Oncology reports最新文献

{"title":"SGPP1 as a tumor suppressor in esophageal squamous cell carcinoma: Potential molecular mechanisms involving UGT1A9/UGT2B28 and clinical prognostic significance.","authors":"Linlin Su, Liubing Hou, Xuetao Han, Ge Zhang, Jiayuan Li, Yu Wang, Yuxin Han, Xiaoying Xue, Huandi Zhou","doi":"10.3892/or.2026.9199","DOIUrl":"10.3892/or.2026.9199","url":null,"abstract":"<p><p>The present study aimed to characterize the expression pattern and biological function of sphingosine‑1‑phosphate phosphatase 1 (SGPP1) in esophageal squamous cell carcinoma (ESCC), investigate its potential molecular regulatory mechanisms, and evaluate its clinical value as a prognostic biomarker and therapeutic target. SGPP1 expression in ESCC cell lines was assessed by reverse transcription‑quantitative PCR and western blotting. Models of SGPP1 overexpression in KYSE150 cells and SGPP1 knockdown in ECA109 cells were established. 5‑Ethynyl‑2'‑deoxyuridine, Cell Counting Kit‑8, colony formation, terminal deoxynucleotidyl transferase dUTP nick‑end labeling, wound healing and Transwell assays were performed to systematically analyze the effects of SGPP1 on ESCC cell proliferation, apoptosis, migration and invasion. The Cancer Genome Atlas‑ESCC data were integrated with Gene Ontology and Kyoto Encyclopedia of Genes and Genomes enrichment analyses, gene set enrichment analysis and UpSet plotting to identify key downstream pathways and candidate target genes. SGPP1 protein expression was evaluated by immunohistochemistry in tumor tissues from 68 patients with ESCC, and Cox regression analysis was used to assess its association with patient prognosis. The results demonstrated that SGPP1 expression varied markedly among ESCC cell lines, with low expression in KYSE150 cells and high expression in ECA109 cells. SGPP1 overexpression significantly inhibited ESCC cell proliferation, migration and invasion, and increased apoptosis‑associated DNA fragmentation, whereas SGPP1 knockdown produced the opposite effects. Mechanistically, the data suggested that SGPP1 modulates extracellular matrix remodeling and xenobiotic metabolism, potentially through negative regulation of UGT1A9 and UGT2B28 expression. Clinically, low SGPP1 expression was an independent risk factor for poor prognosis in patients with ESCC (HR=6.016, 95% CI: 3.143‑11.513, P<0.001), and the overall survival was significantly longer in the high‑expression group than in the low‑expression group (P<0.001). In conclusion, SGPP1 functions as a tumor suppressor gene in ESCC and may inhibit tumor progression by regulating UGT1A9/UGT2B28‑mediated metabolic pathways. SGPP1 may therefore serve as a prognostic biomarker and a potential therapeutic target in ESCC.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13635725/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149040187","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of EZH2 regulation of the JAK2/STAT3 signaling pathway on proliferation and apoptosis in non‑small cell lung cancer cells.","authors":"Shuang Wu, Wei Zhang","doi":"10.3892/or.2026.9190","DOIUrl":"10.3892/or.2026.9190","url":null,"abstract":"<p><p>Enhancer of zeste homolog 2 (EZH2) is frequently overexpressed in non‑small cell lung cancer (NSCLC) and is associated with aggressive tumor behavior and poor patient prognosis. However, the molecular mechanisms through which EZH2 drives NSCLC progression, particularly its interplay with major oncogenic signaling cascades, remain incompletely defined. EZH2 expression was analyzed using publicly available databases. Functional perturbations were achieved via short hairpin RNA (shRNA)‑mediated knockdown in NCI‑H1299 and A549 NSCLC cell lines. Cell proliferation, migration, invasion, apoptosis, and colony formation were assessed using Cell Counting Kit‑8, Transwell, flow cytometry and colony formation assays, respectively. Involvement of the JAK2/STAT3 pathway was examined by western blotting and rescue experiments using a JAK2 agonist. <i>In vivo</i> validation was conducted using a xenograft mouse model. EZH2 was markedly upregulated in NSCLC tissues. Its silencing markedly suppressed cell proliferation, impaired migratory and invasive capacities, induced apoptosis, and curtailed tumor growth <i>in vivo</i>. Mechanistically, EZH2 silencing attenuated the phosphorylation of both JAK2 and STAT3. Crucially, the anti‑tumor effects of EZH2 knockdown were effectively reversed by JAK2 agonism, positioning EZH2 upstream of the JAK2/STAT3 axis. The present study demonstrated that EZH2 promotes NSCLC progression through activation of the JAK2/STAT3 signaling pathway, identifying the EZH2‑JAK2/STAT3 axis as a potential therapeutic vulnerability in this malignancy.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13586802/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148945423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"[Expression of Concern] <i>In vitro</i> and <i>in vivo</i> activities of an antitumor peptide HM‑3: A special dose‑efficacy relationship on an HCT‑116 xenograft model in nude mice.","authors":"Sitelbanat Yassin, Jialiang Hu, Hanmei Xu, Ce Li, Sarra Setrerrahmane","doi":"10.3892/or.2026.9191","DOIUrl":"10.3892/or.2026.9191","url":null,"abstract":"<p><p>Following the publication of the above article and a corrigendum (doi: 10.3892/or.2020.7503) that was published to take account of duplications of data noted in Fig. 3 (panels 'C' and 'D') and Fig. 7 (also panels 'C' and 'D'), it has come to light that the originally published version of Fig. 7 also contained a small overlapping section of data comparing Fig. 7A with 7D. Upon receiving notification of this further issue associated with the presentation of data in Fig. 7, owing to the non‑availability of the first author who performed these experiments and the inability to identify the original data for this figure, the authors proposed removing the data from Fig. 7A‑D, and simply presenting Fig. 7E in a revised version of this figure in a subsequent corrigendum; however, the Editor of <i>Oncology Reports</i> requested that the authors repeat the experiments shown in Fig. 7. and submit a new and complete version of this figure for the corrigendum. The authors were agreeable to this course of action, although to date, the proposed revised version of this figure has not been received by the Editorial Office; therefore, we are now issuing an Expression of Concern statement to notify readers of the newly identified problems associated with the presentation of certain of the data in this paper. [Oncology Reports 36: 2951‑2959, 2016; DOI: 10.3892/or.2016.5077].</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13586701/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148945377","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pemetrexed increases BRCA1 protein stability and sensitizes TNBC cells to radiotherapy.","authors":"Hee Jin, Kyung-Hwa Jeon, Chaerin Kang, Joohyun Lee, Yeonjin Lee, Youngjoo Kwon, Yun-Sil Lee","doi":"10.3892/or.2026.9194","DOIUrl":"10.3892/or.2026.9194","url":null,"abstract":"<p><p>BRCA1 is a multifunctional tumor suppressor that orchestrates homologous recombination repair, chromatin remodeling, cell cycle control and apoptosis. Although pathogenic BRCA1 mutations are relatively uncommon, decreased BRCA1 protein expression, which is typically driven by accelerated proteasomal degradation, is implicated in aggressive breast cancer (BC), particularly triple‑negative (TN)BC. These mutations may modulate therapeutic response to DNA‑damaging agents. Given the absence of clinically available strategies to restore BRCA1 stability, the present study evaluated whether pemetrexed (Peme), a multitargeted antifolate identified through an <i>in silico</i> US Food and Drug Administration‑approved drug screen, modulates BRCA1 protein homeostasis in TNBC models. BRCA1 protein abundance, ubiquitination and turnover were assessed using immunoblotting, ubiquitin pull‑down and cycloheximide chase analyses and BRCA1 domain mutants. Functional consequences of Peme treatment were measured by apoptosis assay and BRCA1‑dependent signaling readouts. The radiosensitizing effect of Peme was evaluated <i>in vitro</i> and validated in TNBC xenografts. Peme increased BRCA1 protein levels without altering BRCA1 mRNA, indicating post‑translational regulation. Mechanistically, <i>in silico</i> docking and BRCA1 deletion mutant analyses suggested that the BRCA1 C‑terminal domain may contribute to the effect of Peme on BRCA1 stability, suppressing ubiquitin‑mediated proteasomal degradation and resulting in protein stabilization. Stabilized BRCA1 enhanced apoptotic responses, whereas BRCA1 knockdown attenuated these effects. Combined Peme‑radiation treatment significantly potentiated cytotoxicity <i>in vitro</i> and inhibited tumor growth <i>in vivo</i>, demonstrating a radiosensitizing effect linked to BRCA1 stabilization. Collectively, these findings identified Peme as a BRCA1‑stabilizing agent that enhances therapeutic response to radiation in TNBC. Pharmacological restoration of BRCA1 stability represents a promising strategy to overcome therapeutic resistance in BRCA1‑deficient or functionally compromised BC.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13613309/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148991047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"FXYD5 promotes the growth of glioblastoma by targeting the PI3K/AKT/ACSL4 signaling axis.","authors":"Bang Wang, Yong Qin, Hang Cheng, Yibin Zeng, Lianglei Jiang, Xuebin Hu","doi":"10.3892/or.2026.9193","DOIUrl":"10.3892/or.2026.9193","url":null,"abstract":"<p><p>Glioblastoma (GBM) is the most malignant primary brain tumor, with limited therapeutic options. Dysregulation of FXYD5 has been reported in multiple malignancies, suggesting FXYD5 as a potential target for precision medicine. In the present study, FXYD5 expression and prognostic significance were analyzed using biological analysis on multiple databases and it was identified that FXYD5 was observably upregulated in GBM and inversely correlated with the prognosis of patients. Functional studies were investigated in LN229 and U251 GBM cell lines through FXYD5 knockdown and overexpression approaches, assessing proliferation (Cell Counting Kit‑8), apoptosis (flow cytometry), migration/invasion (Transwell assays) and lipid metabolism (free fatty acids, triglycerides, cholesterol, Nile Red staining). Knockdown of FXYD5 suppressed GBM cell proliferation, migration and invasion, while increasing apoptosis, indicating that FXYD5 may serve as a therapeutic target for GBM. Mechanistic studies examined the PI3K/AKT/long‑chain acyl‑coenzyme A (CoA) synthase 4 4 (ACSL4) pathway via western blotting and rescue experiments, finding that FXYD5 activated the PI3K/AKT signaling pathway, leading to upregulation of ACSL4 and enhanced lipid metabolism. <i>In vivo</i>, a subcutaneous xenograft mouse model was used to evaluate whether PI3K/AKT inhibition could antagonize FXYD5 overexpression‑induced tumor growth and PI3K/AKT inhibition reversed FXYD5 overexpression‑induced tumor growth in the subcutaneous mouse model. These findings revealed that FXYD5 promotes GBM progression via the PI3K/AKT/ACSL4 signaling axis and represents a potential therapeutic target for GBM.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13613038/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148990879","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting the DNHD1‑HDAC6 axis inactivates prostate cancer cell aggressiveness <i>in vitro</i>, suggesting potential therapeutic vulnerability.","authors":"An Ni Lee, Chia Chang Wu, Su Wei Hu, Chih Heng Chen, Yi Te Chiang, Wei Tang Kao, Kai Yi Tzou, Chia Hung Liu, Shao Wei Dong, Yu Ting Wang, Yueh Lin Lee, Siou Bi Li, Che An Wu, Chiao Chun Liao, Ming Hsien Chan, Po Han Chiu, Chien Hsiu Li","doi":"10.3892/or.2026.9204","DOIUrl":"10.3892/or.2026.9204","url":null,"abstract":"<p><p>Prostate cancer progression toward an aggressive, therapy‑resistant disease state remains a major clinical challenge, indicating a need to identify novel molecular drivers of such progression and actionable therapeutic targets. The present study analyzed the role of dynein heavy chain domain 1 (<i>DNHD1</i>), a previously uncharacterized regulator of malignancy, in prostate cancer. Integrative transcriptomic analyses across The Cancer Genome Atlas and independent clinical cohorts revealed that <i>DNHD1</i> is markedly upregulated in advanced‑stage prostate cancer and positively correlated with increasing Gleason scores. Elevated <i>DNHD1</i> expression was associated with poor overall survival and disease‑free survival, which supports its clinical relevance as a prognostic biomarker. Functional analyses demonstrated that <i>DNHD1</i> promoted tumor cell proliferation, colony formation, migration and invasion <i>in vitro</i>. Molecular correlation modeling and pathway analyses revealed histone deacetylase 6 (<i>HDAC6</i>) as a key downstream effector of <i>DNHD1</i>. <i>DNHD1</i> expression was positively correlated with and regulated <i>HDAC6</i> expression in clinical datasets. Gain‑of‑function and loss‑of‑function experiments further revealed that <i>HDAC6</i> is required for <i>DNHD1</i>‑mediated oncogenic phenotypes in prostate cancer, positioning <i>HDAC6</i> as a functional mediator downstream of <i>DNHD1</i>. The DNHD1‑HDAC6 axis was associated with cilium assembly‑related pathways, suggesting a previously unrecognized association between ciliary regulation and prostate cancer progression. HDAC6 inhibition with tubastatin A effectively suppressed <i>DNHD1</i>‑driven tumor growth and motility, as well as increased acetylated α‑tubulin and decreased androgen receptor signaling. These findings indicated a potential therapeutic vulnerability within the DNHD1‑HDAC6 axis. They implied that in prostate cancer, the DNHD1‑HDAC6 axis, a novel regulatory pathway, promotes aggressiveness and that <i>HDAC6</i> is a targetable mediator of <i>DNHD1</i>‑driven malignancy. This axis can be considered a prognostic indicator and mechanistic foundation for developing targeted therapeutic strategies for advanced prostate cancer.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 5","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13659732/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149112730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TPD54 contributes to docetaxel resistance through modulation of P‑glycoprotein localization and activity in oral squamous cell carcinoma cells.","authors":"Maki Nara, Yoshiki Mukudai, Masataka Watanabe, Nodoka Kindaichi, Konomi Yamada, Yuzo Abe, Toshikazu Shimane, Tatsuo Shirota, Seigo Ohba","doi":"10.3892/or.2026.9169","DOIUrl":"https://doi.org/10.3892/or.2026.9169","url":null,"abstract":"<p><p>Tumor protein D52 (TPD52) family proteins are involved in the proliferation, survival and malignant progression of oral squamous cell carcinoma (OSCC). However, their roles in chemoresistance remain incompletely understood. The present study investigated the contribution of TPD52 family proteins to anticancer drug resistance, with particular emphasis on tumor protein D54 (TPD54). OSCC cells were treated with cisplatin, 5‑fluorouracil, or docetaxel (DTX), and the expression of TPD52 family members was examined. Gain‑ and loss‑of‑function analyses were performed to evaluate cell viability, apoptotic responses, cytochrome p450 (P450) and P‑glycoprotein (P‑gp) activities, protein expression, intracellular localization and membrane/cytosol distribution. Anticancer drug treatment increased the expression of TPD52, TPD53 and TPD54. Among these family members, TPD54 showed the strongest association with DTX resistance by attenuating the reduction in cell viability without affecting cell‑cycle progression. TPD54 overexpression attenuated DTX‑associated apoptotic responses and was associated with changes in apoptosis‑, ferroptosis‑, and autophagy‑related marker proteins. TPD54 expression had little effect on the activities of P450 3A4 or P450 1B1 but significantly increased P‑gp activity. Membrane/cytosol fractionation demonstrated increased membrane localization of endogenous P‑gp following TPD54 overexpression, whereas co‑immunoprecipitation and immunocytofluorescence analyses revealed an association and partial co‑localization between TPD54 and P‑gp. These findings suggest that TPD54 contributes to DTX resistance in OSCC cells through modulation of P‑gp localization and activity. The present study identifies TPD54 as a potential contributor to P‑gp‑associated chemoresistance and provides a basis for further investigation of the molecular mechanisms underlying multidrug resistance in OSCC.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 4","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148579325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"[Retracted] MicroRNA‑365 inhibits proliferation, migration and invasion of glioma by targeting PIK3R3.","authors":"Yonggang Zhu, Hongguang Zhao, Min Rao, Songbai Xu","doi":"10.3892/or.2026.9173","DOIUrl":"10.3892/or.2026.9173","url":null,"abstract":"<p><p>Following the publication of the above article, a concerned reader drew to the Editor's attention that western blot data featured in Fig. 5D were apparently the same as those featured in a different research article by the same group in the journal American Journal of Translational Research. In addition, various of the western blot data featured in Figs. 5, 6 and 7, and the cell migration and invasion assay data in Fig. 2C and D, were strikingly similar to data that were featured in other papers written by different authors at different research institutes, some of which have since been retracted, including a pair published in 2014/2015 in the journal PLoS One. Given the fact that the contentious data mentioned above had been included in articles published by other research groups in different journals before this paper was received at <i>Oncology Reports</i>, the Editor has decided that this paper should be retracted from the Journal. The authors were asked for an explanation to account for these concerns, but the Editorial Office did not receive a reply. The Editor apologizes to the readership for any inconvenience caused. [Oncology Reports 37: 2185‑2192, 2017; DOI: 10.3892/or.2017.5458].</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 4","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13439034/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148630836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anticancer effects of tangeretin associated with reactive oxygen species generation, mitochondrial dysfunction and apoptosis in CaSki cells.","authors":"Seung-Hyeon Ahn, Zeeshan Ahmad Bhutta, Hwayoung Na, Hong Kyu Lee, Kyung-Chul Choi","doi":"10.3892/or.2026.9171","DOIUrl":"10.3892/or.2026.9171","url":null,"abstract":"<p><p>Cervical cancer is the fourth most common cancer and the fourth leading cause of cancer‑related mortality among women worldwide. Tangeretin (TAN), a polymethoxylated flavonoid derived from citrus fruit peel, exhibits relatively high structural stability due to its methoxy groups and exerts anticancer effects in various malignancies, including lung, liver and breast cancer. However, to the best of our knowledge, the anticancer effects of TAN in cervical cancer remain insufficiently explored. The present study investigated the mechanisms underlying the anticancer effects of TAN on the CaSki cervical cancer cell line. Cell viability was evaluated using the EZ‑Cytox cell viability assay. The colony formation and cell cycle arrest assays demonstrated that TAN inhibited cell proliferation by inducing G₁ phase arrest. The wound‑healing and Transwell migration assays demonstrated that TAN could reduce the migratory ability of CaSki cells, and the Annexin V/propidium iodide staining assay revealed that TAN increased the apoptotic cell population. Mitochondrial reactive oxygen species (ROS) were identified using MitoSOX™ staining and the mitochondrial membrane potential (MMP) was detected using JC‑1 staining. The findings of these assays suggested that TAN could increase mitochondrial ROS levels and decrease mitochondrial MMP in CaSki cells. Western blot analysis showed that TAN upregulated the protein expression levels of E‑cadherin and Bax. In addition, TAN restored the tumor suppressor protein p53. Collectively, these findings suggested that may exhibit anticancer activity in CaSki cells.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 4","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13445593/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148630855","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polyphenol‑based interventions in breast cancer: Signaling pathways, molecular mechanisms and translational therapeutic strategies (Review).","authors":"Jingjing Zeng, Jinyan Hu, Zhiyuan Ma, Suansuan Zhu, Xiangling Lv, Lanhai Zhang, Mimi Shen, Taolang Li","doi":"10.3892/or.2026.9176","DOIUrl":"10.3892/or.2026.9176","url":null,"abstract":"<p><p>Breast cancer (BC) comprises multiple molecular subtypes with distinct epidemiological, biological and therapeutic features. Although advances in diagnosis and systemic therapy have improved patient outcomes, therapeutic resistance, treatment‑related toxicity and disease recurrence remain major clinical challenges. Growing evidence suggests that plant‑derived polyphenols may influence BC progression through multiple biological mechanisms. These compounds can inhibit tumor‑cell proliferation, migration, angiogenesis, inflammation, epithelial‑mesenchymal transition and metastasis, while promoting apoptosis, autophagy, cell‑cycle arrest and tumor‑suppressive responses. Mechanistically, polyphenols may regulate several interconnected signaling pathways involved in BC development and progression, including PI3K/AKT/mTOR, p53, NF‑κB, STAT3, Wnt/β‑catenin and MAPK signaling. In addition to their direct effects on tumor cells, polyphenols may interact with the gut microbiome, which in turn influences polyphenol metabolism, estrogen homeostasis, immune regulation, inflammation and bioavailability. Probiotics, prebiotics and microbiota‑derived metabolites may further influence this polyphenol‑gut microbiome‑BC axis. Polyphenols have also been explored as adjuvant or supportive agents in combination with chemotherapy, endocrine therapy and radiotherapy, as well as in novel delivery systems designed to improve their bioavailability and therapeutic efficacy. However, most current evidence remains preclinical. Well‑designed clinical trials are therefore needed to define the optimal formulations, doses, safety profiles, pharmacokinetics and therapeutic relevance of polyphenol‑based interventions in BC.</p>","PeriodicalId":19527,"journal":{"name":"Oncology reports","volume":"56 4","pages":""},"PeriodicalIF":4.7,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13488138/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148761305","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}