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Bo Zhu, Ashutosh Shrivastava, Cristina Luongo, Ting Chen, John W Harney, Alessandro Marsili, Thuy-Van Tran, Anulika Bhadouria, Radhika Mopala, Amanda I Steen, P Reed Larsen and Ann Marie Zavacki

Introduction The iodothyronine deiodinases are selenoenzymes that modulate tri-iodothyronine (T 3 ) concentrations by catalyzing both its production and degradation ( Bianco et al . 2002 , Gereben et al . 2008 ). Thyroxine (T 4 ) is activated via

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Local control of thyroid hormone action: role of type 2 deiodinase

Deiodinases: the balance of thyroid hormone

Graham R Williams and J H Duncan Bassett

3 is catalyzed by the type 2 iodothyronine deiodinase enzyme (DIO2), while the type 3 enzyme (DIO3) prevents activation of T 4 and inactivates T 3 . This pre-receptor control of ligand availability to TRs in target cells is a crucial mechanism that

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Simone Magagnin Wajner, Márcia dos Santos Wagner, Rossana C N Melo, Gleydes G Parreira, Hélio Chiarini-Garcia, Antonio C Bianco, Csaba Fekete, Edith Sanchez, Ronald M Lechan and Ana Luiza Maia

Introduction The iodothyronine deiodinases types 1, 2, and 3 (D1, D2, and D3) constitute a family of oxidoreductases that catalyze the removal of iodine from the outer ring (D1 and D2, activation) or inner ring (D3, inactivation) of

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C H J Verhoelst, V M Darras, S A Roelens, G M Artykbaeva and S Van der Geyten

interference of the so-called iodothyronine deiodinases. Three different deiodinases (type I iodothyronine deiodinase (D1), type II iodothyronine deiodinase (D2) and type III iodothyronine deiodinase (D3)) have been cloned and characterized for different

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S Van der Geyten, N Byamungu, G E Reyns, E R Kühn and V M Darras

and exert its full biologic activity. This activation, as well a s the inactivation of thyroid hormones, occurs not in the thyroid, but in the periphery through the action of iodothyronine deiodinases ( Eales & Brown 1993 , Mol et al. 1997 , 1998

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Renata Lopes Araujo, Bruno Moulin de Andrade, Álvaro Souto Padron de Figueiredo, Monique Leandro da Silva, Michelle Porto Marassi, Valmara dos Santos Pereira, Eliete Bouskela and Denise P Carvalho

( Ahima 2000 , Krotkiewski 2000 ), and to changes in the peripheral deiodination of thyroid hormones ( Bianco et al . 2002 ). Three iodothyronine deiodinases have been identified and characterized in different tissues. Type 1 deiodinase (D1) is found in

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Michelle P Marassi, Rodrigo S Fortunato, Alba C Matos da Silva, Valmara S Pereira, Denise P Carvalho, Doris Rosenthal and Vânia M Corrêa da Costa

) respectively. Based on several functional criteria and molecular characterization, three distinct deiodinase enzymes have been identified: type 1 (D1), type 2 (D2), and type 3 (D3). D1 seems to be the only selenodeiodinase that can function as either an outer

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Marcia S Wagner, Simone M Wajner, José M Dora and Ana Luiza Maia

Introduction Thyroxine (T 4 ), a major secretory product of the thyroid gland, needs to be converted to tri-iodothyronine (T 3 ) to exert its biological activity. Two isoenzymes, types 1 and 2 iodothyronine deiodinase (D1 and D2

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Brenda Anguiano, Alejandra López, Guadalupe Delgado, Carlos Romero and Carmen Aceves

(D1) and type 2 (D2) deiodinases. Both enzymes remove one iodine atom from position 5′ of the T 4 outer ring, giving rise to T 3 ( Bianco et al. 2002 , Kohrle 2002 ). These enzymes have been cloned and biochemically and molecularly characterized

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Domenico Salvatore

-hormone thyroxine (T 4 ), and only about 20% of the active hormone, T 3 . T 4 is largely inactive until it is deiodinated to T 3 by the type 1 (D1) or 2 (D2) deiodinase. This reaction produces about 80% of the T 3 present in the circulation in healthy subjects. A