Oncology reports最新文献

{"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}

{"title":"Stable overexpression of Nup88 enhances HeLa cell migration through independent regulation of Kif7 and Gli1.","authors":"Masaki Makise, Ryota Uchimura, Ayano Shiraishi, Akihiko Kuniyasu","doi":"10.3892/or.2026.9170","DOIUrl":"10.3892/or.2026.9170","url":null,"abstract":"<p><p>Elevated expression of nucleoporin (Nup) 88 is often observed in various types of cancer and correlates with tumor grade. However, the underlying molecular mechanism by which Nup88 induces cancer malignancy remains unclear. The present study showed that stable overexpression of Nup88 in HeLa cells enhanced cell migration by modulating the expression of kinesin family member (Kif) 7 and glioma‑associated oncogene homolog (Gli) 1. The expression level of Kif7, a negative regulator of the Hedgehog (Hh) pathway acting through the processing of Gli2 and Gli3, was markedly reduced at both the mRNA and protein levels in Nup88 overexpressing HeLa cells. The reduced expression of Kif7 was restored by treatment with a DNA methylation inhibitor, suggesting epigenetic regulation. Co‑overexpression of a truncated Kif7 (514‑1343 aa), which possesses a large part of the Gli2 binding domain, suppressed the Nup88‑induced migration, suggesting that the downregulation of Kif7 contributed to the enhanced cell migration. In parallel, Gli1 expression was elevated through activation of the MEK‑ERK pathway and its knockdown markedly suppressed Nup88‑induced cell migration. Although both Kif7 and Gli1 are components of the Hh pathway, neither the knockdown of Kif7 nor the overexpression of Gli1 affected the expression of the other. Instead, the truncated Kif7 (514‑1343 aa) physically interacted with Gli1, suggesting that Kif7 suppressed enhanced migration by inhibiting Gli1 function. These findings revealed that Nup88 promotes cell migration by modulating the expression of Kif7 and Gli1, providing new insight into the mechanism of Nup88‑driven malignancy.</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/PMC13445597/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148579278","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":"Decoding the metabolic‑immune crosstalk: The role of glutamine and ammonium reprogramming in prostate cancer immune evasion (Review).","authors":"Peilong Wang, Xiaoran Li, Teng Ma, Jun Mi","doi":"10.3892/or.2026.9186","DOIUrl":"10.3892/or.2026.9186","url":null,"abstract":"<p><p>Prostate cancer progression is typically driven by metabolic reprogramming and immune evasion, yet the interface between these processes remains incompletely understood. Dysregulated glutamine metabolism extends beyond bioenergetic support to actively shape antitumor immunity through nutrient competition and ammonium accumulation within the tumor microenvironment. Ammonium, traditionally viewed as a toxic waste product, is a critical immunosuppressive metabolite that impairs T cell function and promotes macrophage M2 polarization. The present review aimed to summarize the bidirectional crosstalk between tumor metabolism and immune cells, with emphasis on how metabolic alterations drive therapeutic resistance. While the majority of evidence supporting this axis derives from preclinical models, the present review highlights the glutamine‑ammonium axis as a promising but largely untapped therapeutic target requiring translation into clinical investigation, including combination strategies with immunotherapy.</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/PMC13547942/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148840883","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":"Cancer‑associated fibroblast‑derived extracellular vesicles promote pancreatic cancer progression via the RAP1B/ANLN axis.","authors":"Daigo Yoshimori, Mitsuhiro Kudo, Kousuke Ishino, Junji Ueda, Yukako Shintani-Domoto, Akira Matsushita, Youichi Kawano, Takashi Ono, Takahiro Haruna, Kazuhiko Endo, Akira Hamaguchi, Takenori Fujii, Yoko Kawamoto, Kiyoshi Teduka, Taeko Kitamura, Atsushi Masamune, Akihisa Matsuda, Hiroshi Yoshida, Ryuji Ohashi","doi":"10.3892/or.2026.9182","DOIUrl":"10.3892/or.2026.9182","url":null,"abstract":"<p><p>Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal malignancies worldwide, characterized by late diagnosis, rapid progression and resistance to conventional therapies. Cancer‑associated fibroblast (CAF)‑derived extracellular vesicles (EVs) contribute to PDAC progression, but their downstream molecular effectors remain unclear. In the present study, it was demonstrated that CAF‑derived EVs enhanced the proliferative, migratory and invasive capacity of PDAC cells across two independent cell lines, as assessed by Cell Counting Kit‑8 assays and Transwell migration and Matrigel invasion assays. RAP1B was identified as a prominently upregulated protein by label‑free proteomic profiling following EV exposure. High RAP1B expression, evaluated by immunohistochemistry, in a cohort of 77 resected PDAC specimens tended to be more frequent with advancing pathological stage and was associated with poorer overall survival. RAP1B knockdown using small interfering RNA suppressed proliferation and motility in PDAC cells and induced cytokinesis failure characterized by multinucleation and cytoskeletal abnormalities, as demonstrated by time‑lapse imaging and immunofluorescence staining. Proteomic profiling of RAP1B‑knockdown cells identified anillin (ANLN) as a downstream mediator; ANLN knockdown recapitulated these cytokinetic defects, whereas ANLN knockdown did not reciprocally affect RAP1B levels, establishing a unidirectional RAP1B/ANLN axis. Furthermore, RAP1B depletion sensitized PDAC cells to gemcitabine, showing additive growth inhibition. In conclusion, CAF‑derived EVs mediate PDAC progression via the RAP1B/ANLN axis, representing a novel and promising therapeutic target in PDAC.</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/PMC13504667/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148796259","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":"OLR1 promotes cell proliferation and invasion while represses apoptosis via regulating histone H3 lysine 18 lactylation‑mediated LEMD1 in papillary thyroid cancer.","authors":"Jiawei Yu, Rui Pang, Bo Liu, Lili Chen, Jiewu Zhang","doi":"10.3892/or.2026.9178","DOIUrl":"10.3892/or.2026.9178","url":null,"abstract":"<p><p>Oxidized low density lipoprotein receptor 1 (OLR1) regulates glycolytic metabolism, lactate production and carcinogenesis, but its role in papillary thyroid cancer (PTC) is still unclear. The present study aimed to investigate the effect of OLR1 modification on PTC cellular functions and its interaction with histone H3 lysine 18 lactylation (H3K18la) and downstream molecular mechanisms. Lectin‑like oxidized low‑density lipoprotein receptor‑1 (LOX‑1; OLR1 coding protein) and H3K18la expression was detected in twenty pairs of PTC and non‑tumor tissues by immunohistochemistry. Overexpressed OLR1 and small interfering (si)RNA were transfected into two PTC cell lines (TPC‑1 and IHH‑4 cells). After which, oxamate (to reduce lactate production) or LEM domain containing 1 (LEMD1) siRNA combined with OLR1 overexpression plasmid was used to treat PTC cell lines. Furthermore, PTC xenograft mice were constructed for <i>in vivo</i> verification. LOX‑1 and H3K18la expression was upregulated in PTC tissues versus non‑tumor tissues and LOX‑1 expression positively associated with H3K18la expression in PTC tissues. OLR1 overexpression facilitated cell proliferation and invasion but repressed cell apoptosis in PTC cell lines, while OLR1 siRNA revealed an opposite effect. OLR1 positively regulated lactate production, H3K18la expression and LEMD1 expression. Furthermore, a chromatin immunoprecipitation assay confirmed a direct binding between H3K18la and the LEMD1 promoter. H3K18la expression was lowered by oxamate‑induced lactate reduction, which also attenuated the effect of OLR1 overexpression on PTC cell proliferation, apoptosis and invasion and downregulated LEMD1 expression. Moreover, LEMD1 siRNA weakened the effect of OLR1 overexpression on PTC cell proliferation, apoptosis and invasion. <i>In vivo </i>experiments revealed that OLR1 overexpression elevated tumor volume and weight and upregulated the expressions of LEMD1 and H3K18la; while LEMD1 knockdown reduced tumor volume and weight. In conclusion, OLR1 promotes PTC proliferation and invasion, while represses apoptosis through regulating H3K18la‑mediated LEMD1.</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/PMC13495067/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148762285","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":"[Retracted] Restoration of the tumor‑suppressor function to mutant p53 by <i>Ganoderma lucidum</i> polysaccharides in colorectal cancer cells.","authors":"Dan Jiang, Lingyao Wang, Tong Zhao, Zhaoyu Zhang, Renxia Zhang, Jingji Jin, Yong Cai, Fei Wang","doi":"10.3892/or.2026.9181","DOIUrl":"10.3892/or.2026.9181","url":null,"abstract":"<p><p>Following the publication of the above paper, it was drawn to the Editor's attention by a concerned reader that western blots portraying the protein p53 in Figs. 1C and 4C had previously appeared as p53 bands in an article published in 2010 in the journal <i>PLoS One</i> that featured the author Fei Wang in common, although the exprimental conditions were reported to be different in the previous paper. In addition, regarding the flow cytometric plots shown in Fig. 1D on p. 596, the 'HCT116 P53^' plots for the NTC (upper row) and 5‑FU (lower row) experiments appeared to show similar groupings of dots in specific areas of the quadrants, which would not have been anticipated if these experiments had been performed discretely under different experimental conditions, suggesting a fundamental flaw either in the way in which these experiments were performed or in how the results were outputted. Given that these issues have come to light, the Editor of <i>Oncology Reports</i> has decided that this paper should be retracted from the Journal on account of a lack of confidence in the presented data. After contacting the authors, they accepted the decision to retract the paper. The Editor apologizes to the readership for any inconvenience caused. [Oncology Reports 37: 594‑600, 2017; DOI: 10.3892/or.2016.5246].</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/PMC13501493/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148796305","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] Inhibition of TMEM45A suppresses proliferation, induces cell cycle arrest and reduces cell invasion in human ovarian cancer cells.","authors":"Jing Guo, Li Chen, Ning Luo, Weihong Yang, Xiaoyan Qu, Zhongping Cheng","doi":"10.3892/or.2026.9185","DOIUrl":"10.3892/or.2026.9185","url":null,"abstract":"<p><p>Following the publication of the above article, a concerned author drew to the authors' attention that the western blot data showing the TGF β1‑experiments in Fig. 4C and D on p. 3129 for the HO‑8910 and A2780 cell lines were strikingly similar, suggesting that the data in this figure had been assembled incorrectly. In addition, various of the western blots featured in this figure, and also in Fig. 2B on p. 3127, were remarkably similar to data which were subsequently submitted for publication in articles written by different authors at different research institutes to a number of different journals, at least one of which has since been retracted on account of data sharing issues with other papers. The authors have been contacted by the Editorial Office to offer an explanation for the apparent anomalies in the presentation of the western blot data in this paper, and we are awaiting their response. Owing to the fact that the Editorial Office has been made aware of potential issues surrounding the scientific integrity of this paper, we are issuing an Expression of Concern to notify readers of this potential problem while the Editorial Office continues to investigate this matter further. [Oncology Reports 33: 3124‑3130, 2015; DOI: 10.3892/or.2015.3902].</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/PMC13542680/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148840930","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":"[Corrigendum] Targeting ribonucleotide reductase M2 subunit by small interfering RNA exerts anti‑oncogenic effects in gastric adenocarcinoma.","authors":"Wei Kang, Joanna H M Tong, Anthony W H Chan, Junhong Zhao, Shiyan Wang, Yujuan Dong, Frankie M C Sin, Saifung Yeung, Alfred S L Cheng, Jun Yu, Kafai To","doi":"10.3892/or.2026.9183","DOIUrl":"10.3892/or.2026.9183","url":null,"abstract":"<p><p>Subsequently to the publication of the above article, an interested reader drew to the Editor's attention that apparently the same set of GADPH data panels had been featured in a number of research articles by this group, even though it appeared as if these were intended to have shown the same experimental conditions in most cases. The authors have realized that the GAPDH loading control panel in question, shown in Fig. 1C on p. 2581, had been inappropriately used to represent the same batch of tissue samples in several articles. Although the tissue samples were from the same batch, the authors recognize that using the same GAPDH panel as the loading control across a number of different publications was inappropriate. To address this issue, the authors have replaced both the RRM2 and the GAPDH data in Fig. 1C of the above paper, and the revised version of Fig. 1 is shown on the next page. In addition, upon re‑examining their original data, the authors also realized that certain images captured for the invasion assay in Fig. 3C on p. 2584 contained overlapping sections (for example, the 'Scramble siRNA' and 'RPM2 siRNA' data panels for the AGS cell line). Therefore, the invasion assay experiments were also repeated, and the corresponding panels in Fig. 3C have been replaced. The revised version of Fig. 3 is shown on the second subsequent page. The authors wish to emphasize that the errors made in assembling the data in these figures did not affect the overall conclusions reported in the paper. The authors are grateful to the Editor of <i>Oncology Reports</i> for granting them this opportunity to publish a Corrigendum, and apologize to both the Editor and the readership for any inconvenience caused. [Oncology Reports 31: 2579‑2586, 2014; DOI: 10.3892/or.2014.3148].</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/PMC13504653/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148796324","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] Suppression of PTEN/AKT signaling decreases the expression of TUBB3 and TOP2A with subsequent inhibition of cell growth and induction of apoptosis in human breast cancer MCF-7 cells via ATP and caspase-3 signaling pathways.","authors":"Zhenhua Yang, Ying Liu, Changzheng Shi, Yuqin Zhang, Rongzhao Lv, Rong Zhang, Qian Wang, Yiming Wang","doi":"10.3892/or.2026.9179","DOIUrl":"10.3892/or.2026.9179","url":null,"abstract":"<p><p>Following the publication of the above article, a concerned author drew to the authors' attention that, regarding the data showing caspase-3 activity as measured by a colorimetric assay in Fig. 7 on p. 1015, given the use of the MCF‑7 cell line in this study, it was unexpected that the authors would have identified changes in caspase‑3 activity, since it has been demonstrated that MCF‑7 cells do not express caspase‑3 [for example, see the paper by Jänicke and colleagues entitled 'MCF‑7 breast carcinoma cells do not express caspase‑3'. Breast Cancer Res. Treat., vol. 117.1 (2009); p. 219‑221]. In addition, the reader noted that, in the Materials and methods section, it was stated that an Ac-DEVD-pNA-based assay had been used, which has been reported not to be specific for caspase-3, since this assay also reacts to caspase-7 ['Preparation of the caspase-3/-7 substrate Ac-DEVD-pNA via solution-phase peptide synthesis'. Nat Protoc., vol. 5(2) (2010); p. 294-302]. The reader also noted that it was surprising that none of the western blot experiments included in this study actually probed for the presence of the caspase-3 protein, given that the caspase-3 signaling pathway represented one of the principal foci of the study. The authors have been contacted by the Editorial Office to offer an explanation for these apparent anomalies or curiosities in the presentation of the data in this paper, and we are awaiting their response. Owing to the fact that the Editorial Office has been made aware of potential issues surrounding the scientific integrity of this paper, we are issuing an Expression of Concern to notify readers of this potential problem while the Editorial Office continues to investigate this matter further. [Oncology Reports 37: 1011-1019, 2017; DOI: 10.3892/or.2017.5358].</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/PMC13495066/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148760589","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}