Cell Stress & Chaperones最新文献

FKBP51 Overexpression in the Corticolimbic System Stabilizes Circadian Rhythms. 皮质边缘系统中 FKBP51 的过度表达可稳定昼夜节律

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-12 DOI: 10.1016/j.cstres.2024.12.003

Niat T Gebru, David Beaulieu-Abdelahad, Danielle Gulick, Laura J Blair

{"title":"FKBP51 Overexpression in the Corticolimbic System Stabilizes Circadian Rhythms.","authors":"Niat T Gebru, David Beaulieu-Abdelahad, Danielle Gulick, Laura J Blair","doi":"10.1016/j.cstres.2024.12.003","DOIUrl":"https://doi.org/10.1016/j.cstres.2024.12.003","url":null,"abstract":"<p><p>Circadian rhythm disruptions have been associated with a wide range of health issues and complications, including an increased risk of circadian rhythm sleep disorders (CRSDs). CRSDs are common among individuals who have been through a traumatic event, particularly in those who have post-traumatic stress disorder (PTSD). Allelic variations in the gene encoding for FK506-binding protein 51 (FKBP51) can increase the susceptibility for PTSD and other stress-related disorders following trauma. At least one of these variants increases the levels of FKBP51 following stress through a glucocorticoid receptor-mediated process. Here, we used a mouse model that overexpresses human FKBP51 throughout the forebrain, rTgFKBP5, to investigate if elevated FKBP51 contributes to circadian rhythm disruption. Surprisingly, our findings indicate a greater rhythm amplitude and decreased rhythm fragmentation in rTgFKBP5 mice, particularly females, compared to controls. Female rTgFKBP5 mice also showed higher corticosterone levels basally and following stress exposure. Overall, this study associates FKBP51 overexpression with beneficial circadian rhythm outcomes.</p>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2024-12-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142823926","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular response of canine testis to GnRH agonist: Insights into AR, HIF-1α, and HSPs expression during arrest and recovery of spermatogenesis.

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-02 DOI: 10.1016/j.cstres.2024.11.007

Anastasiia Vasetska, Eva-Maria Packeiser, Hanna Körber, Selim Aslan, Serhan Ay, Murat Findik, Firdevs Binli, Murat Selçuk, Christelle Speiser-Fontaine, Sandra Goericke-Pesch

{"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, Eva-Maria Packeiser, Hanna Körber, Selim Aslan, Serhan Ay, Murat Findik, Firdevs Binli, Murat Selçuk, Christelle Speiser-Fontaine, Sandra Goericke-Pesch","doi":"10.1016/j.cstres.2024.11.007","DOIUrl":"10.1016/j.cstres.2024.11.007","url":null,"abstract":"<p><p>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. AR, hypoxia-inducible factor 1 (HIF1A), heat shock proteins heat shock protein 72 (HSP72), heat shock protein 73 (heat shock cognate, HSPA8) (HSP73), heat shock protein A2 (HSPA2), heat shock protein 90 alpha (inducible isoform) (HSP90AA1), and heat shock protein 90 beta (constitutive isoform) (HSP90AB1) were investigated by quantitative real-time polymerase chain reaction and AR, HSP72, HSP73, and HSP90 immunohistochemically. While AR, HIF1A, and HSP70 were upregulated at gene expression level, HSPA8, HSPA2, and HSP90AA1 expression were downregulated during spermatogenic arrest; HSP90AB1 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.</p>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":" ","pages":"9-21"},"PeriodicalIF":3.3,"publicationDate":"2024-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","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":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Ceapin-A7 suppresses the protective effects of Octreotide in human and bovine lung endothelial cells.

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-02 DOI: 10.1016/j.cstres.2024.12.001

Saikat Fakir, Madan Sigdel, Md Matiur Rahman Sarker, Joy T Folahan, Nektarios Barabutis

引用次数: 0

Endoplasmic reticulum stress-mediated apoptosis and autophagy in osteoarthritis: From molecular mechanisms to therapeutic applications. 骨关节炎中内质网应激介导的细胞凋亡和自噬：从分子机制到治疗应用。

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-01 Epub Date: 2024-11-19 DOI: 10.1016/j.cstres.2024.11.005

Yifan Lu, Jing Zhou, Hong Wang, Hua Gao, Eryu Ning, Zhiqiang Shao, Yuefeng Hao, Xing Yang

{"title":"Endoplasmic reticulum stress-mediated apoptosis and autophagy in osteoarthritis: From molecular mechanisms to therapeutic applications.","authors":"Yifan Lu, Jing Zhou, Hong Wang, Hua Gao, Eryu Ning, Zhiqiang Shao, Yuefeng Hao, Xing Yang","doi":"10.1016/j.cstres.2024.11.005","DOIUrl":"10.1016/j.cstres.2024.11.005","url":null,"abstract":"<p><p>Osteoarthritis (OA) is characterized primarily by the degeneration of articular cartilage, with a high prevalence and disability rate. The functional phenotype of chondrocytes, as the sole cell type within cartilage, is vital for OA progression. Due to the avascular nature of cartilage and its limited regenerative capacity, repair following injury poses significant challenges. Various cellular stressors, including hypoxia, nutrient deprivation, oxidative stress, and collagen mutations, can lead to the accumulation of misfolded proteins in the endoplasmic reticulum (ER), resulting in ER stress (ERS). In response to restore ER homeostasis as well as cellular vitality and function, a series of adaptive mechanisms are triggered, including the unfolded protein response, ER-associated degradation, and ER-phagy. Prolonged or severe ERS may exceed the adaptive capacity of cells, leading to dysregulation in apoptosis and autophagy-key pathogenic factors contributing to chondrocyte damage and OA progression. This review examines the relationship between ERS in OA chondrocytes and both apoptosis and autophagy in order to identify potential therapeutic targets and strategies for prevention and treatment of OA.</p>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":" ","pages":"805-830"},"PeriodicalIF":3.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142686066","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The role of the FKBP51-Hsp90 complex in Alzheimer's disease: An emerging new drug target.

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-01 Epub Date: 2024-11-29 DOI: 10.1016/j.cstres.2024.11.006

Xavier Jeanne, Zsolt Török, László Vigh, Chrisostomos Prodromou

{"title":"The role of the FKBP51-Hsp90 complex in Alzheimer's disease: An emerging new drug target.","authors":"Xavier Jeanne, Zsolt Török, László Vigh, Chrisostomos Prodromou","doi":"10.1016/j.cstres.2024.11.006","DOIUrl":"10.1016/j.cstres.2024.11.006","url":null,"abstract":"<p><p>With increasing age comes the inevitable decline in proteostasis, where chaperone and co-chaperone activity becomes imbalanced. These changes lead to global disturbances and pathogenic rewiring of the chaperone system into epichaperones consisting of protein networks that are ultimately dysfunctional. Such imbalances in proteostasis may favor mechanisms that can lead to neurological diseases, such as Alzheimer's disease (AD). Consequently, there has been an increase in research activity toward finding small molecules that can re-balance the chaperone and co-chaperone machinery to counter the effects of disease resulting from old age. The Hsp90 co-chaperone FKBP51 has recently been identified as a protein whose induction not only increases with age but is elevated further in AD cells. Significantly, FKBP51 plays a role in the Hsp90-dependent isomerization of tau, which in turn influences its phosphorylation and susceptibility to aggregation. We hypothesize that FKBP51 is a major player that is able to elicit tauopathy in response to amyloid-beta senile plaques that damage the brain. We propose that elevated FKBP51 levels result in an abnormal FKBP51-Hsp90 activity that alters the normal processing of tau, which manifests as hyperphosphorylation and oligomerization of tau. Thus, the Hsp90-FKBP51 complex is emerging as a drug target against AD. In support of this idea, the structure of the FKBP51-Hsp90 complex was recently described, and significantly, the small-molecule dihydropyridine LA1011 was shown to be able to disrupt the Hsp90-FKBP51 complex. LA1011 was previously shown to effectively prevent neurodegeneration in the APPxPS1 AD transgenic mouse model. This review looks at the role of Hsp90 and its co-chaperones in AD with a focus on FKBP51.</p>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":" ","pages":"792-804"},"PeriodicalIF":3.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142766587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Pyrotinib induces cell death in HER2-positive breast cancer via triggering HSP90-dependent HER2 degradation and ROS/HSF-1-dependent oxidative DNA damage. 派罗替尼通过引发依赖HSP90的HER2降解和依赖ROS/HSF-1的氧化性DNA损伤，诱导HER2阳性乳腺癌细胞死亡。

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-01 Epub Date: 2024-11-18 DOI: 10.1016/j.cstres.2024.11.004

Xiaomin Gao, Xu Guo, Wenbo Yuan, Sunmin Jiang, Zihong Lu, Qing Luo, Yuan Zha, Ling Wang, Shu Li, Ke Wang, Xue Zhu, Ying Yao

{"title":"Pyrotinib induces cell death in HER2-positive breast cancer via triggering HSP90-dependent HER2 degradation and ROS/HSF-1-dependent oxidative DNA damage.","authors":"Xiaomin Gao, Xu Guo, Wenbo Yuan, Sunmin Jiang, Zihong Lu, Qing Luo, Yuan Zha, Ling Wang, Shu Li, Ke Wang, Xue Zhu, Ying Yao","doi":"10.1016/j.cstres.2024.11.004","DOIUrl":"10.1016/j.cstres.2024.11.004","url":null,"abstract":"<p><p>HER2-positive breast cancer (HER2+ BC) is distinguished by its poor prognosis, propensity for early onset, and high risk of recurrence and metastasis. Consequently, anti-HER2-targeted therapy has emerged as a principal strategy in the treatment of this form of breast cancer. Pyrotinib, a novel irreversible pan-HER2 tyrosine kinase inhibitor, has brought fresh hope to patients with advanced HER2+ breast cancer. In this study, we conducted a comprehensive exploration of pyrotinib's antitumor mechanism. The in vitro results showed that pyrotinib significantly inhibited SKBR3 cells viability and induced apoptosis by promoting HER2 endocytosis and ubiquitylation, leading to HER2 degradation through the displacement of HSP90 from HER2. Beyond targeting the HER2 signaling pathway, pyrotinib also induced DNA damage, which was mediated by the activation of the reactive oxygen species/heat shock factor 1 signaling pathway and the downregulation of proliferating cell nuclear antigen expression. Furthermore, the in vivo results demonstrated a pronounced anticancer effect of pyrotinib in the SKBR3 xenograft mouse model, concomitant with a reduction in HER2 expression. In summary, our findings provide novel insights into the mechanism of pyrotinib in the treatment of HER2+ BC.</p>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":" ","pages":"777-791"},"PeriodicalIF":3.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142680098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Protective role of short-chain fatty acids on intestinal oxidative stress induced by TNF-α 短链脂肪酸对 TNF-α 诱导的肠道氧化应激的保护作用

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-12-01 DOI: 10.1016/j.cstres.2024.11.002

Miguel Ferrer , Berta Buey , Laura Grasa , Jose Emilio Mesonero , Eva Latorre

{"title":"Protective role of short-chain fatty acids on intestinal oxidative stress induced by TNF-α","authors":"Miguel Ferrer , Berta Buey , Laura Grasa , Jose Emilio Mesonero , Eva Latorre","doi":"10.1016/j.cstres.2024.11.002","DOIUrl":"10.1016/j.cstres.2024.11.002","url":null,"abstract":"<div><div>Inflammatory bowel diseases (IBDs) are driven by an exaggerated inflammatory response, which leads to a marked increase in oxidative stress. This, in turn, exacerbates the inflammatory process and causes significant cellular and tissue damage. Intestinal dysbiosis, a common observation in IBD patients, alters the production of bacterial metabolites, including short-chain fatty acids (SCFAs), which are key by-products of dietary fiber fermentation. While the role of SCFAs in intestinal physiology is still being elucidated, this study aimed to investigate their effects on intestinal oxidative stress, particularly under inflammatory conditions induced by the proinflammatory mediator tumor necrosis factor alpha (TNF-α). The Caco-2/TC7 cell line was employed as an in vitro model of the intestinal epithelium, and the cells were treated with a range of SCFAs, including acetate, propionate, and butyrate. The levels of protein and lipid oxidation were quantified, as well as the activity of antioxidant enzymes. Our findings demonstrate that microbiota-derived SCFAs can effectively mitigate TNF-α-induced oxidative stress by modulating antioxidant enzyme activity. The proinflammatory mediator TNF-α induces lipid peroxidation by inhibiting catalase and glutathione peroxidase activities. SCFAs are able to upregulate antioxidant enzyme activity to restore lipid oxidative levels. These results underscore the critical role of the gut microbiota in maintaining intestinal homeostasis and highlight the therapeutic potential of SCFAs in managing oxidative stress-related pathologies.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 6","pages":"Pages 769-776"},"PeriodicalIF":3.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142638467","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}

引用次数: 0

An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography 低温电子断层扫描技术证实了体外推断的伴侣素加速蛋白质重折叠的过时机制。

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-11-15 DOI: 10.1016/j.cstres.2024.11.003

Paolo De Los Rios , Mathieu E. Rebeaud , Pierre Goloubinoff

引用次数: 0

Regulation of chondrocyte apoptosis in osteoarthritis by endoplasmic reticulum stress 内质网应激对骨关节炎中软骨细胞凋亡的调节作用

IF 3.3 3区生物学

Cell Stress & Chaperones Pub Date : 2024-11-06 DOI: 10.1016/j.cstres.2024.11.001

Renzhong Li , Kui Sun

引用次数: 0

Corrigendum to “The mechanism and therapeutic strategies in doxorubicin induced cardiotoxicity: Role of programmed cell death” [Cell Stress Chaperones. 2024;29:666-680] 多柔比星诱发心脏毒性的机制和治疗策略：细胞应激合子的作用》[Cell Stress Chaperones.］