Oncology reports最新文献

Esophageal squamous cell carcinoma (ESCC) ranks among the primary contributors to cancer‑related mortality in China. Resistance to paclitaxel markedly diminishes its therapeutic effectiveness and outcomes. Anaerobic glycolysis is a pivotal mechanism in cancer progression. Insulin‑like growth factor 2 mRNA binding protein 2 (IGF2BP2) as a reader of RNA N6‑methyladenosine (m6A) modification ensures the stability of RNA at the post‑transcriptional level. Nonetheless, the role and mechanism of IGF2BP2 in mediating paclitaxel resistance and anaerobic glycolysis in ESCC remain unclear. The current study selected two ESCC cell lines (KYSE30 and KYSE150). Cell proliferation and clonogenic ability were assessed via functional experiments. Apoptosis was quantified through flow cytometry. The rate of anaerobic glycolysis was determined via glycolysis assays. The stability of Forkhead box M1 (FOXM1) mRNA was assessed through reverse transcription‑quantitative polymerase chain reaction following actinomycin D treatment. Protein levels were analyzed through western blotting. Bioinformatics analysis revealed an overexpression of IGF2BP2 in ESCC. Furthermore, IGF2BP2 silencing inhibited cell proliferation and clonogenic activity. RNA and m6A‑sequencing results suggested that FOXM1 is critical to IGF2BP2‑mediated paclitaxel resistance in ESCC. Additionally, it was discovered that the silencing of IGF2BP2 compromises FOXM1 mRNA stability, reduces anaerobic glycolysis, and diminishes paclitaxel resistance. Finally, FOXM1 overexpression mitigated the effects of IGF2BP2 silencing in ESCC cells. The current findings underscore the significant role of the IGF2BP2‑FOXM1 signaling pathway in modulating anaerobic glycolysis and paclitaxel resistance in ESCC, offering insights into future therapeutic approaches to this malignancy.

Acute myeloid leukemia (AML) is a highly heterogeneous hematologic malignancy, characterized by complex molecular features and mechanisms of treatment resistance, which lead to a poor prognosis and high relapse rates. The complexity of multi‑pathway interactions and the dysregulated dynamics of tumor cell death pathways may contribute to the wide range of clinical outcomes observed despite advancements in current therapies. Most current research focuses on a single form of cell death, neglecting the mechanisms of other death pathways and their synergistic interactions, which hinders the development of novel therapeutic approaches. The present review systematically integrates and compares the molecular features of key cell death modalities in AML, including autophagy, apoptosis, pyroptosis, necroptosis, ferroptosis and cuproptosis. The present review analyzes their specific triggers, signaling hubs and regulatory networks within the metabolic microenvironment, and discusses the dynamic crosstalk among these pathways. A key focus is the therapeutic potential of exploiting this crosstalk to design synergistic combination therapies. To overcome the limitations of conventional treatments and improve patient outcomes, it is essential to further investigate the transition mechanisms of various cell death modes in AML progression, drug resistance and relapse. Additionally, establishing a theoretical foundation for the development of innovative therapies that synergistically regulate multiple death pathways is crucial.

Following the publication of the above paper, it was drawn to the Editor's attention by a concerned reader that, regarding the cell migration and invasion assay experiments shown in Fig. 4, the 'Mock' data panel in Fig. 4A‑a (A549 cell line, migration assay) was apparently identical to the 'Mock' data panel in Fig. 4B‑b (SPC‑A1 cell line, invasion assay), even though the reported experimental conditions were different. The authors were contacted by the Editorial Office to offer an explanation for this apparent data duplication; however, up to this time, no response from them has been forthcoming. 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 30: 2027‑2034, 2013; DOI: 10.3892/or.2013.2728].

Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that, for the Transwell assay data shown in Fig. 5B on p. 1088, the rightmost panels in the top and the bottom rows appeared to contain a small overlapping section, suggesting that data which were intended to show the results of differently performed experiments had been derived from the same original source. The authors were contacted by the Editorial Office to offer an explanation for this apparent anomaly in the presentation of the data in this paper; however, up to this time, no response from them has been forthcoming. 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 35: 1083‑1090, 2016; DOI: 10.3892/or.2015.4467].

Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that, regarding the western blot experiments shown in Figs. 6E and 7C, a pair of the gel slices were strikingly similar in appearance, suggesting that the same data had been included in these figures to show the results with different proteins. Moreover, two additional gel slices in these figures had apparently been re‑used in a pair of subsequent papers published by the same research group, where the experimental conditions were indicated to be different, and it was noted by the Editorial Office that one of the gel slices may have contained an anomaly in the form of a break in the continuity of the gel. Upon asking the authors to provide the Editorial Office with an explanation of the above issues, they did supply us with revised versions of Figs. 6E and 7C; however, it was subsequently pointed out to the authors that certain of the western blot data in Fig. 6E had apparently reappeared in a further paper by the same authors, in the journal Integrative Cancer Therapies. Owing to the lack of a further response from the authors in relation to the latter query, the Editor of Oncology Reports has decided that this paper should now be retracted from the Journal on account of a lack of confidence in the presented data. The Editor apologizes to the readership for any inconvenience caused. [Oncology Reports 44: 2595‑2609, 2020; DOI: 10.3892/or.2020.7787].

Poorly differentiated cancers, including esophageal squamous cell carcinoma (ESCC), exhibit higher malignant potential and worse prognoses than well‑differentiated types. The present study aimed to identify microRNAs (miRNAs or miRs) involved in ESCC progression and their target mRNAs, focusing on tumor differentiation. miRNA candidates were selected using a miRNA array‑based approach and GEO datasets, comparing expression levels between poorly and non‑poorly differentiated ESCC. Clinical samples (n=61) and cell lines were analyzed to determine the significance and function of the selected miRNAs and their target mRNA. miR‑100‑5p and miR‑203a‑3p were significantly downregulated in poorly differentiated ESCC, with lower expression strongly associated with poorer overall survival (OS) (miR‑100‑5p: P=0.02; miR‑203a‑3p: P=0.05) and relapse‑free survival (RFS) (miR‑100‑5p: P=0.04; miR‑203a‑3p: P=0.12). Overexpression of these miRNAs suppressed cell migration and invasion. FKBP5 was identified as a common target, with its expression significantly reduced upon double‑transfection with miR‑100‑5p and miR‑203a‑3p. FKBP5 downregulation reduced tumor aggressiveness in KYSE70 cells, and clinical samples showed significantly worse survival rates in patients with high FKBP5 expression (OS: P=0.02; RFS: P=0.04). These findings suggest that miR‑100‑5p and miR‑203a‑3p act as tumor suppressors by targeting FKBP5, highlighting FKBP5 as a potential therapeutic target in ESCC.

In recent years, immune checkpoint inhibitors such as nivolumab have been used to treat recurrent or metastatic head and neck cancer. However, some patients do not respond to nivolumab, and the treatment options for these patients are limited. Therefore, identifying compounds for developing new therapeutic strategies for intractable cancer is important. The acquired multidrug‑resistant metastatic head and neck squamous cell carcinoma cell line, R HSC‑3, expresses refractory cancer‑specific proteins such as the drug excretion transporter, ATP binding cassette subfamily G member 2, the cancer stem cell markers, CD44, SRY‑box transcription factor 9 and Notch, and the poor prognosis factor, fibroblast growth factor 9, and is a useful in vitro model for acquired multidrug resistance. In the present study, compounds that may be more effective than conventional chemotherapeutic drugs in R HSC‑3 cells were searched and the cell death mechanism was investigated. The results showed that naphthoquinones inhibited the viability of R HSC‑3 cells at low concentrations and induced necroptotic cell death. Naphthoquinone‑induced necroptotic cell death in R HSC‑3 cells induced the expression of calreticulin, an immunogenic marker. It was further found that mitochondrial‑derived reactive oxygen species mediated the oxidative stress damage by naphthoquinone‑induced necroptotic cell death in these cells. Moreover, necroptotic cell death by shikonin, a naphthoquinone, may generate immunogenic signals from multidrug‑resistant cancer cells. The present study revealed that naphthoquinones may not only induce necroptosis in refractory head and neck cancer cells but also induce tumor immunity. Therefore, naphthoquinones may represent a new avenue for the development of new therapeutic agents targeting multidrug‑resistant head and neck cancer.

Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that, for the western blot data shown in Figs. 1E and 4, the FGFR blots and control GAPDH blots were both strikingly similar in these figures, suggesting that the same data had been included in these, even though the results from differently performed experiments were intended to have been portrayed. The authors were contacted by the Editorial Office to offer an explanation for these apparent anomalies in the presentation of the data in this paper; however, up to this time, no response from them has been forthcoming. 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 30: 2777‑2784, 2013; DOI: 10.3892/or.2013.2796].

Following the publication of this paper, it was drawn to the Editor's attention by a concerned reader that the 'Normoxia / U87' panel in Fig. 1A appeared to overlap with the 'CCR5 siRNA' panel in Fig. 2B; in addition, the 'Hypoxia / U87‑Mφ' panel in Fig. 1A appeared to overlap with the 'Control siRNA' panel in Fig. 2B. The authors were contacted by the Editorial Office to offer an explanation for these apparent anomalies in the presentation of the data in this paper; however, up to this time, no response from them has been forthcoming. 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 36: 3522‑3528, 2016; DOI: 10.3892/or.2016.5171].

Following the publication of the above paper, it was drawn to the Editor's attention by a concerned reader that, regarding the Transwell assay data shown in Fig. 2C and 4D, two pairs of overlapping sections of data were identified comparing the panels in these figures, where the results from differently performed experiments were intended to have been portrayed. The authors were contacted by the Editorial Office to offer an explanation for this apparent duplication of data within the two figures; however, up to this time, no response from them has been forthcoming. 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 25: 1581‑1587, 2011; DOI: 10.3892/or.2011.1251].