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PERK enhances the expression of antioxidant defense system through Nrf2-dependent mechanisms: implications for PD.
Protein kinase RNA-like endoplasmic reticulum (ER) kinase (PERK) is an ER-localized transmembrane kinase, which is known to induce the unfolded protein response (UPR) in the cells. It has been shown that the activation of UPR mediated by PERK modulates the transcription of genes encoding chaperone proteins, such as BiP, Grp78, and the Hsp70 family members in ER. The binding of bZIP transcription factors (ATF4/ATF6) to promoter regions of UPR-responsive genes is known to be a key step in the activation of UPR. Activated PERK also induces the expression of some antioxidant proteins, such as heme oxygenase-1, thioredoxin, glutathione peroxidase, and catalase, by activating nuclear factor erythroid 2-related factor 2 (Nrf2). Our recent study also shows that the induction of Nrf2 by activated PERK mediates the expression of a subset of antioxidant proteins in the UPR-independent manner. PERK in fact acts as a critical antioxidant factor under conditions where the Nrf2 pathway is attenuated. Therefore, the activation of Nrf2 appears to be a robust mechanism for the defense system against oxidative stress. This review provides a perspective on the roles of PERK, Nrf2, and UPR in oxidative stress, and provides an updated overview of the mechanism underlying the induction of antioxidant proteins by activated PERK.#include "Align.h"
#include
Align::Align(const vector& faces, const vector& labels, const vector& rgb){
maxR=rgb[2];
maxG=rgb[1];
maxB=rgb[0];
maxR_color=rgb[1];
maxG_color=rgb[2];
maxB_color=rgb[
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