scholarly journals Modulation of the Unfolded Protein Response by Tauroursodeoxycholic Acid Counteracts Apoptotic Cell Death and Fibrosis in a Mouse Model for Secondary Biliary Liver Fibrosis

2017 ◽  
Vol 18 (1) ◽  
pp. 214 ◽  
Author(s):  
Annelies Paridaens ◽  
Sarah Raevens ◽  
Lindsey Devisscher ◽  
Eliene Bogaerts ◽  
Xavier Verhelst ◽  
...  
Keyword(s):  
Cell Death ◽  
Liver Fibrosis ◽  
Mouse Model ◽  
Unfolded Protein Response ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Tauroursodeoxycholic Acid ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals The unfolded protein response and its potential role in Huntington ́s disease elucidated by a systems biology approach

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 103 ◽  
Author(s):  
Ravi Kiran Reddy Kalathur ◽  
Joaquin Giner-Lamia ◽  
Susana Machado ◽  
Kameshwar R S Ayasolla ◽  
Matthias E. Futschik
Keyword(s):  
Cell Death ◽  
Unfolded Protein Response ◽  
Potential Role ◽  
Apoptotic Cell ◽  
Fatal Outcome ◽  
Neuronal Cell ◽  
Misfolded Proteins ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

Huntington ́s disease (HD) is a progressive, neurodegenerative disease with a fatal outcome. Although the disease-causing gene (huntingtin) has been known for over 20 years, the exact mechanisms leading to neuronal cell death are still controversial. One potential mechanism contributing to the massive loss of neurons observed in the brain of HD patients could be the unfolded protein response (UPR) activated by accumulation of misfolded proteins in the endoplasmic reticulum (ER). As an adaptive response to counter-balance accumulation of un- or misfolded proteins, the UPR upregulates transcription of chaperones, temporarily attenuates new translation, and activates protein degradation via the proteasome. However, persistent ER stress and an activated UPR can also cause apoptotic cell death. Although different studies have indicated a role for the UPR in HD, the evidence remains inconclusive. Here, we present extensive bioinformatic analyses that revealed UPR activation in different experimental HD models based on transcriptomic data. Accordingly, we have identified 58 genes, including RAB5A, HMGB1, CTNNB1, DNM1, TUBB, TSG101, EEF2, DYNC1H1 and SLC12A5 that provide a potential link between UPR and HD. To further elucidate the potential role of UPR as a disease-relevant process, we examined its connection to apoptosis based on molecular interaction data, and identified a set of 40 genes including ADD1, HSP90B1, IKBKB, IKBKG, RPS3A and LMNB1, which seem to be at the crossroads between these two important cellular processes.

scholarly journals A Peptidic Unconjugated GRP78/BiP Ligand Modulates the Unfolded Protein Response and Induces Prostate Cancer Cell Death

PLoS ONE ◽  
2012 ◽  
Vol 7 (10) ◽  
pp. e45690 ◽  
Author(s):  
Danilo Maddalo ◽  
Antje Neeb ◽  
Katja Jehle ◽  
Katja Schmitz ◽  
Claudia Muhle-Goll ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Death ◽  
Unfolded Protein Response ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Unfolded Protein ◽  
Cancer Cell Death ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Nonlinear relationship between ER Ca2+ depletion versus induction of the unfolded protein response, autophagy inhibition, and cell death

Cell Calcium ◽  
2018 ◽  
Vol 76 ◽  
pp. 48-61 ◽  
Author(s):  
Paula Szalai ◽  
Jan B. Parys ◽  
Geert Bultynck ◽  
Søren Brøgger Christensen ◽  
Poul Nissen ◽  
...  
Keyword(s):  
Cell Death ◽  
Unfolded Protein Response ◽  
Nonlinear Relationship ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response ◽  
Autophagy Inhibition

scholarly journals Netrin-1 Protects Hepatocytes Against Cell Death Through Sustained Translation During the Unfolded Protein Response

2016 ◽  
Vol 2 (3) ◽  
pp. 281-301.e9 ◽  
Author(s):  
Thomas Lahlali ◽  
Marie-Laure Plissonnier ◽  
Cristina Romero-López ◽  
Maud Michelet ◽  
Benjamin Ducarouge ◽  
...  
Keyword(s):  
Cell Death ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Loss of αA or αB-Crystallin Accelerates Photoreceptor Cell Death in a Mouse Model of P23H Autosomal Dominant Retinitis Pigmentosa

2021 ◽  
Vol 23 (1) ◽  
pp. 70
Author(s):  
Tiantian Wang ◽  
Jingyu Yao ◽  
Lin Jia ◽  
Patrice E. Fort ◽  
David N. Zacks
Keyword(s):  
Cell Death ◽  
Mouse Model ◽  
Unfolded Protein ◽  
Retinal Degenerations ◽  
Light Sensing ◽  
Cell Death Pathways ◽  
Αb Crystallin ◽  
The Unfolded Protein Response ◽  
Protein Response ◽  
Photoreceptor Death

Inherited retinal degenerations (IRD) are a leading cause of visual impairment and can result from mutations in any one of a multitude of genes. Mutations in the light-sensing protein rhodopsin (RHO) is a leading cause of IRD with the most common of those being a missense mutation that results in substitution of proline-23 with histidine. This variant, also known as P23H-RHO, results in rhodopsin misfolding, initiation of endoplasmic reticulum stress, the unfolded protein response, and activation of cell death pathways. In this study, we investigate the effect of α-crystallins on photoreceptor survival in a mouse model of IRD secondary to P23H-RHO. We find that knockout of either αA- or αB-crystallin results in increased intraretinal inflammation, activation of apoptosis and necroptosis, and photoreceptor death. Our data suggest an important role for the ⍺-crystallins in regulating photoreceptor survival in the P23H-RHO mouse model of IRD.

Sign in / Sign up

Export Citation Format

Share Document