Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells.

摘要: Glutaredoxin belongs to the oxidoreductase family, with cytosolic glutaredoxin 1 (Grx1) and mitochondrial 2 (Grx2) isoforms. Of two isozymes, function of Grx2 is not well understood. This paper describes effects deletion on cellular using primary lens epithelial cell cultures isolated from gene knockout (KO) wild-type (WT) mice. We found that both types showed similar growth patterns morphology comparable glutathione pool complex I activity. Cells deleted did show affected Grx1 or thioredoxin expression but exhibited high sensitivity oxidative stress. Under treatment H(2)O(2), KO cells less viability, higher membrane leakage, enhanced ATP loss inactivation, weakened ability detoxify H(2)O(2) in comparison WT cells. The had glutathionylation proteins, particularly 75-kDa subunit I. Recombinant deglutathionylated restored most its conclude has a protects against H(2)O(2)-induced injury via peroxidase dethiolase activities; particularly, prevents inactivation preserves function.