{"title":"Allyl isothiocyanate suppresses the growth and pathogenicity of Candida albicans","authors":"Hideki Nishiura , Muneaki Tamura , Rieko Matsuike , Marni C. Cueno , Tomoka Ito , Yasuhiro Namura , Toshimitsu Iinuma , Kenichi Imai","doi":"10.1016/j.cstres.2025.100125","DOIUrl":"10.1016/j.cstres.2025.100125","url":null,"abstract":"<div><div><em>Candida albicans</em> is a fungus that is predominantly detected in the oral cavity and causes opportunistic infections. Among the elderly, a decline in the host's resistance to pathogens due to immunosenescence makes them more susceptible to oral candidiasis, which eventually may progress to systemic candidiasis. Allyl isothiocyanate (AITC) is a component found in Brassicaceae plants (such as wasabi), which possesses strong antibacterial properties and is used as a food preservative. In this study, the effects of AITC on <em>C. albicans</em> were investigated though: (1) inhibition of growth and biofilm formation, (2) inhibition of adhesion to denture base resin, (3) inhibition of dimorphic transformation that exacerbates pathogenicity, and (4) inhibition of the production of secretory aspartic protease and lipase. Taken together, this suggests that AITC suppresses the growth and pathogenicity of this fungus. Further investigation of the mechanism revealed a decrease in hyphae-specific gene expression in the intracellular signaling MAP kinase cascade and cAMP pathway, as well as the induction of oxidative stress and a tendency toward apoptosis within <em>C. albicans</em> cells. Based on these findings, we propose that AITC may be beneficial for the prevention and suppression of oral candidiasis and has the potential for clinical application aimed at improving oral care and quality of life.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 6","pages":"Article 100125"},"PeriodicalIF":3.2,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145273970","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}
Cell Stress & ChaperonesPub Date : 2025-12-01Epub Date: 2025-10-17DOI: 10.1016/j.cstres.2025.100126
Carol Nguyen , Rafael Ishihara Figueiroa , Cristiano Mendes da Silva , Elaine Hatanaka , Gary Sweeney , Rafael Herling Lambertucci
{"title":"Melatonin attenuates cardiac oxidative stress in diabetic rats following acute exhaustive exercise","authors":"Carol Nguyen , Rafael Ishihara Figueiroa , Cristiano Mendes da Silva , Elaine Hatanaka , Gary Sweeney , Rafael Herling Lambertucci","doi":"10.1016/j.cstres.2025.100126","DOIUrl":"10.1016/j.cstres.2025.100126","url":null,"abstract":"<div><h3>Introduction</h3><div>Diabetes mellitus affects millions of people worldwide and there is evidence linking the increase of oxidative stress to the development of diabetic cardiomyopathy. Melatonin has been found to possess powerful antioxidant properties <em>via</em> modulating both enzymatic and non-enzymatic antioxidant systems.</div></div><div><h3>Objective</h3><div>To evaluate the antioxidant potential of melatonin on the heart of diabetic animals at basal conditions and following 2 h of strenuous exercise.</div></div><div><h3>Methods</h3><div>Diabetic animals were divided into two groups: non-supplemented and supplemented (melatonin). We evaluated oxidative stress biomarkers, total glutathione amount, oxidative stress index and antioxidant enzymes mRNA expression, immediately after an exhaustive exercise (IA group), and 2 h after exhausted exercise (2 h group). We also included a non-exercised group (0 h).</div></div><div><h3>Results</h3><div>Comparing to non-exercised animals, exercise immediately induced an increase of nitrite and total antioxidant status in non-supplemented and supplemented animals, respectively. In melatonin-supplemented animals, the oxidative stress index decreased immediately after exercise (IA group) compared to non-exercised animals (0 h), an effect not seen in the non-supplemented group. Compared to non-supplemented, melatonin supplementation was shown to attenuate TBARS at all time points and increase total glutathione content at times 0 h and IA. mRNA expression of some antioxidant enzymes (CAT and GPX) was modulated by melatonin, especially when associated with exercise [catalase (CAT) and Cu, Zn superoxide dismutase (SOD)].</div></div><div><h3>Conclusion</h3><div>Our findings demonstrate that melatonin confers antioxidant protection to the diabetic heart, primarily by increasing glutathione levels and attenuating lipid peroxidation. This establishes a protective state that enhances cardiac resilience, and the combination of melatonin and exercise may offer synergistic benefits against acute, stress-induced oxidative damage in diabetic animals.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 6","pages":"Article 100126"},"PeriodicalIF":3.2,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145328419","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}
Cell Stress & ChaperonesPub Date : 2025-12-01Epub Date: 2025-09-09DOI: 10.1016/j.cstres.2025.100113
Guoqin Wang , Chaojiang Fu , Changling Tu , Zhuangqing Yang , Wei Shi , Lijuan Zhang , Shufen Tan , Youguang Huang
{"title":"TBX5-AS1 induces ER stress and suppresses lung cancer growth and tumor stemness via the miR-494-3p/ATF6 axis","authors":"Guoqin Wang , Chaojiang Fu , Changling Tu , Zhuangqing Yang , Wei Shi , Lijuan Zhang , Shufen Tan , Youguang Huang","doi":"10.1016/j.cstres.2025.100113","DOIUrl":"10.1016/j.cstres.2025.100113","url":null,"abstract":"<div><div>Tumor stemness maintenance and endoplasmic reticulum (ER) stress response have been strongly correlated with the progression of lung cancer (LC). Nevertheless, the role of long non-coding RNAs (lncRNAs) in these processes remains incompletely understood. We screened LC-associated lncRNAs from the GEO database and validated the expression of TBX5-AS1 in clinical samples. Functional experiments were conducted to assess the biological effects of TBX5-AS1, and western blot was used to detect ER stress marker proteins. The interaction mechanism of the TBX5-AS1/miR-494–3p/ATF6 axis was elucidated through dual-luciferase reporter assays, RNA immunoprecipitation (RIP), and pull-down experiments. Rescue experiments and a nude mouse xenograft model were employed to validate the functional outcomes. TBX5-AS1 was significantly downregulated in LC tissues and cell lines, and its low expression was associated with advanced tumor stages and poor patient prognosis. Overexpression of TBX5-AS1 markedly suppressed LC cell proliferation, migration, invasion, and self-renewal while promoting the activation of the ER stress pathway. Mechanistically, TBX5-AS1 competitively binds to miR-494–3p, thereby relieving its transcriptional repression of Activating transcription factor 6 (ATF6). Rescue experiments demonstrated that miR-494–3p overexpression reversed the regulatory effects of TBX5-AS1 on tumor malignant phenotype and ER stress. In vivo experiments further confirmed that TBX5-AS1 overexpression significantly inhibited tumor growth, accompanied by upregulation of ATF6 and ER stress-related proteins. TBX5-AS1 functioned as a tumor-suppressive lncRNA by activating ER stress signaling through the miR-494–3p/ATF6 axis, thereby inhibiting LC growth and tumor stemness.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 6","pages":"Article 100113"},"PeriodicalIF":3.2,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145039149","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}
Cell Stress & ChaperonesPub Date : 2025-12-01Epub Date: 2025-11-03DOI: 10.1016/j.cstres.2025.100128
Wael M. Elshemey , Hamdy I.A. Mostafa , Abdo A. Elfiky
{"title":"Computational characterization of HIV envelope interactions with cellular GRP78 as a potential entry mechanism","authors":"Wael M. Elshemey , Hamdy I.A. Mostafa , Abdo A. Elfiky","doi":"10.1016/j.cstres.2025.100128","DOIUrl":"10.1016/j.cstres.2025.100128","url":null,"abstract":"<div><div>Human Immuno-deficiency virus (HIV) is still spreading all over the world. There are many routes through which the virus recognizes host cells by its envelope protein. One of these routes is through binding to glucose-regulated protein 78 (GRP78), which is overexpressed in stressed cells. In this study, we investigate the association between GRP78 and HIV envelope protein at four different binding sites (R1: C130-C162), (R2: C223-C252), (R3: C301-C335), and (R4: C388-C418) using a comprehensive <em>in silico</em> approach. Protein-protein docking and molecular dynamics simulations (MDS) are conducted to evaluate the binding. Results indicate that the R4 region (C388-C418) is the potential binding site of the envelope protein to GRP78 on the cell surface with an average binding energy of −12.20 ± 2.0 kcal/mol. The predicted findings open the gate towards further studies that could lead to the development of effective inhibitors that can alleviate viral recognition of the host cell and eradicate the viral infection.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 6","pages":"Article 100128"},"PeriodicalIF":3.2,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145450757","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}
{"title":"Monocyte USP7-p65 axis mediates immune responses to the immunogenicity of nucleus pulposus","authors":"Peng Feng , Xuelei Chu , Ying Che , Jinghua Gao , Chunyu Gao , Ting Zhang","doi":"10.1016/j.cstres.2025.100114","DOIUrl":"10.1016/j.cstres.2025.100114","url":null,"abstract":"<div><div>The nucleus pulposus (NP) of the intervertebral disc is an immune-privileged tissue. During intervertebral disc degeneration (IDD), this immune privilege is compromised, resulting in the exposure of NP components to the peripheral immune system, which in turn activates monocytes and elicits an immune response. In this study, we demonstrate that monocytes respond to NP immunogenicity by activating damage-associated molecular patterns (DAMPs), thereby initiating a sustained NF-κB–mediated inflammatory response in NP tissue and ultimately driving a vicious cycle of inflammation and oxidative stress within NP cells. Mechanistically, NP-derived immunogenic stimulation induces monocyte activation, accompanied by increased expression and nuclear translocation of the deubiquitinase USP7. USP7 promotes the accumulation and nuclear translocation of the NF-κB subunit p65 via a deubiquitination-dependent mechanism, leading to enhanced transcription of TNF-α, HMGB1, and IL-1β. These DAMP-associated cytokines further stimulate NP cells, resulting in upregulation of HMGB1, TNF-α, COX-2, IL-1β, and reactive oxygen species (ROS), along with a concomitant decrease in the antioxidant enzyme SOD2—collectively amplifying inflammation and oxidative stress within the NP microenvironment. Dual-luciferase reporter assays and chromatin immunoprecipitation (ChIP)-qPCR demonstrated that knockdown of USP7 in monocytes significantly reduced p65 binding to the promoter regions of TNF-α, HMGB1, and IL-1β, thereby attenuating the downstream inflammatory and oxidative stress responses in NP cells. Together, these findings uncover a novel immune-inflammatory mechanism underlying IDD and highlight the USP7-mediated pathway in monocytes as a potential therapeutic target for modulating disc degeneration.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 6","pages":"Article 100114"},"PeriodicalIF":3.2,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145063599","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}
Cell Stress & ChaperonesPub Date : 2025-09-01Epub Date: 2025-07-29DOI: 10.1016/j.cstres.2025.100094
Ting Liu , Lu Li , Meixia Meng , Ming Gao , Jinhua Zhang , Yuan Zhang , Yukun Gan , Yangjie Dang , Limin Liu
{"title":"Corrigendum to “The protective role of the IRE1α/XBP1 signaling cascade in autophagy during ischemic stress and acute kidney injury” [Cell Stress Chaperones. 2025;30(3):160-171]","authors":"Ting Liu , Lu Li , Meixia Meng , Ming Gao , Jinhua Zhang , Yuan Zhang , Yukun Gan , Yangjie Dang , Limin Liu","doi":"10.1016/j.cstres.2025.100094","DOIUrl":"10.1016/j.cstres.2025.100094","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 5","pages":"Article 100094"},"PeriodicalIF":3.2,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144722548","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}
Cell Stress & ChaperonesPub Date : 2025-09-01Epub Date: 2025-07-09DOI: 10.1016/j.cstres.2025.100090
Lisa Goutami , Soumya Ranjan Jena , Ajaya Kumar Moharana , Anwesha Pradhan , Sujata Kar , Luna Samanta
{"title":"HSPA2 emerges as a key biomarker: Insights from global lysine acetylproteomic profiling in idiopathic male infertility","authors":"Lisa Goutami , Soumya Ranjan Jena , Ajaya Kumar Moharana , Anwesha Pradhan , Sujata Kar , Luna Samanta","doi":"10.1016/j.cstres.2025.100090","DOIUrl":"10.1016/j.cstres.2025.100090","url":null,"abstract":"<div><div>Spermatozoa are highly specialized cells, and any alterations in their protein profiles may affect their function and fertilizing ability. In spermatozoa, which are transcriptionally and translationally inactive, molecular chaperones, particularly heat shock proteins, play crucial roles in maintaining redox balance and preserving protein integrity. Post-translational modifications, particularly lysine acetylation, influence chaperone function and are lately being recognized in the pathophysiology of male infertility. To assess the impact of lysine acetylation on sperm chaperone proteins in idiopathic infertile patients (IIP) compared to fertile donors (FD), we performed immunoprecipitation coupled with liquid chromatography and tandam mass spectroscpy analysis of lysine acetylated sperm proteins from both groups. Proteomic analysis revealed 2988 acetylated proteins, comprising 26 chaperone proteins that were differentially expressed, with four upregulated and nine downregulated in the IIP group. Functional analyses demonstrated enrichment of these proteins in protein folding, spermatogenesis, and response to oxidative stress. CytoHubba analysis reported key HSP70 family members, HSPA2, HSPA4, and HSPA1A as central hub proteins in protein–protein interaction networks. STRING and Ingenuity Pathway Analysis (IPA) network analyses further highlighted the central regulatory roles of these chaperones, with HSPA2 emerging as a key hub protein based on friendship analysis. Western blot validation revealed hypoacetylation and downregulation of HSPA2 in spermatozoa from the IIP group, accompanied by elevated levels of 4-Hydroxynonenal (4-HNE), indicating a link between redox imbalance and altered lysine acetylation in chaperone proteins. Additionally, intense aniline blue staining of sperm nuclei in the IIP group suggested aberrant spermiogenesis. Considering HSPA2′s well-documented involvement in sperm maturation and oocyte recognition, its diminished acetylation and expression may not only act as a potential biomarker but also contribute mechanistically to the development of idiopathic male infertility. This study underscores the significance of lysine acetylation in HSPA2 in regulating chaperone function and highlights its diagnostic and therapeutic potential in unexplained male infertility.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"30 5","pages":"Article 100090"},"PeriodicalIF":3.2,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144616472","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}