Thioredoxin reductase and cytoplasmic glutathione peroxidase activity in human foetal and neonatal liver

M H Lewin, R Hume, A F Howie, K Richard, John Arthur, Fergus Nicol, S W Walker, G J Beckett

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Cytosolic thioredoxin reductase (TR) is an FAD-containing homodimeric selenoenzyme which, together with thioredoxin (Trx) and NADPH, forms a powerful oxidoreductase system. Cytoplasmic glutathione peroxidase (GPX-1) is a selenoprotein with antioxidant activity. The TR/Trx system has been associated with cellular processes including regulation of cell growth, and modification of activity of transcription factors. TR may also act as an antioxidant. We have measured TR activity, TR concentration, and GPX-1 activity in human hepatic cytosols from foetuses and neonates. The concentration of TR was significantly greater (P < 0.05) in foetal (43.6, 37.9-50.8 mug/g protein, median, interquartile range) than in neonatal liver (11.6, 8.70-15.0 mug/g). This was also true of TR activity which was 2.1, 1.8-2.5 U/g protein in foetal, and 0.65, 0.44-0.74 U/g protein in neonatal liver (P < 0.0005). Similarly, GPX-1 activity was significantly higher (P < 0.005) in the foetal (199.7, 144.0-227.9 U/g protein) than in neonatal(77.0, 58.4-110.3 U/g protein) hepatic cytosol. Overall, foetal liver expressed approx. 3-fold higher activities of TR and GPX-1 than neonatal liver. (C) 2001 Elsevier Science B.V. All rights reserved.

Original languageEnglish
Pages (from-to)237-241
Number of pages5
JournalBiochimica et Biophysica Acta (BBA) - General Subjects
Issue number3
Publication statusPublished - 15 Jun 2001


  • hepatic
  • thioredoxin reductase
  • antioxidant
  • fetal neonatal
  • measurement

Cite this

Lewin, M. H., Hume, R., Howie, A. F., Richard, K., Arthur, J., Nicol, F., Walker, S. W., & Beckett, G. J. (2001). Thioredoxin reductase and cytoplasmic glutathione peroxidase activity in human foetal and neonatal liver. Biochimica et Biophysica Acta (BBA) - General Subjects, 1526(3), 237-241.