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Cellular Stress Response in Health and Disease

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A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (31 October 2018) | Viewed by 91234

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Dr. Alessandra Stacchiotti

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1. Department of Biomedical Sciences for Health, University of Milan, Via Mangiagalli 31, 20133 Milan, Italy
2. UO Laboratorio di Morfologia Umana Applicata, IRCCS San Donato, 20133 Milan, Italy
Interests: translational preclinical models of diseases; metabolic diseases; oxidative damage; endoplasmic reticulum stress; mitochondria; autophagy; mitophagy; role of antioxidants; ageing; sirtuins; natural compounds to limit metabolic diseases; cardiovascular damage and sirtuins modulation; obesity and mitochondrial endoplasmic reticulum interplay; selective autophagy in aging and disease
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Dear Colleagues,

Stress is implied in cellular life, and according to the “hormesis principle”, a mild cellular stress is sometimes useful to best react against a more severe insult. Historically, we owe the seminal discovery of the “heat stress response” to the Italian scientist Ferruccio Ritossa in the 1960s, which demonstrated an intense transcriptional activity in chromosomal puffs in heated Drosophila salivary glands. Afterwards, heat shock proteins (HSPs) have been characterized not only in hyperthermia but also in the response to environmental, metabolic, or toxic inputs. In aging, a stressful reaction occurs because stress proteins are reduced. However, HSPs are not only inside cells but also in the extracellular environment in cancer, inflammation, and intercellular communication through exosomes. Besides classical HSPs, when homeostasis is disrupted, abnormal endoplasmic reticulum (ER) and mitochondrial stress triggers the unfolded protein response (UPR). This mechanism is dramatically involved in the pathogenesis of cancer, neurodegenerative diseases like Alzheimer’s, Parkinson’s, and amyotrophic lateral sclerosis, in retinal damage, and in cardiovascular and metabolic morbidities. So, strategies aimed at modulating ER stress or mitochondrial response are crucial. This Special Issue offers an Open Access forum that aims to bring together a collection of original research and review articles addressing the expanding field of cellular stress response and modulation. We hope to provide a stimulating resource for the fascinating subject of cell stress research. Suggested potential topics may be: hormesis; ER stress and mitochondrial stress in diseases; the role of HSPs in exercise and in longevity; molecular chaperones as therapeutic targets; exosomes and HSPs; and new models to study stress response

Dr. Alessandra Stacchiotti
Guest Editor

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Keywords

heat shock proteins
mitochondria-associated membranes
neurodegenerative disorders
ER stress response and UPR
metabolic disorders

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Published Papers (12 papers)

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Editorial

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6 pages, 1076 KiB

Open AccessEditorial

Exploring Cellular Stress Response and Chaperones

by Alessandra Stacchiotti

Cells 2019, 8(5), 408; https://doi.org/10.3390/cells8050408 - 2 May 2019

Cited by 11 | Viewed by 4833

Abstract

Since the pioneering discovery of heat shock proteins in Drosophila by Ferruccio Ritossa in 1960s, a long and exciting journey has been undertaken by molecular biologists and researchers worldwide. Not only lower organisms like worms, yeast, amoeba, and flies but also eukaryotes share common cellular response signals to stressful conditions that can arise from the outside but also from the inside. Moreover, extraordinary interplay between nucleus and subcellular organelles, and between different organelles, like mitochondria and the endoplasmic reticulum called mitochondria-associated endoplasmic reticulum membranes (MAMs), are involved in aging and human diseases like obesity, diabetes, inflammation, neurodegeneration, autoimmune diseases, atherosclerosis, and cancer. Actually, we know that to hit abnormal proteostasis and lipid exchanges in the endoplasmic reticulum is crucial to best guide effective therapies or discover new drugs. Indeed, restoration or impairment of endoplasmic reticulum shape and function lead to cellular homeostasis by autophagy or to final death generally by apoptosis or pyroptosis. This Special Issue collects current valuable articles or reviews on cellular stress research and each contribution opens a new window for further studies and hypothesis. I hope that readers interested in this fascinating topic may be stimulated to know more and more. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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Research

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15 pages, 2547 KiB

Open AccessArticle

Modulation of Protein Synthesis by eIF2α Phosphorylation Protects Cell from Heat Stress-Mediated Apoptosis

by Soyoung Park, Yohan Lim, Duckgue Lee, Rosalie Elvira, Ji-Min Lee, Man Ryul Lee and Jaeseok Han

Cells 2018, 7(12), 254; https://doi.org/10.3390/cells7120254 - 7 Dec 2018

Cited by 19 | Viewed by 5109

Abstract

Global warming poses a considerable threat to human health, necessitating a proper understanding of mechanisms underlying cell death in the pathogenesis of heat-related diseases. Although mechanisms governing cytoplasmic response to heat are well understood, processes regulating cellular response to disruption of proteostasis in the endoplasmic reticulum (ER) due to heat stress remain unclear. The current study reveals that hyperthermic conditions may lead to a disturbance of ER homeostasis, also known as ER stress. Subsequent activation of the unfolded protein response (UPR) resulted in concomitant induction of cell death. Among the three UPR signaling pathways, the eIF2α phosphorylation pathway, and not the IRE1α/ATF6α pathways, is likely the main contributor to cell death under heat stress. Considering the role of eIF2α in translational control, we investigated the protective effect of translation rate on heat stress-mediated cell death. When protein synthesis was attenuated using cycloheximide or homoharringtonine, cell death due to heat stress was significantly reduced. In summation, we propose that transient modulation of protein synthesis by eIF2α phosphorylation has a pivotal role in protecting cells from heat stress-induced apoptosis. Therefore, pharmacological agents that promote eIF2α phosphorylation or reduce ER stress may contribute to the development of promising therapeutic approaches against heat-related diseases. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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19 pages, 4080 KiB

Open AccessArticle

The ER Stress Inducer l-Azetidine-2-Carboxylic Acid Elevates the Levels of Phospho-eIF2α and of LC3-II in a Ca²⁺-Dependent Manner

by Gemma Roest, Evelien Hesemans, Kirsten Welkenhuyzen, Tomas Luyten, Nikolai Engedal, Geert Bultynck and Jan B. Parys

Cells 2018, 7(12), 239; https://doi.org/10.3390/cells7120239 - 30 Nov 2018

Cited by 14 | Viewed by 5604

Abstract

Accumulation of misfolded proteins in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) to reduce protein load and restore homeostasis, including via induction of autophagy. We used the proline analogue l-azetidine-2-carboxylic acid (AZC) to induce ER stress, and assessed its effect on autophagy and Ca²⁺ homeostasis. Treatment with 5 mM AZC did not induce poly adenosine diphosphate ribose polymerase (PARP) cleavage while levels of binding immunoglobulin protein (BiP) and phosphorylated eukaryotic translation initiation factor 2α (eIF2α) increased and those of activating transcription factor 6 (ATF6) decreased, indicating activation of the protein kinase RNA-like ER kinase (PERK) and the ATF6 arms of the UPR but not of apoptosis. AZC treatment in combination with bafilomycin A1 (Baf A1) led to elevated levels of the lipidated form of the autophagy marker microtubule-associated protein light chain 3 (LC3), pointing to activation of autophagy. Using the specific PERK inhibitor AMG PERK 44, we could deduce that activation of the PERK branch is required for the AZC-induced lipidation of LC3. Moreover, both the levels of phospho-eIF2α and of lipidated LC3 were strongly reduced when cells were co-treated with the intracellular Ca²⁺ chelator 1,2-bis(O-aminophenoxy)ethane-N,N,N′,N′-tetraaceticacid tetra(acetoxy-methyl) ester (BAPTA-AM) but not when co-treated with the Na⁺/K⁺ ATPase inhibitor ouabain, suggesting an essential role of Ca²⁺ in AZC-induced activation of the PERK arm of the UPR and LC3 lipidation. Finally, AZC did not trigger Ca²⁺ release from the ER though appeared to decrease the cytosolic Ca²⁺ rise induced by thapsigargin while also decreasing the time constant for Ca²⁺ clearance. The ER Ca²⁺ store content and mitochondrial Ca²⁺ uptake however remained unaffected. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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18 pages, 1983 KiB

Open AccessArticle

Proteomic Signatures of Clostridium difficile Stressed with Metronidazole, Vancomycin, or Fidaxomicin

by Sandra Maaß, Andreas Otto, Dirk Albrecht, Katharina Riedel, Anke Trautwein-Schult and Dörte Becher

Cells 2018, 7(11), 213; https://doi.org/10.3390/cells7110213 - 15 Nov 2018

Cited by 14 | Viewed by 4758

Abstract

The anaerobic pathogen Clostridium difficile is of growing significance for the health care system due to its increasing incidence and mortality. As C. difficile infection is both supported and treated by antibiotics, a deeper knowledge on how antimicrobial agents affect the physiology of this important pathogen may help to understand and prevent the development and spreading of antibiotic resistant strains. As the proteomic response of a cell to stress aims at counteracting the harmful effects of this stress, it can be expected that the pattern of a pathogen’s responses to antibiotic treatment will be dependent on the antibiotic mechanism of action. Hence, every antibiotic treatment is expected to result in a specific proteomic signature characterizing its mode of action. In the study presented here, the proteomic response of C. difficile 630∆erm to vancomycin, metronidazole, and fidaxomicin stress was investigated on the level of protein abundance and protein synthesis based on 2D PAGE. The quantification of 425 proteins of C. difficile allowed the deduction of proteomic signatures specific for each drug treatment. Indeed, these proteomic signatures indicate very specific cellular responses to each antibiotic with only little overlap of the responses. Whereas signature proteins for vancomycin stress fulfil various cellular functions, the proteomic signature of metronidazole stress is characterized by alterations of proteins involved in protein biosynthesis and protein degradation as well as in DNA replication, recombination, and repair. In contrast, proteins differentially expressed after fidaxomicin treatment can be assigned to amino acid biosynthesis, transcription, cell motility, and the cell envelope functions. Notably, the data provided by this study hint also at so far unknown antibiotic detoxification mechanisms. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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10 pages, 2200 KiB

Open AccessArticle

Insertion Defects of Mitochondrially Encoded Proteins Burden the Mitochondrial Quality Control System

by Braulio Vargas Möller-Hergt, Andreas Carlström, Tamara Suhm and Martin Ott

Cells 2018, 7(10), 172; https://doi.org/10.3390/cells7100172 - 17 Oct 2018

Cited by 4 | Viewed by 3493

Abstract

The mitochondrial proteome contains proteins from two different genetic systems. Proteins are either synthesized in the cytosol and imported into the different compartments of the organelle or directly produced in the mitochondrial matrix. To ensure proteostasis, proteins are monitored by the mitochondrial quality control system, which will degrade non-native polypeptides. Defective mitochondrial membrane proteins are degraded by membrane-bound AAA-proteases. These proteases are regulated by factors promoting protein turnover or preventing their degradation. Here we determined genetic interactions between the mitoribosome receptors Mrx15 and Mba1 with the quality control system. We show that simultaneous absence of Mrx15 and the regulators of the i-AAA protease Mgr1 and Mgr3 provokes respiratory deficiency. Surprisingly, mutants lacking Mrx15 were more tolerant against proteotoxic stress. Furthermore, yeast cells became hypersensitive against proteotoxic stress upon deletion of MBA1. Contrary to Mrx15, Mba1 cooperates with the regulators of the m-AAA and i-AAA proteases. Taken together, these results suggest that membrane protein insertion and mitochondrial AAA-proteases are functionally coupled, possibly reflecting an early quality control step during mitochondrial protein synthesis. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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21 pages, 3928 KiB

Open AccessArticle

Interplay between Endoplasmic Reticular Stress and Survivin in Colonic Epithelial Cells

by Rohit Gundamaraju, Ravichandra Vemuri, Wai Chin Chong, Stephen Myers, Shaghayegh Norouzi, Madhur D. Shastri and Rajaraman Eri

Cells 2018, 7(10), 171; https://doi.org/10.3390/cells7100171 - 15 Oct 2018

Cited by 17 | Viewed by 5708

Abstract

Sustained endoplasmic reticular stress (ERS) is implicated in aggressive metastasis of cancer cells and increased tumor cell proliferation. Cancer cells activate the unfolded protein response (UPR), which aids in cellular survival and adaptation to harsh conditions. Inhibition of apoptosis, in contrast, is a mechanism adopted by cancer cells with the help of the inhibitor of an apoptosis (IAP) class of proteins such as Survivin to evade cell death and gain a proliferative advantage. In this study, we aimed to reveal the interrelation between ERS and Survivin. We initially verified the expression of Survivin in Winnie (a mouse model of chronic ERS) colon tissues by using immunohistochemistry (IHC) and immunofluorescence (IF) in comparison with wild type Blk6 mice. Additionally, we isolated the goblet cells and determined the expression of Survivin by IF and protein validation. Tunicamycin was utilized at a concentration of 10 µg/mL to induce ERS in the LS174T cell line and the gene expression of the ERS markers was measured. This was followed by determination of inflammatory cytokines. Inhibition of ERS was carried out by 4Phenyl Butyric acid (4PBA) at a concentration of 10 mM to assess whether there was a reciprocation effect. The downstream cell death assays including caspase 3/7, Annexin V, and poly(ADP-ribose) polymerase (PARP) cleavage were evaluated in the presence of ERS and absence of ERS, which was followed by a proliferative assay (EdU click) with and without ERS. Correspondingly, we inhibited Survivin by YM155 at a concentration of 100 nM and observed the succeeding ERS markers and inflammatory markers. We also verified the caspase 3/7 assay. Our results demonstrate that ERS inhibition not only significantly reduced the UPR genes (Grp78, ATF6, PERK and XBP1) along with Survivin but also downregulated the inflammatory markers such as IL8, IL4, and IL6, which suggests a positive correlation between ERS and the inhibition of apoptosis. Furthermore, we provided evidence that ERS inhibition promoted apoptosis in LS174T cells and shortened the proliferation rate. Moreover, Survivin inhibition by YM155 led to a comparable effect as that of ERS inhibition, which includes attenuation of ERS genes and inflammatory markers as well as the promotion of programmed cell death via the caspase 3/7 pathway. Together, our results propose the interrelation between ERS and inhibition of apoptosis assigning a molecular and therapeutic target for cancer treatment. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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Review

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19 pages, 1130 KiB

Open AccessReview

Mitochondrial Quality Control Mechanisms and the PHB (Prohibitin) Complex

by Blanca Hernando-Rodríguez and Marta Artal-Sanz

Cells 2018, 7(12), 238; https://doi.org/10.3390/cells7120238 - 29 Nov 2018

Cited by 61 | Viewed by 9278

Abstract

Mitochondrial functions are essential for life, critical for development, maintenance of stem cells, adaptation to physiological changes, responses to stress, and aging. The complexity of mitochondrial biogenesis requires coordinated nuclear and mitochondrial gene expression, owing to the need of stoichiometrically assemble the oxidative phosphorylation (OXPHOS) system for ATP production. It requires, in addition, the import of a large number of proteins from the cytosol to keep optimal mitochondrial function and metabolism. Moreover, mitochondria require lipid supply for membrane biogenesis, while it is itself essential for the synthesis of membrane lipids. To achieve mitochondrial homeostasis, multiple mechanisms of quality control have evolved to ensure that mitochondrial function meets cell, tissue, and organismal demands. Herein, we give an overview of mitochondrial mechanisms that are activated in response to stress, including mitochondrial dynamics, mitophagy and the mitochondrial unfolded protein response (UPR^mt). We then discuss the role of these stress responses in aging, with particular focus on Caenorhabditis elegans. Finally, we review observations that point to the mitochondrial prohibitin (PHB) complex as a key player in mitochondrial homeostasis, being essential for mitochondrial biogenesis and degradation, and responding to mitochondrial stress. Understanding how mitochondria responds to stress and how such responses are regulated is pivotal to combat aging and disease. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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15 pages, 3359 KiB

Open AccessFeature PaperReview

Hsp60 in Skeletal Muscle Fiber Biogenesis and Homeostasis: From Physical Exercise to Skeletal Muscle Pathology

by Antonella Marino Gammazza, Filippo Macaluso, Valentina Di Felice, Francesco Cappello and Rosario Barone

Cells 2018, 7(12), 224; https://doi.org/10.3390/cells7120224 - 22 Nov 2018

Cited by 34 | Viewed by 10301

Abstract

Hsp60 is a molecular chaperone classically described as a mitochondrial protein with multiple roles in health and disease, participating to the maintenance of protein homeostasis. It is well known that skeletal muscle is a complex tissue, rich in proteins, that is, subjected to continuous rearrangements, and this homeostasis is affected by many different types of stimuli and stresses. The regular exercise induces specific histological and biochemical adaptations in skeletal muscle fibers, such as hypertrophy and an increase of mitochondria activity and oxidative capacity. The current literature is lacking in information regarding Hsp60 involvement in skeletal muscle fiber biogenesis and regeneration during exercise, and in disease conditions. Here, we briefly discuss the functions of Hsp60 in skeletal muscle fibers during exercise, inflammation, and ageing. Moreover, the potential usage of Hsp60 as a marker for disease and the evaluation of novel treatment options is also discussed. However, some questions remain open, and further studies are needed to better understand Hsp60 involvement in skeletal muscle homeostasis during exercise and in pathological condition. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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20 pages, 1793 KiB

Open AccessReview

Metabolic Stress in the Immune Function of T Cells, Macrophages and Dendritic Cells

by Charlotte Domblides, Lydia Lartigue and Benjamin Faustin

Cells 2018, 7(7), 68; https://doi.org/10.3390/cells7070068 - 29 Jun 2018

Cited by 56 | Viewed by 8281

Abstract

Innate and adaptive immune cells from myeloid and lymphoid lineages resolve host infection or cell stress by mounting an appropriate and durable immune response. Upon sensing of cellular insults, immune cells become activated and undergo rapid and efficient functional changes to unleash biosynthesis of macromolecules, proliferation, survival, and trafficking; unprecedented events among other mammalian cells within the host. These changes must become operational within restricted timing to rapidly control the insult and to avoid tissue damage and pathogen spread. Such changes occur at high energy cost. Recent advances have established that plasticity of immune functions occurs in distinct metabolic stress features. Evidence has accumulated to indicate that specific metabolic signatures dictate appropriate immune functions in both innate and adaptive immunity. Importantly, recent studies have shed light on whether successfully manipulating particular metabolic targets is sufficient to modulate immune function and polarization, thereby offering strong therapeutic potential for various common immune-mediated diseases, including inflammation and autoimmune-associated diseases and cancer. In this review, we detail how cellular metabolism controls immune function and phenotype within T cells and macrophages particularly, and the distinct molecular metabolic programming and targets instrumental to engage this regulation. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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35 pages, 1252 KiB

Open AccessReview

Endoplasmic Reticulum Stress in Metabolic Disorders

by Rose Ghemrawi, Shyue-Fang Battaglia-Hsu and Carole Arnold

Cells 2018, 7(6), 63; https://doi.org/10.3390/cells7060063 - 19 Jun 2018

Cited by 157 | Viewed by 15463

Abstract

Metabolic disorders have become among the most serious threats to human health, leading to severe chronic diseases such as obesity, type 2 diabetes, and non-alcoholic fatty liver disease, as well as cardiovascular diseases. Interestingly, despite the fact that each of these diseases has different physiological and clinical symptoms, they appear to share certain pathological traits such as intracellular stress and inflammation induced by metabolic disturbance stemmed from over nutrition frequently aggravated by a modern, sedentary life style. These modern ways of living inundate cells and organs with saturating levels of sugar and fat, leading to glycotoxicity and lipotoxicity that induce intracellular stress signaling ranging from oxidative to ER stress response to cope with the metabolic insults (Mukherjee, et al., 2015). In this review, we discuss the roles played by cellular stress and its responses in shaping metabolic disorders. We have summarized here current mechanistic insights explaining the pathogenesis of these disorders. These are followed by a discussion of the latest therapies targeting the stress response pathways. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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24 pages, 2567 KiB

Open AccessFeature PaperReview

Unfolding the Endoplasmic Reticulum of a Social Amoeba: Dictyostelium discoideum as a New Model for the Study of Endoplasmic Reticulum Stress

by Eunice Domínguez-Martín, Mariana Hernández-Elvira, Olivier Vincent, Roberto Coria and Ricardo Escalante

Cells 2018, 7(6), 56; https://doi.org/10.3390/cells7060056 - 10 Jun 2018

Cited by 14 | Viewed by 8684

Abstract

The endoplasmic reticulum (ER) is a membranous network with an intricate dynamic architecture necessary for various essential cellular processes. Nearly one third of the proteins trafficking through the secretory pathway are folded and matured in the ER. Additionally, it acts as calcium storage, and it is a main source for lipid biosynthesis. The ER is highly connected with other organelles through regions of membrane apposition that allow organelle remodeling, as well as lipid and calcium traffic. Cells are under constant changes due to metabolic requirements and environmental conditions that challenge the ER network’s maintenance. The unfolded protein response (UPR) is a signaling pathway that restores homeostasis of this intracellular compartment upon ER stress conditions by reducing the load of proteins, and by increasing the processes of protein folding and degradation. Significant progress on the study of the mechanisms that restore ER homeostasis was achieved using model organisms such as yeast, Arabidopsis, and mammalian cells. In this review, we address the current knowledge on ER architecture and ER stress response in Dictyostelium discoideum. This social amoeba alternates between unicellular and multicellular phases and is recognized as a valuable biomedical model organism and an alternative to yeast, particularly for the presence of traits conserved in animal cells that were lost in fungi. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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9 pages, 747 KiB

Open AccessPerspective

Perspective: Mitochondria-ER Contacts in Metabolic Cellular Stress Assessed by Microscopy

by Alessandra Stacchiotti, Gaia Favero, Antonio Lavazza, Raquel Garcia-Gomez, Maria Monsalve and Rita Rezzani

Cells 2019, 8(1), 5; https://doi.org/10.3390/cells8010005 - 21 Dec 2018

Cited by 23 | Viewed by 8127

Abstract

The interplay of mitochondria with the endoplasmic reticulum and their connections, called mitochondria-ER contacts (MERCs) or mitochondria-associated ER membranes (MAMs), are crucial hubs in cellular stress. These sites are essential for the passage of calcium ions, reactive oxygen species delivery, the sorting of lipids in whole-body metabolism. In this perspective article, we focus on microscopic evidences of the pivotal role of MERCs/MAMs and their changes in metabolic diseases, like obesity, diabetes, and neurodegeneration. Full article

(This article belongs to the Special Issue Cellular Stress Response in Health and Disease)

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