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.

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were featured in other papers written by different authors at different research institutes, some of which have since been retracted, including a pair published in 2014/2015 in the journal PLoS One.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 Oncology Reports, 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].

The tumor immune microenvironment (TIME) is the key determinant of limited efficacy and acquired resistance to cancer immunotherapy across human malignancies. In this context, connective tissue growth factor (CTGF) has been implicated in multiple TIME‑related processes, including tumor‑cell phenotypic regulation, extracellular matrix (ECM) remodeling, immune‑cell modulation, and cytokine‑network alterations. Collectively, this suggests that CTGF may participate in coordinated crosstalk among structural, signaling, and immune components of the TIME. Empirical evidence supports roles for CTGF in selected tumor and stromal settings. However, its broader contribution to coordinated TIME remodeling remains partly inferential and requires further experimental validation. Where present, such coordinated effects may impair antitumor immune recognition and promote tumor‑cell survival within specific tumor microenvironmental settings. The present review summarizes the core mechanisms of CTGF‑mediated TIME remodeling and outlines the translational potential of CTGF‑targeted combination immunotherapies and key research priorities to advance its clinical translation.

Breast cancer has the highest incidence among malignant tumors in women worldwide. Although targeted therapy, chemotherapy, and endocrine therapy have achieved significant efficacy, acquired resistance remains a major challenge affecting patient prognosis. The present review systematically outlines five core mechanisms of resistance to breast cancer treatment, including overexpression of ATP‑binding cassette transporters that reduce intracellular drug accumulation; a hypoxic and immunosuppressive tumor microenvironment, together with breast cancer stem cells, that sustains stemness and impairs treatment response; DNA methylation, histone modifications, and non‑coding RNAs that mediate epigenetic reprogramming, leading to silencing of tumor suppressors or activation of resistance pathways; compensatory activation of multiple DNA damage repair pathways, including homologous recombination, non‑homologous end joining, base excision repair, nucleotide excision repair, and mismatch repair, which compromises the efficacy of chemotherapy and poly (ADP‑ribose) polymerase inhibitors; and metabolic reprogramming involving glycolysis, amino acid, nucleotide, and lipid metabolism that supplies tumor cells with energy, reducing equivalents, and biomass for proliferation, while simultaneously promoting immune evasion. Corresponding to these mechanisms, this review also summarizes potential therapeutic strategies, including combined targeted therapy, immunotherapy, and novel drug delivery systems. Therefore, a comprehensive dissection of the multidimensional networks mediating therapy resistance in breast cancer will provide both theoretical foundations and practical pathways for discovering novel biomarkers, optimizing precision combination therapies, and ultimately prolonging patient survival.

Polyphyllin II, a natural steroidal saponin extracted from Paris polyphylla, exhibits potent antitumor activity in thyroid cancer. In the present study, bioinformatics analysis, molecular docking, Drug Affinity Responsive Target Stability assay, Cell Counting Kit‑8 assay, flow cytometry, Transwell assay, wound‑healing assay, reverse transcription‑quantitative PCR, western blotting and xenograft experiments were performed to investigate the antitumor effects and molecular mechanism of polyphyllin II in thyroid cancer. Polyphyllin II significantly inhibited cell proliferation, migration and invasion, while inducing apoptosis more prominently in TPC‑1 cells and causing cell cycle arrest in both TPC‑1 and 8305C cells. By using integrated bioinformatics screening and experimental validation, histamine receptor H1 (HRH1) was identified as a key oncogenic target that is highly expressed in thyroid cancer and contributes to malignant progression. With regard to its mechanism of action, polyphyllin II suppressed HRH1‑mediated activation of the Wnt/β‑catenin signaling pathway, reduced β‑catenin nuclear accumulation and downregulated the expression levels of downstream pathway‑related genes. Collectively, these findings demonstrate that polyphyllin II attenuates thyroid cancer progression by targeting HRH1 and blocking Wnt/β‑catenin signaling, highlighting its potential as a promising candidate for targeted therapy.

M2 tumor‑associated macrophages (M2‑TAMs) have been reported to promote tumor growth through exosome‑dependent mechanisms. However, the exact role of exosomes derived from M2‑TAMs (M2‑TAM‑Exos) in lung cancer progression remains unclear. In The present study, M2‑like macrophages (IL‑4/IL‑13‑polarized THP‑1‑derived macrophages) were shown to release exosomes that lung cancer cells effectively internalized. These exosomes markedly enhanced the proliferation, migration, and invasion of lung cancer cells, thereby promoting malignancy. Further analyses revealed that M2‑like macrophage‑derived exosomes contain high levels of microRNA (miR)‑491‑3p. In vitro and in vivo experiments confirmed miR‑491‑3p as an oncogenic miR, while its inhibition markedly reduced cancer cell aggressiveness. Additional experiments demonstrated that miR‑491‑3p suppressed UBE2D3 expression after entering lung cancer cells. Collectively, these findings suggest a model in which M2‑like macrophages deliver miR‑491‑3p via exosomes to downregulate UBE2D3, facilitating lung cancer progression.

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.

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.

Exportin 1 (XPO1) is a key nuclear export receptor that mediates the nuclear export of tumor suppressor proteins and growth‑regulatory mRNAs from the nucleus to the cytoplasm. In several types of cancer, XPO1 is overexpressed or hyperactivated, leading to aberrant cytoplasmic sequestration of key tumor suppressors such as p53, p21, p73, FOXO and Rb. This mislocalization abrogates their nuclear transcriptional functions, disrupting cell cycle arrest, apoptosis and DNA repair, thereby promoting uncontrolled proliferation, survival and therapy resistance. Targeting XPO1 with selective inhibitors of nuclear export (SINE) has emerged as a promising anticancer strategy. The present review systematically examines the molecular mechanisms of XPO1‑driven tumorigenesis and its rationale as a therapeutic target. The present review focuses on the clinical translation of SINE drugs, especially selinexor (KPT‑330), in hematologic and solid tumors, critically assesses the limitations of monotherapy and explores the mechanistic basis for synergistic combination strategies. Ongoing clinical trials and future directions to optimize therapeutic efficacy are also highlighted. Collectively, the present review aims to provide a comprehensive foundation for advancing basic and clinical research on XPO1‑targeted therapies.

Transmembrane protein 6 superfamily member 2 (TM6SF2) is a potential tumor suppressor in hepatocellular carcinoma (HCC). At present, the role of TM6SF2 in HCC is poorly studied. The aim of the present study was to elucidate the potential role of TM6SF2 in hepatocellular carcinoma and its associated molecular mechanisms. The correlation between TM6SF2 and HCC progression was assessed using a bioinformatics approach. A TM6SF2‑overexpressing Huh‑7 cell model was constructed to examine the effects of TM6SF2 on cell proliferation, migration, invasion, cell‑cycle distribution, and apoptosis. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses of differentially expressed genes (DEGs) in the control Vector and TM6SF2 groups were performed using RNA sequencing (RNA‑Seq) data. Reverse transcription‑quantitative PCR and western blotting were used to verify the expression of candidate DEGs involved in cell cycle regulation and apoptosis. Overexpression of TM6SF2 inhibited HCC cell proliferation, invasion, and migration and promoted apoptosis. TM6SF2 overexpression induced S‑phase cell‑cycle arrest and promoted apoptosis in Huh‑7 cells. RNA‑Seq analysis showed that the majority of DEGs were involved in cell growth and biological processes, including the negative regulation of cell growth. KEGG pathway analysis identified the p53 signaling pathway as significantly enriched. Western blot analysis further showed increased levels of phosphorylated p53 and p21, suggesting p53‑related molecular changes. These findings suggest that TM6SF2 may exert anti‑tumor effects in Huh‑7 cells by inducing S‑phase cell‑cycle arrest and promoting apoptosis. The observed increases in phosphorylated p53 and p21 indicate that p53‑related molecular changes may be associated with TM6SF2 overexpression, although this requires further validation.

Subsequently to the publication of the above paper, an interested reader drew to the authors' attention that the western blot Hsp90α bands in Fig. 1A were strikingly similar to data featured in two other papers written by the same research group; in Fig. 3A of reference 20 (by Qilin Wang et al, in the journal Cancer Cell International, published in 2012), and Fig. 8A in reference 43 (by Qilin Wang and Xiangguo Liu, also in the journal Cancer Cell International, published in 2020). The authors explained that they performed the Hsp90α knockdown experiments and western blot assays using duplicate membranes from the same experiments, although these were published separately in the three papers. The Hsp90α data were intentionally shared among the papers in order to show the same knockdown efficiency. Secondly, the microscopic image showing 1.0 µM Tanespimycin treatment in Fig. 2C of the abovementioned article had also apparently been included in Fig. 5B in a paper by Qilin Wang and Xiangguo Liu published in 2020, also in the journal Cancer Cell International. In that case, the authors re‑examined their original data, and realized that the data in question in Fig. 2C had been inadvertently copied during editing. The authors proposed providing alternative data for Fig. 1A from other independent Hsp90α and Hsp90β knockdown experiments, respectively, and the revised version of Fig. 1 is shown on the next page. The revised version of Fig. 2, now showing all the correct data in Fig. 2C, is shown on the third page. The authors regret the errors that were made during the compilation of the original figures, and are grateful to the editor of Oncology Reports for allowing them the opportunity to publish this Corrigendum. Note that these errors did not have a significant impact on the conclusions reached in this study. All the authors agree with the publication of this corrigendum; furthermore, they apologize to the readership for any inconvenience caused. [Oncology Reports 44: 2725‑2734, 2020; DOI: 10.3892/or.2020.7789].

Subsequently to the publication of the above paper, an interested reader drew to the authors' attention that the rabbit anti‑apoptosis‑associated speck‑like protein containing a C‑terminal caspase recruitment domain (ASC) western blot data shown in Fig. 4A on p. 275 were strikingly similar to data that had already been published two years previously in Fig. 6 of an article in British Journal of Pharmacology that featured the author Xufeng Tao in common. Upon investigating the figure in question, the authors have realized that the data in Fig. 4A in the above article had inadvertently been assembled incorrectly. A revised version of Fig. 4, now showing western blot data from an alternative experiment in Fig. 4A (where the results presented are very similar to those in the originally published article) is shown on the next page. In addition, the authors have realized that the immunohistochemical data shown in Fig. 3A, highlighting the effects of emodin on MPO‑immunopositive stained regions of the pancreas, were not representative of these experiments, and a revised version of Fig. 3, showing replacement data for Fig. 3A, is also shown on the next page. The authors regret the errors that were made during the compilation of the original figures, and are grateful to the editor of Oncology Reports for allowing them the opportunity to publish this Corrigendum. Note that the errors that were made in compiling this pair of figures did not have a significant impact on the conclusions reached in this study. All the authors agree with the publication of this corrigendum; furthermore, they apologize to the readership for any inconvenience caused. [Oncology Reports 41: 270‑278, 2019; DOI: 10.3892/or.2018.6844].

Ferroptosis, an iron‑dependent form of programmed cell death, is a promising target for cancer therapy. Peptidyl‑prolyl cis/trans isomerase 1 (PIN1), a member of the peptidyl‑prolyl cis/trans isomerase family, is often overexpressed in cancer and contributes to tumor cell proliferation, survival and metastasis. The present study investigated whether PIN1 regulates ferroptosis in gastric cancer (GC). GC cell models with either PIN1 knockdown or overexpression were established and treated with the ferroptosis inducer erastin, followed by assessment of cell viability and proliferation rate using Cell Couting Kit‑8 and colony formation assays, detection of PIN1 and cytoplasmic polyadenylation element binding protein 1 (CPEB1) expression via western blotting and reverse transcription‑quantitative PCR, and evaluation of glutathione peroxidase 4 (GPX4) expression through immunofluorescence assay. Experimental results indicate that PIN1 depletion increases erastin‑induced ferroptosis, as evidenced by increased levels of reactive oxygen species, malondialdehyde and intracellular free iron. PIN1 overexpression attenuates the erastin‑induced ferroptotic response, as evidenced by decreased levels of ferroptosis‑related biomarkers. Further analysis reveals that silencing PIN1 upregulates CPEB1, which, in turn, suppresses GPX4 expression. Simultaneous knockdown of CPEB1 reverses the ferroptosis‑enhancing effect of PIN1 depletion. These mechanistic findings suggest that PIN1 promotes GPX4 expression by repressing CPEB1, thus inhibiting Erastin‑induced ferroptotic cell death in GC. In vivo experiments further suggest that PIN1 knockdown significantly reduces the tumorigenic potential of GC cells. A novel PIN1‑CPEB1‑GPX4 axis was identified, in which PIN1 downregulates CPEB1 to mediate ferroptosis resistance. This axis represents a potential therapeutic target, as PIN1 knockout demonstrates significant tumor suppression in animal models. The present study identifies a novel PIN1‑CPEB1‑GPX4 regulatory axis that controls ferroptosis, suggesting its potential as a therapeutic target for advanced GC.

With the increasing global burden of cancer, traditional chemotherapy is limited by issues such as high toxicity and poor targeting, making the development of new therapeutic strategies an urgent priority. As natural bioactive macromolecules, herbal polysaccharides have become a hotspot in antitumor research due to their multi‑target effects, low toxicity, and excellent biocompatibility. The present review summarizes recent advances in the mechanisms of plant polysaccharides in antitumor activity and their applications in drug delivery systems. It highlights their synergistic antitumor effects through multiple pathways, including regulation of the immune microenvironment, induction of programmed cell death, modulation of the microbiota‑immune axis, and inhibition of angiogenesis and metastasis. These compounds significantly enhance the efficacy of chemotherapy and immunotherapy while reversing drug resistance. Novel formulations such as polysaccharide‑based nano‑delivery systems, selenium‑modified complexes and gel platforms have further improved drug targeting, stability, and immunomodulatory efficacy, providing a solid theoretical foundation and innovative directions for integrated traditional Chinese and Western medicine in cancer treatment.

Tanshinone IIA (Tan IIA), a lipophilic abietane‑type diterpenoid isolated from Salvia miltiorrhiza, exhibits a set of mechanistic features that distinguish it from numerous other natural products. Recent studies in breast cancer models have revealed that Tan IIA not only induces apoptosis but also targets several cancer‑relevant vulnerabilities, including the stabilization of G‑quadruplex (G4) DNA structures, the disruption of mitochondrial oxidative phosphorylation and the inhibition of estrogen receptor α/human epidermal growth factor receptor 2‑driven signaling. Tan IIA further modulates epigenetic regulators such as lysine demethylase 1A and promotes ferroptosis by disturbing redox homeostasis. These mechanisms support the multifaceted anticancer potential of Tan IIA; however, their relative contribution appears to be highly dependent on concentration, formulation, derivative structure and breast cancer subtype. Nevertheless, Tan IIA suffers from poor aqueous solubility, rapid metabolic conversion and low oral bioavailability, reported to be ~2‑6% in rats, which hinder its translational prospects. Recent efforts involving structural optimization and nanoscale delivery systems have partially addressed these limitations. Overall, this review integrates current mechanistic and pharmacological evidence and highlights both the therapeutic promise and the critical barriers that must be overcome for the successful development of Tan IIA‑based interventions in breast cancer. High‑micromolar in vitro findings, particularly those related to reactive oxygen species‑dependent cytotoxicity, ferroptosis or G4 stabilization, should be interpreted cautiously unless supported by pharmacokinetic, tumor‑exposure and in vivo target‑engagement data.