Cell Stress & Chaperones最新文献

{"title":"Editorial Board Members/Copyright","authors":"","doi":"10.1016/S1355-8145(25)00014-8","DOIUrl":"10.1016/S1355-8145(25)00014-8","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 2","pages":"Page i"},"PeriodicalIF":3.3,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143628277","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":"CHOP aggravates hepatocyte apoptosis upon endoplasmic reticulum stress by downregulating autophagy","authors":"Jia-Yu Wu ,&nbsp;Bing Han ,&nbsp;Ting Yang ,&nbsp;Lu Zheng ,&nbsp;Yi-Xin Guo ,&nbsp;Jia-Yao Li ,&nbsp;Xiao-Yu Guo ,&nbsp;Huan-Huan Yin ,&nbsp;Ru-Jia Xie","doi":"10.1016/j.cstres.2025.02.005","DOIUrl":"10.1016/j.cstres.2025.02.005","url":null,"abstract":"<div><div>Endoplasmic reticulum (ER) stress-induced apoptosis plays a crucial role in various liver diseases. Hepatocytes respond to ER stress by activating the unfolded protein response and autophagy, which is essential for maintaining ER homeostasis. However, failure to restore ER balance via autophagy contributes to apoptosis. In this study, we aimed to explore the role of C/EBP homologous protein (CHOP) in regulating ER stress-induced apoptosis in rat hepatocytes. We found that CHOP downregulates autophagy, aggravating apoptosis. Our results revealed that inhibition of CHOP expression enhanced autophagy and reduced DTT-induced apoptosis in BRL-3A cells, whereas CHOP overexpression worsened apoptosis. Chromatin immunoprecipitation assays revealed that CHOP negatively regulates autophagy-related genes, such as ATG12, ATG5, and LC3. These findings suggest that CHOP modulation plays a crucial role in ER stress-induced hepatocyte apoptosis by regulating autophagy.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 3","pages":"Pages 109-118"},"PeriodicalIF":3.3,"publicationDate":"2025-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143536593","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":"Low serum HSPA12B levels are associated with an increased risk of sarcopenia in a Chinese population of older adults","authors":"Xin-Feng Jiao ,&nbsp;Yue Gao ,&nbsp;Ran Ni ,&nbsp;Wen-Ya Zhao ,&nbsp;Can Zhao ,&nbsp;Xiang Lu ,&nbsp;Hai-Feng Zhang ,&nbsp;Wei Gao ,&nbsp;Lan Luo","doi":"10.1016/j.cstres.2025.02.003","DOIUrl":"10.1016/j.cstres.2025.02.003","url":null,"abstract":"<div><div>Sarcopenia is a geriatric syndrome characterized by progressive loss of muscle mass and function. Heat shock protein (HSP) A12B is essential for angiogenesis and endothelial function. However, the association of HSPA12B levels with sarcopenia remains unclear. A total of 936 community-dwelling elderly people were recruited, and serum HSPA12B was measured by enzyme-linked immunosorbent assay. Appendicular skeletal muscle mass index (ASMI), grip strength, and gait speed were taken to assess sarcopenia. We found that serum HSPA12B levels in patients with sarcopenia (median [interquartile range] = 182.15 [137.58–225.86] ng/mL) were lower than those in elderly people without sarcopenia (228.96 [193.03–292.93] ng/mL, <em>P</em> &lt; 0.001). Receiver operating characteristic curve analysis indicated that the optimal cut-off value of serum HSPA12B level for predicting sarcopenia was 185.50 ng/mL, with a sensitivity of 52.6% and a specificity of 80.8% (area under curve = 0.742, 95% confidence interval [CI] = 0.711–0.772, <em>P</em> &lt; 0.001). Moreover, serum HSPA12B concentration was positively correlated with ASMI (<em>r</em> = 0.354, <em>P</em> &lt; 0.001), grip strength (<em>r</em> = 0.381, <em>P</em> &lt; 0.001), and gait speed (<em>r</em> = 0.169, <em>P</em> &lt; 0.001). Multivariate logistic regression analysis showed that decreased serum HSPA12B levels (&lt;185.50 ng/mL) were a risk factor for increased risk of sarcopenia (adjusted odds ratio = 4.335, 95% CI = 3.136–5.993, <em>P</em> &lt; 0.001). In addition, serum HSPA12B level was also positively correlated with serum levels of angiogenesis markers, vascular endothelial growth factor (<em>r</em> = 0.080, <em>P</em> = 0.014), and angiopoietin-1 (<em>r</em> = 0.108, <em>P</em> = 0.001). In summary, our results indicate that low serum HSPA12B level is associated with an increased risk of sarcopenia in the elderly, suggesting a potential role of HSPA12B in the development of sarcopenia.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 2","pages":"Pages 100-108"},"PeriodicalIF":3.3,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143472192","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":"Increased intracellular stress responses and decreased KLF2 in adult patients with atopic dermatitis","authors":"Shuji Sugiura ,&nbsp;Hiderou Yoshida ,&nbsp;Hisashi Sugiura ,&nbsp;Masami Uehara ,&nbsp;Yasuo Sugiura ,&nbsp;Yoshihiro Maruo ,&nbsp;Yuji Hayashi ,&nbsp;Takefumi Yamamoto ,&nbsp;Takeshi Kato ,&nbsp;Noriki Fujimoto ,&nbsp;Jun Udagawa","doi":"10.1016/j.cstres.2025.02.001","DOIUrl":"10.1016/j.cstres.2025.02.001","url":null,"abstract":"<div><div>Atopic dermatitis (AD) is prone to exacerbations in response to various triggering factors and flare-ups after remission. We searched for molecules associated with relapse/exacerbation of AD among molecules with altered gene expression in the skin of patients with AD. Microarray analyses were performed on lesional and nonlesional skin of adolescent or adult patients with recalcitrant AD and healthy controls. Five chaperones involved in intracellular stress responses, namely heat shock protein family A (Hsp70) member 9 (<em>HSPA9</em>), heat shock protein 90 beta family member 1 (<em>HSP90B1</em>), calnexin (<em>CANX</em>), malectin (<em>MLEC</em>; endoplasmic reticulum-associated degradation), and heat shock protein family D (Hsp60) member 1 (<em>HSPD1</em>), were consistently upregulated in involved and uninvolved skin of patients with AD. Damage-associated molecular patterns were upregulated in involved skin. KLF transcription factor 2 (<em>KLF2</em>) was decreased in involved skin and exhibited a decreasing trend in uninvolved skin of patients with AD. CD4(+)/CD8(+) double-positive cells (1.4% of T cells) were detected in lesions with declined KLF2 levels. WNT inhibitory factor 1 (WIF1) was downregulated in involved skin. Prolactin-induced protein was upregulated in only uninvolved skin of patients with AD. We found increased intracellular stress responses and decreased expression of KLF2 in the skin of patients with AD. Multifactorial genetic diseases, such as asthma, inflammatory bowel disease, type 2 diabetes, and rheumatoid arthritis, are associated with intracellular stress. Intracellular abnormalities may also be responsible for AD. Further research on AD may incorporate enhanced intracellular stress response and the decreased expression of KLF2 into the mechanism underlying AD.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 2","pages":"Pages 84-99"},"PeriodicalIF":3.3,"publicationDate":"2025-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143406088","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":"FKBP51 functions in the regulation of circadian rhythm and Alzheimer's disease","authors":"Jill L. Johnson","doi":"10.1016/j.cstres.2025.02.002","DOIUrl":"10.1016/j.cstres.2025.02.002","url":null,"abstract":"<div><div>The FK506-binding protein 51 (FKBP51) is an important regulator of glucocorticoid receptor activity and an Hsp90 cochaperone. FKBP51 has previously been identified as a drug target due to its roles in stress-related disorders and pain tolerance. Two recent publications in Cell Stress and Chaperones further explore FKBP51 functions. To understand whether FKBP51 plays a role in sleep disturbances linked to stress disorders, one study examined the role of FKBP51 in regulating the circadian rhythm. Broadening the range of Hsp90 cochaperone function, the other article summarized the role of multiple cochaperones in Alzheimer’s disease, discussing how cochaperones affect both Aβ and tau. They emphasize the role of FKBP51 in promoting tau pathogenesis and discuss the small molecule LA1011, which binds Hsp90 and competes with Hsp90-FKBP51 interaction. Further studies with LA1011 may lead to new treatments for Alzheimer’s disease and will help clarify the contributions of FKBP51 to human disorders.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 2","pages":"Pages 81-83"},"PeriodicalIF":3.3,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143398314","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":"Molecular response of canine testis to GnRH agonist: Insights into AR, HIF-1α, and HSPs expression during arrest and recovery of spermatogenesis","authors":"Anastasiia Vasetska ,&nbsp;Eva-Maria Packeiser ,&nbsp;Hanna Körber ,&nbsp;Selim Aslan ,&nbsp;Serhan Ay ,&nbsp;Murat Findik ,&nbsp;Firdevs Binli ,&nbsp;Murat Selçuk ,&nbsp;Christelle Speiser-Fontaine ,&nbsp;Sandra Goericke-Pesch","doi":"10.1016/j.cstres.2024.11.007","DOIUrl":"10.1016/j.cstres.2024.11.007","url":null,"abstract":"<div><div>Slow-release gonadotropin-releasing hormone (GnRH) agonist implants are frequently used for contraception in male dogs. Although the effects are fully reversible, there is still concern about the safety of the implant’s mode of action. Addressing this, we investigated cellular stress and androgen receptor (AR) signaling during downregulation and recovery. Testicular tissues were sampled from dogs castrated at different time points after GnRH implant removal and compared with untreated controls. <em>AR</em>, hypoxia-inducible factor 1 (<em>HIF1A</em>), heat shock proteins heat shock protein 72 (<em>HSP72</em>), heat shock protein 73 (heat shock cognate, HSPA8) (<em>HSP73</em>), heat shock protein A2 (<em>HSPA2</em>), heat shock protein 90 alpha (inducible isoform) (<em>HSP90AA1</em>), and heat shock protein 90 beta (constitutive isoform) (<em>HSP90AB1</em>) were investigated by quantitative real-time polymerase chain reaction and AR, HSP72, HSP73, and HSP90 immunohistochemically. While <em>AR</em>, <em>HIF1A</em>, and <em>HSP70</em> were upregulated at gene expression level, <em>HSPA8</em>, <em>HSPA2</em>, and <em>HSP90AA1</em> expression were downregulated during spermatogenic arrest; <em>HSP90AB1</em> expression did not change. Immunohistochemistry verified AR-expression in Sertoli, peritubular, and Leydig cells, occasionally also in spermatogonia. Stress-inducible HSP72 was occasionally detected, while constitutive HSP73 and HSP90 were abundantly expressed by germ cells. Our results were similar to studies on seasonal breeders such as pine voles, geese, fish, and soft-shelled turtles. Accordingly, GnRH implants did not impose additional cellular stress on testicular cells when compared with natural recrudescence. Since comparative data on HIF1α are scarce, we cannot draw conclusions about hypoxic conditions.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 1","pages":"Pages 9-21"},"PeriodicalIF":3.3,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11719361/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142779494","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":"Secreted extracellular heat shock protein gp96 and inflammatory cytokines are markers of severe malaria outcome","authors":"Fatou Thiam ,&nbsp;Djibaba Djoumoi ,&nbsp;Mame Ndew Mbaye ,&nbsp;Aminata Fall ,&nbsp;Abou Abdallah Malick Diouara ,&nbsp;Mamadou Diop ,&nbsp;Cheikh Momar Nguer ,&nbsp;Babacar Mbengue ,&nbsp;Gora Diop ,&nbsp;Evelyne Kohli ,&nbsp;Alioune Dieye","doi":"10.1016/j.cstres.2024.12.004","DOIUrl":"10.1016/j.cstres.2024.12.004","url":null,"abstract":"<div><div>Malaria caused by <em>Plasmodium spp.</em>, is a major public health issue in sub-Saharan Africa. The fight against malaria has stalled due to increasing resistance to treatments and insecticides. There is an urgent need to focus on new therapeutic targets to combat malaria effectively. This study aimed to measure the secreted heat shock protein gp96 levels in both malaria patients and controls. Indeed, gp96 plays a crucial role in parasite survival within the host and in establishing a successful infection. Therefore, gp96 could be a promising target for antimalarial drugs. In our study, we included 60 malaria patients, 30 with severe malaria (SM) and 30 with uncomplicated malaria (UM). Additionally, 28 controls were included. Using the ELISA method, we measured gp96 levels in the participants' blood samples. We then used the Mann–Whitney or analyse of variance tests to calculate descriptive statistics and determined the correlation between gp96 level and parasitemia using Spearman's rank correlation test. The study found that gp96 levels in the plasma significantly increased in malaria patients (23.86 ng/mL) compared to control (5.88 ng/mL), with a <em>P</em> &lt; 0.0001. Interestingly, there was a significant difference between SM (27.56 ng/mL) and UM (13.9 ng/mL), with a <em>P</em>-value of 0.001. These findings are accompanied by significantly higher parasitemia and elevated proinflammatory cytokines such as IL-17A and IL-1β levels in SM patients compared to UM and controls. Furthermore, there was no significant positive correlation between gp96 levels and parasitemia/proinflammatory cytokines. Our research has revealed, for the first time, that individuals with SM have significantly higher levels of gp96 in the context of high parasitemia and proinflammatory cytokines. Our preliminary results will be taken further to evaluate gp96 as a valuable biomarker for the diagnosis of SM and a potential target for antimalarial drug discovery.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 1","pages":"Pages 48-56"},"PeriodicalIF":3.3,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11761890/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142892403","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":"Cover and caption","authors":"","doi":"10.1016/S1355-8145(25)00005-7","DOIUrl":"10.1016/S1355-8145(25)00005-7","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 1","pages":"Page OFC"},"PeriodicalIF":3.3,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143427651","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 Board Members/Copyright","authors":"","doi":"10.1016/S1355-8145(25)00006-9","DOIUrl":"10.1016/S1355-8145(25)00006-9","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 1","pages":"Page i"},"PeriodicalIF":3.3,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143427652","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":"Large-scale energy decomposition for the analysis of protein stability","authors":"Samman Mansoor ,&nbsp;Elena Frasnetti ,&nbsp;Ivan Cucchi ,&nbsp;Andrea Magni ,&nbsp;Giorgio Bonollo ,&nbsp;Stefano A. Serapian ,&nbsp;Luca F. Pavarino ,&nbsp;Giorgio Colombo","doi":"10.1016/j.cstres.2025.01.001","DOIUrl":"10.1016/j.cstres.2025.01.001","url":null,"abstract":"<div><div>To carry out their functions in cells, proteins are required to fold into well-defined three-dimensional conformations. The stability of the folded state dictates several aspects of protein life, such as their evolution, interactions, and selection of structures that are ultimately linked to activity. Sequence mutations may change the stability profile and consequently impact structure and function. Here, we use a simple, molecular dynamics-based energy decomposition approach to map the response to mutations of each amino acid in the sequences of a set of five test proteins with different lengths, folds, and topologies. To this end, we make use of the decomposition of the residue-pair nonbonded energy matrix. We show that parameters obtained from this analysis, namely the main eigenvalue reporting on the most stabilizing energy contributions and the spectral gap of the matrix (ENergy Gap), reproduce experimentally determined stability trends. At the same time, our approach identifies the residue-pair couplings that play key roles in defining the 3D properties of a certain fold. We discuss the relevance of these results for the design of protein mutants for experimental applications and the possibility for our energy decomposition approach to complement other computational and experimental analyses of conformational stability.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 1","pages":"Pages 57-68"},"PeriodicalIF":3.3,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143063936","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}