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Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases.
Sun, Q A; Wu, Y; Zappacosta, F; Jeang, K T; Lee, B J; Hatfield, D L; Gladyshev, V N.
Afiliação
  • Sun QA; Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, USA.
J Biol Chem ; 274(35): 24522-30, 1999 Aug 27.
Article em En | MEDLINE | ID: mdl-10455115
The intracellular generation of reactive oxygen species, together with the thioredoxin and glutathione systems, is thought to participate in redox signaling in mammalian cells. The activity of thioredoxin is dependent on the redox status of thioredoxin reductase (TR), the activity of which in turn is dependent on a selenocysteine residue. Two mammalian TR isozymes (TR2 and TR3), in addition to that previously characterized (TR1), have now been identified in humans and mice. All three TR isozymes contain a selenocysteine residue that is located in the penultimate position at the carboxyl terminus and which is encoded by a UGA codon. The generation of reactive oxygen species in a human carcinoma cell line was shown to result in both the oxidation of the selenocysteine in TR1 and a subsequent increase in the expression of this enzyme. These observations identify the carboxyl-terminal selenocysteine of TR1 as a cellular redox sensor and support an essential role for mammalian TR isozymes in redox-regulated cell signaling.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tiorredoxina Dissulfeto Redutase / Transdução de Sinais / Selenocisteína Tipo de estudo: Prognostic_studies Limite: Animals / Humans / Male Idioma: En Revista: J Biol Chem Ano de publicação: 1999 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Estados Unidos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tiorredoxina Dissulfeto Redutase / Transdução de Sinais / Selenocisteína Tipo de estudo: Prognostic_studies Limite: Animals / Humans / Male Idioma: En Revista: J Biol Chem Ano de publicação: 1999 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Estados Unidos