scholarly journals Regulation der Chaperonaktivität im endoplasmatischen Retikulum

BIOspektrum ◽  
2020 ◽  
Vol 26 (6) ◽  
pp. 612-614
Author(s):  
Steffen Preissler
Keyword(s):  
Gene Expression ◽  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Protein Homeostasis ◽  
Short Term ◽  
Adaptive Changes ◽  
Unfolded Protein ◽  
Protein Load

Abstract Maintenance of protein homeostasis depends on cellular stress response pathways that mediate adaptive changes in gene expression. In the endoplasmic reticulum additional mechanisms adjust the availability of the abundant Hsp70-type chaperone, BiP, during short-term fluctuations in the unfolded protein load. Here, recent insights into the regulation of BiP by incorporation into inactive oligomers and reversible AMPylation are discussed.

scholarly journals Liposome-based DNA carriers may induce cellular stress response and change gene expression pattern in transfected cells

2011 ◽  
Vol 12 (1) ◽  
pp. 27 ◽  
Author(s):  
Anna Fiszer-Kierzkowska ◽  
Natalia Vydra ◽  
Aleksandra Wysocka-Wycisk ◽  
Zuzana Kronekova ◽  
Michał Jarząb ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stress Response ◽  
Expression Pattern ◽  
Cellular Stress ◽  
Gene Expression Pattern ◽  
Cellular Stress Response ◽  
Transfected Cells ◽  
Dna Carriers

Cellular stress response and apoptosis in cancer therapy

Blood ◽  
2001 ◽  
Vol 98 (9) ◽  
pp. 2603-2614 ◽  
Author(s):  
Ingrid Herr ◽  
Klaus-Michael Debatin
Keyword(s):  
Stress Response ◽  
Proteolytic Enzymes ◽  
Cellular Stress ◽  
Nuclear Factor Κb ◽  
Cellular Stress Response ◽  
Unfolded Protein ◽  
Anticancer Treatment ◽  
Mediate Cell ◽  
The Unfolded Protein Response ◽  
Protein Response

Abstract Anticancer treatment using cytotoxic drugs is considered to mediate cell death by activating key elements of the apoptosis program and the cellular stress response. While proteolytic enzymes (caspases) serve as main effectors of apoptosis, the mechanisms involved in activation of the caspase system are less clear. Two distinct pathways upstream of the caspase cascade have been identified. Death receptors, eg, CD95 (APO-1/Fas), trigger caspase-8, and mitochondria release apoptogenic factors (cytochrome c, Apaf-1, AIF), leading to the activation of caspase-9. The stressed endoplasmic reticulum (ER) contributes to apoptosis by the unfolded protein response pathway, which induces ER chaperones, and by the ER overload response pathway, which produces cytokines via nuclear factor-κB. Multiple other stress-inducible molecules, such as p53, JNK, AP-1, NF-κB, PKC/MAPK/ERK, and members of the sphingomyelin pathway have a profound influence on apoptosis. Understanding the complex interaction between different cellular programs provides insights into sensitivity or resistance of tumor cells and identifies molecular targets for rational therapeutic intervention strategies.

scholarly journals The Role of PERK in Understanding Development of Neurodegenerative Diseases

2021 ◽  
Vol 22 (15) ◽  
pp. 8146
Author(s):  
Garrett Dalton Smedley ◽  
Keenan E. Walker ◽  
Shauna H. Yuan
Keyword(s):  
Stress Response ◽  
Protein Kinase ◽  
Neurodegenerative Diseases ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Neural Cells ◽  
Review Of The Literature ◽  
Unfolded Protein ◽  
Protein Response

Neurodegenerative diseases are an ever-increasing problem for the rapidly aging population. Despite this, our understanding of how these neurodegenerative diseases develop and progress, is in most cases, rudimentary. Protein kinase RNA (PKR)-like ER kinase (PERK) comprises one of three unfolded protein response pathways in which cells attempt to manage cellular stress. However, because of its role in the cellular stress response and the far-reaching implications of this pathway, error within the PERK pathway has been shown to lead to a variety of pathologies. Genetic and clinical studies show a correlation between failure of the PERK pathway in neural cells and the development of neurodegeneration, but the wide array of methodology of these studies is presenting conflicting narratives about the role of PERK in these affected systems. Because of the connection between PERK and pathology, PERK has become a high value target of study for understanding neurodegenerative diseases and potentially how to treat them. Here, we present a review of the literature indexed in PubMed of the PERK pathway and some of the complexities involved in investigating the protein’s role in the development of neurodegenerative diseases as well as how it may act as a target for therapeutics.

scholarly journals A novel cellular stress response characterised by a rapid reorganisation of membranes of the endoplasmic reticulum

2012 ◽  
Vol 19 (12) ◽  
pp. 1896-1907 ◽  
Author(s):  
S Varadarajan ◽  
E T W Bampton ◽  
J L Smalley ◽  
K Tanaka ◽  
R E Caves ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Cellular Stress ◽  
Cellular Stress Response

Effects of thermal acclimation on transcriptional responses to acute heat stress in the eurythermal fish Gillichthys mirabilis (Cooper)

2011 ◽  
Vol 300 (6) ◽  
pp. R1373-R1383 ◽  
Author(s):  
Cheryl A. Logan ◽  
George N. Somero
Keyword(s):  
Gene Expression ◽  
Heat Stress ◽  
Stress Response ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Acclimation Temperature ◽  
Mild Stress ◽  
Gene Encoding ◽  
Gillichthys Mirabilis ◽  
Acute Heat Stress

The capacities of eurythermal ectotherms to withstand wide ranges of temperature are based, in part, on abilities to modulate gene expression as body temperature changes, notably genes encoding proteins of the cellular stress response. Here, using a complementary DNA microarray, we investigated the sequence in which cellular stress response-linked genes are expressed during acute heat stress, to elucidate how severity of stress affects the categories of genes changing expression. We also studied how prior acclimation history affected gene expression in response to acute heat stress. Eurythermal goby fish ( Gillichthys mirabilis ) were acclimated to 9 ± 0.5, 19 ± 0.5, and 28 ± 0.5°C for 1 mo. Then fish were given an acute heat ramp (4°C/h), and gill tissues were sampled every +4°C to monitor gene expression. The average onset temperature for a significant change in expression during acute stress increased by ∼2°C for each ∼10°C increase in acclimation temperature. For some genes, warm acclimation appeared to obviate the need for expression change until the most extreme temperatures were reached. Sequential expression of different categories of genes reflected severity of stress. Regardless of acclimation temperature, the gene encoding heat shock protein 70 ( HSP70) was upregulated strongly during mild stress; the gene encoding the proteolytic protein ubiquitin ( UBIQ) was upregulated at slightly higher temperatures; and a gene encoding a protein involved in cell cycle arrest and apoptosis, cyclin-dependent kinase inhibitor 1B ( CDKN1B), was upregulated only under extreme stress. The tiered, stress level-related expression patterns and the effects of acclimation on induction temperature yield new insights into the fundamental mechanisms of eurythermy.

scholarly journals Cellular Stress Response Gene Expression During Upper and Lower Body High Intensity Exercises

PLoS ONE ◽  
2017 ◽  
Vol 12 (1) ◽  
pp. e0171247 ◽  
Author(s):  
Andrzej Kochanowicz ◽  
Stanisław Sawczyn ◽  
Bartłomiej Niespodziński ◽  
Jan Mieszkowski ◽  
Kazimierz Kochanowicz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stress Response ◽  
High Intensity ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Lower Body ◽  
Response Gene ◽  
Stress Response Gene

scholarly journals Herpesviruses and the Unfolded Protein Response

2019 ◽  
Author(s):  
Benjamin P. Johnston ◽  
Craig McCormick
Keyword(s):  
Stress Response ◽  
Viral Replication ◽  
Unfolded Protein Response ◽  
Stress Responses ◽  
Cellular Stress ◽  
Cellular Stress Response ◽  
Negative Effects ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

Herpesviruses usurp cellular stress responses to avoid immune detection while simultaneously promoting viral replication and spread. The unfolded protein response (UPR) is an evolutionarily conserved stress response that is activated when the protein load in the ER saturates its chaperone folding capacity causing an accrual of misfolded proteins. Through translational and transcriptional reprogramming, the UPR aims to restore protein homeostasis; however, if this fails the cell undergoes apoptosis. It is commonly thought that many enveloped viruses, including herpesviruses, may activate the UPR due to saturation of the ER with nascent glycoproteins and thus these viruses may have evolved mechanisms to evade the potentially negative effects of UPR signaling. Over the past fifteen years there has been considerable effort to provide evidence that different viruses may reprogram the UPR to promote viral replication. Here we provide an overview of the molecular events of UPR activation, signaling and transcriptional outputs, and highlight key findings that demonstrate that the UPR is an important cellular stress response that herpesviruses have hijacked to facilitate persistent infection.

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