Hemeoxygenase-1 Mediates an Adaptive Response to Spermidine-Induced Cell Death in Human Endothelial Cells
Figure 5
A scheme showing a proposed cytoprotective mechanism against SPD-induced oxidative stress by HO-1 induction. During the degradation of spermidine (SPD) to putrescine by serum amine oxidase, aldehydes, H2O2, and NH3 are produced, which induce oxidative stress. It triggers Nrf2 translocation and ARE binding through PI3K/Akt signaling. Nrf2 activation upregulates HO-1 expression. HO-1 catalyzed heme to biliverdin and bilirubin, with the concurrent release of bioactive molecules, such as ferritin and CO. Heme metabolites exert adaptive response and protect cells against SPD-induced oxidative stress.
