Water Research, Journal Year: 2024, Volume and Issue: 270, P. 122826 - 122826
Published: Nov. 20, 2024
Language: Английский
Water Research, Journal Year: 2024, Volume and Issue: 270, P. 122826 - 122826
Published: Nov. 20, 2024
Language: Английский
Antioxidants, Journal Year: 2025, Volume and Issue: 14(3), P. 257 - 257
Published: Feb. 24, 2025
Thioredoxin-1 (Trx-1) is an important redox protein found in almost all prokaryotic and eukaryotic cells, which has a highly conserved active site sequence: Trp-Cys-Gly-Pro-Cys. To investigate whether the Trp31 residue essential for antioxidant activity of human Trx-1 (hTrx-1), we mutated by replacing with Ala31 (31Ala) or deleting (31Del). We introduced 31Ala 31Del mutations into cells hTrx-1 expression, purification evaluation activity. The results showed that neither mutation to nor deletion affected efficient expression indicating form would disrupt folded structure protein. Comparison purified proteins wild-type, forms revealed both mutant significantly decreased capacity hTrx-1. Further investigations on H2O2 treatment caused massive cell death EA.Hy926 endothelial compared wild-type was associated increased ROS production downregulation Nrf2 HO-1 cells. These suggested remarkably disrupted cellular defense against oxidative stress. relies thiol-disulfide exchange reaction, content thiol groups forming disulfide bonds critical. free specifically participating bond formation lower than hTrx-1; speculated affect between Cys32 Cys35 virtual analysis, thus abolishing cleaving oxidized defending present study provided valuable insights towards understanding importance maintaining correct conformation Trx fold structure, functionality capability
Language: Английский
Citations
0Water Research, Journal Year: 2024, Volume and Issue: 270, P. 122826 - 122826
Published: Nov. 20, 2024
Language: Английский
Citations
3