, M.7    Masaki, H.8    Inada, M.9
  • 137
    • 0029118758 scopus 로고
    • A novel retinoid X receptor-indepent thyroid hormone response element is present in the human type 1 deiodinase gene
    • Toyoda N., Zavacki A.M., Maia A.L., Harney J.W., Larsen P.R. A novel retinoid X receptor-indepent thyroid hormone response element is present in the human type 1 deiodinase gene. Mol. Cell Biol. 15:1995;5100-5112.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 5100-5112
    • Toyoda, N.1    Zavacki, A.M.2    Maia, A.L.3    Harney, J.W.4    Larsen, P.R.5
  • 138
    • 0027506446 scopus 로고
    • Presence of the brown fat-specific mitochondrial uncoupling protein and iodothyronine 5′-deiodinase activity in subcutaneous adipose tissue of neonatal lambs
    • Trayhurn P., Thomas M.E., Duncan J.S., Nicol F., Arthur J.R. Presence of the brown fat-specific mitochondrial uncoupling protein and iodothyronine 5′-deiodinase activity in subcutaneous adipose tissue of neonatal lambs. FEBS Lett. 322:1993;76-78.
    • (1993) FEBS Lett. , vol.322 , pp. 76-78
    • Trayhurn, P.1    Thomas, M.E.2    Duncan, J.S.3    Nicol, F.4    Arthur, J.R.5
  • 139
    • 0031053504 scopus 로고    scopus 로고
    • Cloning and expression of a 5′-iodothyronine deiodinase from the liver of Fundulus heteroclitus
    • Valverde C., Croteau W., Lafleur G.J., Orozco A., Germain D.L.S. Cloning and expression of a 5′-iodothyronine deiodinase from the liver of Fundulus heteroclitus. Endocrinology. 138:1997;642-648.
    • (1997) Endocrinology , vol.138 , pp. 642-648
    • Valverde, C.1    Croteau, W.2    Lafleur, G.J.3    Orozco, A.4    Germain, D.L.S.5
  • 140
    • 0029953792 scopus 로고    scopus 로고
    • Structure-function relationship of the inhibition of the 3,5,3′-triiodothyronine binding to the α1- And β1-thyroid hormone receptor by amiodarone analogs
    • Van Beeren H.C., Bakker O., Wiersinga W.M. Structure-function relationship of the inhibition of the 3,5,3′-triiodothyronine binding to the α1- and β1-thyroid hormone receptor by amiodarone analogs. Endocrinology. 137:1996;2807-2814.
    • (1996) Endocrinology , vol.137 , pp. 2807-2814
    • Van Beeren, H.C.1    Bakker, O.2    Wiersinga, W.M.3
  • 141
    • 0029875824 scopus 로고    scopus 로고
    • Thyroid hormone responses to environmental cold exposure and seasonal changes: A proposed model
    • Van Do N., LeMar H., Reed H.L. Thyroid hormone responses to environmental cold exposure and seasonal changes: a proposed model. Endocrinol. Metab. 3:1996;7-16.
    • (1996) Endocrinol. Metab. , vol.3 , pp. 7-16
    • Van Do, N.1    Lemar, H.2    Reed, H.L.3
  • 142
    • 0021802634 scopus 로고
    • Concentrations of thyroxine and 3,5,3′-triiodothyronine at 34 different sites in euthyroid rats as determined by an isotopic equilibrium technique
    • van Doorn J., Roelfsema F., Van der Heide D. Concentrations of thyroxine and 3,5,3′-triiodothyronine at 34 different sites in euthyroid rats as determined by an isotopic equilibrium technique. Endocrinology. 117:1985;1201-1208.
    • (1985) Endocrinology , vol.117 , pp. 1201-1208
    • Van Doorn, J.1    Roelfsema, F.2    Van Der Heide, D.3
  • 143
    • 0031768544 scopus 로고    scopus 로고
    • Thyroxine administration to infants of less than 30 weeks gestational age decreases plasma tri-iodothyronine concentrations
    • van Wassenaer A.G., Kok J.H., Dekker F.W., Endert E., De Vijlder J.J.M. Thyroxine administration to infants of less than 30 weeks gestational age decreases plasma tri-iodothyronine concentrations. Eur. J. Endocrinol. 139:1998;508-515.
    • (1998) Eur. J. Endocrinol. , vol.139 , pp. 508-515
    • Van Wassenaer, A.G.1    Kok, J.H.2    Dekker, F.W.3    Endert, E.4    De Vijlder, J.J.M.5
  • 144
    • 0032582724 scopus 로고    scopus 로고
    • Thyroid stimulating hormone and selenium supply interact to regulate selenoenzyme gene expression in thyroid cels (FRTL-5) in culture
    • Villette S., Bermano G., Arthur J.R., Hesketh J.E. Thyroid stimulating hormone and selenium supply interact to regulate selenoenzyme gene expression in thyroid cels (FRTL-5) in culture. FEBS Lett. 438:1998;81-84.
    • (1998) FEBS Lett. , vol.438 , pp. 81-84
    • Villette, S.1    Bermano, G.2    Arthur, J.R.3    Hesketh, J.E.4
  • 145
    • 0028240253 scopus 로고
    • Role of sulfation in thyroid hormone metabolism
    • Visser T.J. Role of sulfation in thyroid hormone metabolism. Chem. Biol. Interact. 92:1994;293-303.
    • (1994) Chem. Biol. Interact. , vol.92 , pp. 293-303
    • Visser, T.J.1
  • 146
    • 0020661567 scopus 로고
    • Evidence for two pathways of iodothyronine 5′ deiodination in rat pituitary that differ in kinetics, propylthiouracil sensitivity, and response to hypothyroidism
    • Visser T.J., Kaplan M.M., Leonard J.L., Larsen P.R. Evidence for two pathways of iodothyronine 5′ deiodination in rat pituitary that differ in kinetics, propylthiouracil sensitivity, and response to hypothyroidism. J. Clin. Invest. 71:1983;992-1002.
    • (1983) J. Clin. Invest. , vol.71 , pp. 992-1002
    • Visser, T.J.1    Kaplan, M.M.2    Leonard, J.L.3    Larsen, P.R.4
  • 148
    • 0029150952 scopus 로고
    • Impaired thyroxine and 3,5,3′-triiodothyronine handling by rat hepatocytes in the presence of serum of patients with nonthyroidal illness
    • Vos R.A., De Jong M., Bernard B.F., Docter R., Krenning E.P., Hennemann G. Impaired thyroxine and 3,5,3′-triiodothyronine handling by rat hepatocytes in the presence of serum of patients with nonthyroidal illness. J. Clin. Endocrinol. Metab. 80:1995;2364-2370.
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 2364-2370
    • Vos, R.A.1    De Jong, M.2    Bernard, B.F.3    Docter, R.4    Krenning, E.P.5    Hennemann, G.6
  • 149
    • 0031046241 scopus 로고    scopus 로고
    • 11β-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess
    • White P.C., Mune T., Agarwal A.K. 11β-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess. Endocr. Rev. 18:1997;135-156.
    • (1997) Endocr. Rev. , vol.18 , pp. 135-156
    • White, P.C.1    Mune, T.2    Agarwal, A.K.3
  • 151
    • 0031774213 scopus 로고    scopus 로고
    • RT-PCR analysis of thyrocyte-relevant genes in fine-needle aspiration biopsies of the human thyroid
    • Winzer R., Schmutzler C., Jakobs T.C., Ebert R., Rendl J., Reiners C., Köhrle J. RT-PCR analysis of thyrocyte-relevant genes in fine-needle aspiration biopsies of the human thyroid. Thyroid. 8:1998;981-987.
    • (1998) Thyroid , vol.8 , pp. 981-987
    • Winzer, R.1    Schmutzler, C.2    Jakobs, T.C.3    Ebert, R.4    Rendl, J.5    Reiners, C.6    Köhrle, J.7
  • 152
    • 0031768323 scopus 로고    scopus 로고
    • Further characterization of thyroid hormone response elements in the human type 1 iodothyronine deiodinase gene
    • Zhang C.-Y., Kim S., Harney J.W., Larsen P.R. Further characterization of thyroid hormone response elements in the human type 1 iodothyronine deiodinase gene. Endocrinology. 139:1998;1156-1163.
    • (1998) Endocrinology , vol.139 , pp. 1156-1163
    • Zhang, C.-Y.1    Kim, S.2    Harney, J.W.3    Larsen, P.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.