scholarly journals The Role of Mitophagy in Regulating Cell Death

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Sunao Li ◽  
Jiaxin Zhang ◽  
Chao Liu ◽  
Qianliang Wang ◽  
Jun Yan ◽  
...  
Keyword(s):  
Cell Death ◽  
Cytosolic Calcium ◽  
Cellular Functions ◽  
Power Generators ◽  
Unfolded Protein ◽  
Mitochondrial Homeostasis ◽  
Cell Death Pathways ◽  
Health And Disease ◽  
Protein Response

Mitochondria are multifaceted organelles that serve to power critical cellular functions, including act as power generators of the cell, buffer cytosolic calcium overload, production of reactive oxygen species, and modulating cell survival. The structure and the cellular location of mitochondria are critical for their function and depend on highly regulated activities such as mitochondrial quality control (MQC) mechanisms. The MQC is regulated by several sets of processes: mitochondrial biogenesis, mitochondrial fusion and fission, mitophagy, and other mitochondrial proteostasis mechanisms such as mitochondrial unfolded protein response (mtUPR) or mitochondrial-derived vesicles (MDVs). These processes are important for the maintenance of mitochondrial homeostasis, and alterations in the mitochondrial function and signaling are known to contribute to the dysregulation of cell death pathways. Recent studies have uncovered regulatory mechanisms that control the activity of the key components for mitophagy. In this review, we discuss how mitophagy is controlled and how mitophagy impinges on health and disease through regulating cell death.

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.

scholarly journals ER Stress Signaling and its Role in Cancer Cell Death

2021 ◽  
Vol 8 (S1-Feb) ◽  
pp. 81-86
Author(s):  
Kavitha C V ◽  
Poornima S K
Keyword(s):  
Cell Death ◽  
Er Stress ◽  
Cancer Cell ◽  
Low Oxygen ◽  
Cellular Functions ◽  
Unfolded Protein ◽  
Cancer Cell Death ◽  
The Unfolded Protein Response ◽  
Protein Response ◽  
Cellular Dysfunction

The endoplasmic-reticulum (ER) stress response represents a cellular process that is provoked by a number of circumstances that disturb folding of proteins in the ER. An evolutionarily conserved adaptive mechanismhas been developed by Eukaryotic cells, termed the unfolded protein response (UPR) to clear the unfolded proteins and restore ER homeostasis. The cellular functions deteriorate, in the conditions when ER stress cannot be reversed and this sometime lead to cell death.The poor vascularization, low oxygen supply, nutrient deprivation, and acidic pH in the tumor microenvironment stimulate the ER stress. UPR has been shown to exert a significantcytoprotective part in speedily growing cancers as it helps folding of newly synthesized proteins required for the growth of the tumor.Accumulating evidence showed that ER stress-induced cellular dysfunction and cell death are the major contributors to many diseases and making the modulators of ER stress pathways potentially attractive targets for therapeutics discovery. Herein, we will briefly summarize gesticulating cascade activated upon ER stress and its role in cancer cell death.

scholarly journals GSK-3: A Bifunctional Role in Cell Death Pathways

2012 ◽  
Vol 2012 ◽  
pp. 1-11 ◽  
Author(s):  
Keith M. Jacobs ◽  
Sandeep R. Bhave ◽  
Daniel J. Ferraro ◽  
Jerry J. Jaboin ◽  
Dennis E. Hallahan ◽  
...  
Keyword(s):  
Cell Death ◽  
Glycogen Synthase ◽  
Molecular Target ◽  
Glycogen Synthase Kinase 3 ◽  
Cellular Functions ◽  
Cell Death Pathways ◽  
Wide Range ◽  
Growth Metabolism ◽  
Significant Attention

Although glycogen synthase kinase-3 beta (GSK-3β) was originally named for its ability to phosphorylate glycogen synthase and regulate glucose metabolism, this multifunctional kinase is presently known to be a key regulator of a wide range of cellular functions. GSK-3βis involved in modulating a variety of functions including cell signaling, growth metabolism, and various transcription factors that determine the survival or death of the organism. Secondary to the role of GSK-3βin various diseases including Alzheimer’s disease, inflammation, diabetes, and cancer, small molecule inhibitors of GSK-3βare gaining significant attention. This paper is primarily focused on addressing the bifunctional or conflicting roles of GSK-3βin both the promotion of cell survival and of apoptosis. GSK-3βhas emerged as an important molecular target for drug development.

Role of the unfolded protein response in cell death

APOPTOSIS ◽  
2006 ◽  
Vol 11 (1) ◽  
pp. 5-13 ◽  
Author(s):  
R. Kim ◽  
M. Emi ◽  
K. Tanabe ◽  
S. Murakami
Keyword(s):  
Cell Death ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

The role of the unfolded protein response in chemoresistance and cell death

Pancreatology ◽  
2016 ◽  
Vol 16 (1) ◽  
pp. S46-S47
Author(s):  
P. Dauer ◽  
O. McGinn ◽  
X. Zhao ◽  
N. Arora ◽  
M. Singh ◽  
...  
Keyword(s):  
Cell Death ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals The Role of Nitric Oxide and the Unfolded Protein Response in Cytokine-Induced -Cell Death

Diabetes ◽  
2007 ◽  
Vol 57 (1) ◽  
pp. 124-132 ◽  
Author(s):  
K. T. Chambers ◽  
J. A. Unverferth ◽  
S. M. Weber ◽  
R. C. Wek ◽  
F. Urano ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Cell Death ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Confounding Roles of ER Stress and the Unfolded Protein Response in Skeletal Muscle Atrophy

2021 ◽  
Vol 22 (5) ◽  
pp. 2567
Author(s):  
Yann S. Gallot ◽  
Kyle R. Bohnert
Keyword(s):  
Skeletal Muscle ◽  
Er Stress ◽  
Unfolded Protein Response ◽  
Smooth Endoplasmic Reticulum ◽  
Skeletal Muscle Atrophy ◽  
Unfolded Protein ◽  
The Individual ◽  
The Unfolded Protein Response ◽  
Protein Response

Skeletal muscle is an essential organ, responsible for many physiological functions such as breathing, locomotion, postural maintenance, thermoregulation, and metabolism. Interestingly, skeletal muscle is a highly plastic tissue, capable of adapting to anabolic and catabolic stimuli. Skeletal muscle contains a specialized smooth endoplasmic reticulum (ER), known as the sarcoplasmic reticulum, composed of an extensive network of tubules. In addition to the role of folding and trafficking proteins within the cell, this specialized organelle is responsible for the regulated release of calcium ions (Ca2+) into the cytoplasm to trigger a muscle contraction. Under various stimuli, such as exercise, hypoxia, imbalances in calcium levels, ER homeostasis is disturbed and the amount of misfolded and/or unfolded proteins accumulates in the ER. This accumulation of misfolded/unfolded protein causes ER stress and leads to the activation of the unfolded protein response (UPR). Interestingly, the role of the UPR in skeletal muscle has only just begun to be elucidated. Accumulating evidence suggests that ER stress and UPR markers are drastically induced in various catabolic stimuli including cachexia, denervation, nutrient deprivation, aging, and disease. Evidence indicates some of these molecules appear to be aiding the skeletal muscle in regaining homeostasis whereas others demonstrate the ability to drive the atrophy. Continued investigations into the individual molecules of this complex pathway are necessary to fully understand the mechanisms.

scholarly journals Cell Death Pathways and Viruses: Role of microRNAs

2021 ◽  
Author(s):  
Javid Sadri Nahand ◽  
Layla Shojaie ◽  
Seyed Amirreza Akhlagh ◽  
Mohammad Saeid Ebrahimi ◽  
Hamid Reza Mirzaei ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Death Pathways
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