not received. 4 HUMAN PLACENTAL PERFUSION METHOD IN THE ASSESSMENT OF TRANSPLACENTAL PASSAGE OF ANTIEPILEPTIC DRUGS P. Myllynen,1 E. Hamalainen,2 S. Parkko,2 P. Pienimaki,1 and K. Vaha¨ ¨¨ ¨ ¨ ¨ kangas1,2, 1Department of Pharmacology and Toxicology, University of Oulu, Oulu, Finland, 2Department of Pharmacology and Toxicology, University of Kuopio, Kuopio, Finland The redox environment inside mammalian cells is generally reducing with a high concentration of GSH and free sulfhydryl groups on proteins. Thioredoxin and thioredoxin reductase are the major protein disulfide reductase system using electrons from NADPH (1). Disulfide linkages in proteins may occur as a result of substrate reduction by specific enzymes catalyzing redox reactions like ribonucleotide reductase, methionine sulfoxide reductase or peroxiredoxins. In addition, there is evidence for a variety of other proteins, which form transcient disulfides during specific conditions like cell activation by hydrogen peroxide or during oxidative stress. The mechanism of thioredoxin as a disulfide reductase will be discussed. Reduction of oxidized thioredoxin occurs by thioredoxin reductases, which are enzymes dependent on selenocysteine (2). The antioxidant ebselen is a direct substrate for thioredoxin reductase and an ultrafast oxidant of reduced thioredoxin (3). The in vivo state of thioredoxin during different condition has been
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ICTX Congress Special Issue
Follow Toxicology and Applied Pharmacology
, Volume 197 (3)
Elsevier – Jun 15, 2004
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