An update on the unfolded protein response in brain ischemia: Experimental evidence and therapeutic opportunities

2021 ◽  
pp. 105218
Author(s):  
Xuan Li ◽  
Wei Yang
Keyword(s):  
Experimental Evidence ◽  
Unfolded Protein Response ◽  
Brain Ischemia ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Unfolded protein response in brain ischemia: A timely update

2016 ◽  
Vol 36 (12) ◽  
pp. 2044-2050 ◽  
Author(s):  
Wei Yang ◽  
Wulf Paschen
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Unfolded Protein Response ◽  
Brain Ischemia ◽  
Unfolded Protein ◽  
Vital Functions ◽  
Advance Research ◽  
The Unfolded Protein Response ◽  
Protein Response

Folding and processing newly synthesized proteins are vital functions of the endoplasmic reticulum that are sensitive to a variety of stress conditions. The unfolded protein response is activated to restore endoplasmic reticulum function impaired by stress. While we know that brain ischemia impairs endoplasmic reticulum function, the role of unfolded protein response activation in post-ischemic recovery of neurologic function is only beginning to emerge. Here, we summarize what is known about endoplasmic reticulum stress and unfolded protein response in brain ischemia and discuss recent findings from myocardial ischemia studies that could help to advance research on endoplasmic reticulum stress and unfolded protein response in brain ischemia.

scholarly journals Dysfunction of the Unfolded Protein Response during Global Brain Ischemia and Reperfusion

2003 ◽  
Vol 23 (4) ◽  
pp. 462-471 ◽  
Author(s):  
Rita Kumar ◽  
Gary S. Krause ◽  
Hiderou Yoshida ◽  
Kazutoshi Mori ◽  
Donald J. DeGracia
Keyword(s):  
Er Stress ◽  
Unfolded Protein Response ◽  
Brain Ischemia ◽  
Messenger Rna ◽  
Ischemia And Reperfusion ◽  
Global Brain Ischemia ◽  
Compensatory Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

A variety of endoplasmic reticulum (ER) stresses trigger the unfolded protein response (UPR), a compensatory response whose most proximal sensors are the ER membrane–bound proteins ATF6, IRE1α, and PERK. The authors simultaneously examined the activation of ATF6, IRE1α, and PERK, as well as components of downstream UPR pathways, in the rat brain after reperfusion after a 10-minute cardiac arrest. Although ATF6 was not activated, PERK was maximally activated at 10-minute reperfusion, which correlated with maximal eIF2α phosphorylation and protein synthesis inhibition. By 4-h reperfusion, there was 80% loss of PERK immunostaining in cortex and 50% loss in brain stem and hippocampus. PERK was degraded in vitro by μ-calpain. Although inactive IRE1α was maximally decreased by 90-minute reperfusion, there was no evidence that its substrate xbp-1 messenger RNA had been processed by removal of a 26-nt sequence. Similarly, there was no expression of the UPR effector proteins 55-kd XBP-1, CHOP, or ATF4. These data indicate that there is dysfunction in several key components of the UPR that abrogate the effects of ER stress. In other systems, failure to mount the UPR results in increased cell death. As other studies have shown evidence for ER stress after brain ischemia and reperfusion, the failure of the UPR may play a significant role in reperfusion neuronal death.

Oestrogen-driven changes in the bovine uterus are associated with activation of the unfolded protein response

2014 ◽  
Author(s):  
Mohammed A Alfattah ◽  
Paul Anthony McGettigan ◽  
John Arthur Browne ◽  
Khalid M Alkhodair ◽  
Katarzyna Pluta ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response
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