Naturally occurring free thiols within β2-glycoprotein I in vivo: nitrosylation, redox modification by endothelial cells, and regulation of oxidative stress–induced cell injury

摘要: β2-Glycoprotein I (β2GPI) is an evolutionary conserved, abundant circulating protein. Although its function remains uncertain, accumulated evidence points toward interactions with endothelial cells and components of the coagulation system, suggesting a regulatory role in vascular biology. Our group has shown that thioredoxin 1 (TRX-1) generates free thiols β2GPI, process may have platelet adhesion. This report extends these studies shows for first time β2GPI vivo both multiple human murine serum samples. To explore how surface modulate redox status unstimulated EAhy926 are to be capable amplifying effect thiol generation within β2GPI. Multiple oxidoreductase enzymes, such as endoplasmic reticulum protein 46 (ERp 46) TRX-1 reductase, addition disulfide isomerase secreted on cells. Furthermore, one or more generated also nitrosylated. Finally, functional significance findings explored, by showing thiol-containing powerful protecting from oxidative stress-induced cell death.