Cell Stress & Chaperones最新文献

{"title":"Introduction of Dimitra Bourboulia as the new Editor-in-Chief of Cell Stress & Chaperones","authors":"Lawrence E. Hightower","doi":"10.1016/j.cstres.2024.01.008","DOIUrl":"10.1016/j.cstres.2024.01.008","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 49-50"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000488/pdfft?md5=14a07f4491cf809076bffbdc5ab6e7d3&pid=1-s2.0-S1355814524000488-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139680719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial: A new chapter for Cell Stress and Chaperones","authors":"Dimitra Bourboulia (Editor-in-Chief) , Laura J. Blair , Melody S. Clark , Adrienne L. Edkins , Lawrence E. Hightower , Mehdi Mollapour , Veena Prahlad , Elizabeth A. Repasky , Manuela Truebano , Andrew W. Truman , Matthias C. Truttmann , Patricija van Oosten-Hawle , Mark R. Woodford","doi":"10.1016/j.cstres.2024.01.007","DOIUrl":"10.1016/j.cstres.2024.01.007","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 113-115"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000476/pdfft?md5=f160615f52fd40ee593bed74b402c796&pid=1-s2.0-S1355814524000476-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139680718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone","authors":"Mohammad Al-Ansari ,&nbsp;Taylor Fitzsimons ,&nbsp;Wenbin Wei ,&nbsp;Martin W. Goldberg ,&nbsp;Takekazu Kunieda ,&nbsp;Roy A. Quinlan","doi":"10.1016/j.cstres.2023.12.001","DOIUrl":"https://doi.org/10.1016/j.cstres.2023.12.001","url":null,"abstract":"<div><p>The tardigrade <em>Ramazzottius varieornatus</em> has remarkable resilience to a range of environmental stresses. In this study, we have characterised two members of the small heat shock protein (sHSP) family in <em>R. varieornatus</em>, HSP20–3 and HSP20–6. These are the most highly upregulated sHSPs in response to a 24 h heat shock at 35 ⁰C of adult tardigrades with HSP20–3 being one of the most highly upregulated gene in the whole transcriptome. Both <em>R. varieornatus</em> sHSPs and the human sHSP, CRYAB (HSPB5), were produced recombinantly for comparative structure-function studies. HSP20–3 exhibited a superior chaperone activity than human CRYAB in a heat-induced protein aggregation assay. Both tardigrade sHSPs also formed larger oligomers than CRYAB as assessed by size exclusion chromatography and transmission electron microscopy of negatively stained samples. Whilst both HSP20–3 and HSP20–6 formed particles that were variable in size and larger than the particles formed by CRYAB, only HSP20–3 formed filament-like structures. The particles and filament-like structures formed by HSP20–3 appear inter-related as the filament-like structures often had particles located at their ends. Sequence analyses identified two unique features; an insertion in the middle region of the N-terminal domain (NTD) and preceding the critical-sequence identified in CRYAB, as well as a repeated QNTN-motif located in the C-terminal domain of HSP20–3. The NTD insertion is expected to affect protein-protein interactions and subunit oligomerisation. Removal of the repeated QNTN-motif abolished HSP20–3 chaperone activity and also affected the assembly of the filament-like structures. We discuss the potential contribution of HSP20–3 to protein condensate formation.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 51-65"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814523022435/pdfft?md5=23b54decf36a98c576836709e36a02a9&pid=1-s2.0-S1355814523022435-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139700088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stress biology: Complexity and multifariousness in health and disease","authors":"Matthias P. Mayer ,&nbsp;Laura Blair ,&nbsp;Gregory L. Blatch ,&nbsp;Thiago J. Borges ,&nbsp;Ahmed Chadli ,&nbsp;Gabriela Chiosis ,&nbsp;Aurélie de Thonel ,&nbsp;Albena Dinkova-Kostova ,&nbsp;Heath Ecroyd ,&nbsp;Adrienne L. Edkins ,&nbsp;Takanori Eguchi ,&nbsp;Monika Fleshner ,&nbsp;Kevin P. Foley ,&nbsp;Sotirios Fragkostefanakis ,&nbsp;Jason Gestwicki ,&nbsp;Pierre Goloubinoff ,&nbsp;Jennifer A. Heritz ,&nbsp;Christine M. Heske ,&nbsp;Jonathan D. Hibshman ,&nbsp;Jenny Joutsen ,&nbsp;Tawanda Zininga","doi":"10.1016/j.cstres.2024.01.006","DOIUrl":"10.1016/j.cstres.2024.01.006","url":null,"abstract":"<div><p>Preserving and regulating cellular homeostasis in the light of changing environmental conditions or developmental processes is of pivotal importance for single cellular and multicellular organisms alike. To counteract an imbalance in cellular homeostasis transcriptional programs evolved, called the heat shock response, unfolded protein response, and integrated stress response, that act cell-autonomously in most cells but in multicellular organisms are subjected to cell-nonautonomous regulation. These transcriptional programs downregulate the expression of most genes but increase the expression of heat shock genes, including genes encoding molecular chaperones and proteases, proteins involved in the repair of stress-induced damage to macromolecules and cellular structures. Sixty-one years after the discovery of the heat shock response by Ferruccio Ritossa, many aspects of stress biology are still enigmatic. Recent progress in the understanding of stress responses and molecular chaperones was reported at the 12th International Symposium on Heat Shock Proteins in Biology, Medicine and the Environment in the Old Town Alexandria, VA, USA from 28th to 31st of October 2023.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 143-157"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000464/pdfft?md5=ae52b2fabe5d4714b69d76b11a44f370&pid=1-s2.0-S1355814524000464-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139680721","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"J-domain proteins: From molecular mechanisms to diseases","authors":"Jaroslaw Marszalek ,&nbsp;Paolo De Los Rios ,&nbsp;Douglas Cyr ,&nbsp;Matthias P. Mayer ,&nbsp;Vasista Adupa ,&nbsp;Claes Andréasson ,&nbsp;Gregory L. Blatch ,&nbsp;Janice E.A. Braun ,&nbsp;Jeffrey L. Brodsky ,&nbsp;Bernd Bukau ,&nbsp;J. Paul Chapple ,&nbsp;Charlotte Conz ,&nbsp;Sébastien Dementin ,&nbsp;Pierre Genevaux ,&nbsp;Olivier Genest ,&nbsp;Pierre Goloubinoff ,&nbsp;Jason Gestwicki ,&nbsp;Colin M. Hammond ,&nbsp;Justin K. Hines ,&nbsp;Koji Ishikawa ,&nbsp;Harm H. Kampinga","doi":"10.1016/j.cstres.2023.12.002","DOIUrl":"https://doi.org/10.1016/j.cstres.2023.12.002","url":null,"abstract":"<div><p>J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 21-33"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814523022447/pdfft?md5=f5dfa8f62227a3efe0a4ef2743c9a536&pid=1-s2.0-S1355814523022447-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139694713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neuroprotective effects of cordycepin inhibit glutamate-induced apoptosis in hippocampal neurons","authors":"Huizhen Sun ,&nbsp;Shanshan Wei ,&nbsp;Yanchun Gong ,&nbsp;Kaizhi Ding ,&nbsp;Shan Tang ,&nbsp;Wei Sun ,&nbsp;Chunhua Yuan ,&nbsp;Liping Huang ,&nbsp;Zhibing Liu ,&nbsp;Chong Chen ,&nbsp;Lihua Yao","doi":"10.1016/j.cstres.2024.01.001","DOIUrl":"10.1016/j.cstres.2024.01.001","url":null,"abstract":"<div><p>Glutamate is a neurotransmitter that can cause excitatory neurotoxicity when its extracellular concentration is too high, leading to disrupted calcium balance and increased production of reactive oxygen species (ROS). Cordycepin, a nucleoside adenosine derivative, has been shown to protect against excitatory neurotoxicity induced by glutamate. To investigate its potential neuroprotective effects, the present study employed fluorescence detection and spectrophotometry techniques to analyze primary hippocampal-cultured neurons. The results showed that glutamate toxicity reduced hippocampal neuron viability, increased ROS production, and increased intracellular calcium levels. Additionally, glutamate-induced cytotoxicity activated acetylcholinesterase and decreased glutathione levels. However, cordycepin inhibited glutamate-induced cell death, improved cell viability, reduced ROS production, and lowered Ca²⁺ levels. It also inhibited acetylcholinesterase activation and increased glutathione levels. This study suggests that cordycepin can protect against glutamate-induced neuronal injury in cell models, and this effect was inhibited by adenosine A₁ receptor blockers, indicating that its neuroprotective effect is achieved through activation of the adenosine A₁ receptor.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 10-20"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000014/pdfft?md5=f0db43e9981ef4fe2b3074037cfa8264&pid=1-s2.0-S1355814524000014-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139466346","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat shock response during the resolution of inflammation and its progressive suppression in chronic-degenerative inflammatory diseases","authors":"Helena Trevisan Schroeder ,&nbsp;Carlos Henrique De Lemos Muller ,&nbsp;Thiago Gomes Heck ,&nbsp;Mauricio Krause ,&nbsp;Paulo Ivo Homem de Bittencourt","doi":"10.1016/j.cstres.2024.01.002","DOIUrl":"10.1016/j.cstres.2024.01.002","url":null,"abstract":"<div><p>The heat shock response (HSR) is a crucial biochemical pathway that orchestrates the resolution of inflammation, primarily under proteotoxic stress conditions. This process hinges on the upregulation of heat shock proteins (HSPs) and other chaperones, notably the 70 kDa family of heat shock proteins, under the command of the heat shock transcription factor-1. However, in the context of chronic degenerative disorders characterized by persistent low-grade inflammation (such as insulin resistance, obesity, type 2 diabetes, nonalcoholic fatty liver disease, and cardiovascular diseases) a gradual suppression of the HSR does occur. This work delves into the mechanisms behind this phenomenon. It explores how the Western diet and sedentary lifestyle, culminating in the endoplasmic reticulum stress within adipose tissue cells, trigger a cascade of events. This cascade includes the unfolded protein response and activation of the NOD-like receptor pyrin domain-containing protein-3 inflammasome, leading to the emergence of the senescence-associated secretory phenotype and the propagation of inflammation throughout the body. Notably, the activation of the NOD-like receptor pyrin domain-containing protein-3 inflammasome not only fuels inflammation but also sabotages the HSR by degrading human antigen R, a crucial mRNA-binding protein responsible for maintaining heat shock transcription factor-1 mRNA expression and stability on heat shock gene promoters. This paper underscores the imperative need to comprehend how chronic inflammation stifles the HSR and the clinical significance of evaluating the HSR using cost-effective and accessible tools. Such understanding is pivotal in the development of innovative strategies aimed at the prevention and treatment of these chronic inflammatory ailments, which continue to take a heavy toll on global health and well-being.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 116-142"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000427/pdfft?md5=55cd204d16204e461dac20707cfddd02&pid=1-s2.0-S1355814524000427-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139512047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The dance of proteostasis and metabolism: Unveiling the caloristatic controlling switch","authors":"Helena Trevisan Schroeder ,&nbsp;Carlos Henrique De Lemos Muller ,&nbsp;Thiago Gomes Heck ,&nbsp;Mauricio Krause ,&nbsp;Paulo Ivo Homem de Bittencourt Jr","doi":"10.1016/j.cstres.2024.02.002","DOIUrl":"10.1016/j.cstres.2024.02.002","url":null,"abstract":"<div><p>The heat shock response (HSR) is an ancient and evolutionarily conserved mechanism designed to restore cellular homeostasis following proteotoxic challenges. However, it has become increasingly evident that disruptions in energy metabolism also trigger the HSR. This interplay between proteostasis and energy regulation is rooted in the fundamental need for ATP to fuel protein synthesis and repair, making the HSR an essential component of cellular energy management. Recent findings suggest that the origins of proteostasis-defending systems can be traced back over 3.6 billion years, aligning with the emergence of sugar kinases that optimized glycolysis around 3.594 billion years ago. This evolutionary connection is underscored by the spatial similarities between the nucleotide-binding domain of HSP70, the key player in protein chaperone machinery, and hexokinases. The HSR serves as a hub that integrates energy metabolism and resolution of inflammation, further highlighting its role in maintaining cellular homeostasis. Notably, 5′-adenosine monophosphate-activated protein kinase emerges as a central regulator, promoting the HSR during predominantly proteotoxic stress while suppressing it in response to predominantly metabolic stress. The complex relationship between 5′-adenosine monophosphate-activated protein kinase and the HSR is finely tuned, with paradoxical effects observed under different stress conditions. This delicate equilibrium, known as caloristasis, ensures that cellular homeostasis is maintained despite shifting environmental and intracellular conditions. Understanding the caloristatic controlling switch at the heart of this interplay is crucial. It offers insights into a wide range of conditions, including glycemic control, obesity, type 2 diabetes, cardiovascular and neurodegenerative diseases, reproductive abnormalities, and the optimization of exercise routines. These findings highlight the profound interconnectedness of proteostasis and energy metabolism in cellular function and adaptation.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 175-200"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000506/pdfft?md5=df23390de81c7154b8ea23c0325f2b39&pid=1-s2.0-S1355814524000506-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139706204","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Endoplasmic reticulum stress-mediated cell death in cardiovascular disease","authors":"Yajuan An ,&nbsp;Xinshuang Wang ,&nbsp;Xiuju Guan ,&nbsp;Peng Yuan ,&nbsp;Yue Liu ,&nbsp;Liping Wei ,&nbsp;Fei Wang ,&nbsp;Xin Qi","doi":"10.1016/j.cstres.2023.12.003","DOIUrl":"10.1016/j.cstres.2023.12.003","url":null,"abstract":"<div><p>The endoplasmic reticulum (ER) plays a vital function in maintaining cellular homeostasis. Endoplasmic reticulum stress (ERS) can trigger various modes of cell death by activating the unfolded protein response (UPR) signaling pathway. Cell death plays a crucial role in the occurrence and development of diseases such as cancer, liver diseases, neurological diseases, and cardiovascular diseases. Several cardiovascular diseases including hypertension, atherosclerosis, and heart failure are associated with ER stress. ER stress-mediated cell death is of interest in cardiovascular disease. Moreover, an increasing body of evidence supports the potential of modulating ERS for treating cardiovascular disease. This paper provides a comprehensive review of the UPR signaling pathway, the mechanisms that induce cell death, and the modes of cell death in cardiovascular diseases. Additionally, we discuss the mechanisms of ERS and UPR in common cardiovascular diseases, along with potential therapeutic strategies.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 158-174"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814523022459/pdfft?md5=24ce80cb99147fa43e01584481cb0066&pid=1-s2.0-S1355814523022459-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139721785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones","authors":"Megan M. Mitchem ,&nbsp;Courtney Shrader ,&nbsp;Elizabeth Abedi,&nbsp;Andrew W. Truman","doi":"10.1016/j.cstres.2023.11.001","DOIUrl":"https://doi.org/10.1016/j.cstres.2023.11.001","url":null,"abstract":"<div><p>The activity of the Hsp70 molecular chaperone is regulated by a suite of helper co-chaperones that include J-proteins. Studies on J-proteins have historically focused on their expression, localization, and activation of Hsp70. There is growing evidence that the post-translational modifications (PTMs) of chaperones (the chaperone code) fine-tune chaperone function. This mini-review summarizes the current understanding of the role and regulation of PTMs on the major J-proteins Ydj1 and DNAJA1. Understanding these PTMs may provide novel therapeutic avenues for targeting chaperone activity in cancer and neurodegenerative diseases.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 1-9"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814523022411/pdfft?md5=019c512af7e06d895a68e3542273f7b7&pid=1-s2.0-S1355814523022411-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139674810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}