Protein Aggregation, Unfolded Protein Response and Delayed Neuronal Death after Brain Ischemia

2004 ◽  
pp. 225-237 ◽  
Author(s):  
B. R. Hu ◽  
M. E. Martone ◽  
C. L. Liu
Keyword(s):  
Protein Aggregation ◽  
Unfolded Protein Response ◽  
Brain Ischemia ◽  
Neuronal Death ◽  
Delayed Neuronal Death ◽  
Unfolded Protein ◽  
Protein Response

scholarly journals GM1-Ganglioside-Mediated Activation of the Unfolded Protein Response Causes Neuronal Death in a Neurodegenerative Gangliosidosis

2004 ◽  
Vol 15 (5) ◽  
pp. 753-766 ◽  
Author(s):  
Alessandra Tessitore ◽  
Maria del P. Martin ◽  
Renata Sano ◽  
Yanjun Ma ◽  
Linda Mann ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Neuronal Death ◽  
Gm1 Ganglioside ◽  
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 Yokukansan Inhibits Neuronal Death during ER Stress by Regulating the Unfolded Protein Response

PLoS ONE ◽  
2010 ◽  
Vol 5 (10) ◽  
pp. e13280 ◽  
Author(s):  
Toru Hiratsuka ◽  
Shinsuke Matsuzaki ◽  
Shingo Miyata ◽  
Mitsuhiro Kinoshita ◽  
Kazuaki Kakehi ◽  
...  
Keyword(s):  
Er Stress ◽  
Unfolded Protein Response ◽  
Neuronal Death ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

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.

scholarly journals Effect of the mitochondrial unfolded protein response on hypoxic death and mitochondrial protein aggregation

2021 ◽  
Vol 12 (7) ◽  
Author(s):  
Junyi Yan ◽  
Chun-Ling Sun ◽  
Seokyung Shin ◽  
Marc Van Gilst ◽  
C. Michael Crowder
Keyword(s):  
Cell Death ◽  
Protein Aggregation ◽  
Unfolded Protein Response ◽  
Mitochondrial Protein ◽  
Early Event ◽  
Hypoxic Cell ◽  
C Elegans ◽  
Unfolded Protein ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

AbstractMitochondria are the main oxygen consumers in cells and as such are the primary organelle affected by hypoxia. All hypoxia pathology presumably derives from the initial mitochondrial dysfunction. An early event in hypoxic pathology in C. elegans is disruption of mitochondrial proteostasis with induction of the mitochondrial unfolded protein response (UPRmt) and mitochondrial protein aggregation. Here in C. elegans, we screen through RNAis and mutants that confer either strong resistance to hypoxic cell death or strong induction of the UPRmt to determine the relationship between hypoxic cell death, UPRmt activation, and hypoxia-induced mitochondrial protein aggregation (HIMPA). We find that resistance to hypoxic cell death invariantly mitigated HIMPA. We also find that UPRmt activation invariantly mitigated HIMPA. However, UPRmt activation was neither necessary nor sufficient for resistance to hypoxic death and vice versa. We conclude that UPRmt is not necessarily hypoxia protective against cell death but does protect from mitochondrial protein aggregation, one of the early hypoxic pathologies in C. elegans.

Protein aggregation in association with delayed neuronal death in rat model of brain ischemia

2008 ◽  
Vol 2 (1) ◽  
pp. 70-74
Author(s):  
Pengfei Ge ◽  
Tianfei Luo ◽  
Shuanglin Fu ◽  
Wenchen Li ◽  
Chonghao Wang ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Brain Ischemia ◽  
Rat Model ◽  
Neuronal Death ◽  
Delayed Neuronal Death

Unfolded protein response pathway, IRE1[alpha]-XBP1 is altered during adipogenesis in obese human adipocytes

2013 ◽  
pp. 1-1
Author(s):  
Philip Voyias ◽  
Ciara McCarthy ◽  
Adaikala Antonysunil ◽  
Warunee Kumsaiyai ◽  
Alison Harte ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Human Adipocytes ◽  
Unfolded Protein ◽  
Obese Human ◽  
Protein Response
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