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

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

Research output: Contribution to journalArticlepeer-review

Abstract

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
Original languageEnglish
Pages (from-to)237-41
Number of pages5
JournalBBA - Biomembranes
Volume1526
Issue number3
Publication statusPublished - 2001

Fingerprint

Dive into the research topics of 'Thioredoxin reductase and cytoplasmic glutathione peroxidase activity in human foetal and neonatal liver'. Together they form a unique fingerprint.

Cite this