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Molecular & Cellular Toxicology · 2022 · IF 1.718

circLETM1 upregulates KRT80 via adsorbing miR-143-3p and promotes the progression of colorectal cancer

Li Hua,Guo Junyu,Qin Zhongwei,Wei Mingwei,Guo Houji,Huang Fuda

Background Emerging evidence has indicated that circular RNAs (circRNAs) play vital roles in colorectal cancer (CRC). CircRNA leucine zipper and EF-hand containing transmembrane protein 1 (circLETM1) have been found to be ectopic in CRC, but their role in CRC has not been studied yet. Objective This study aims to explore the roles of circLETM1 in CRC and the possible molecular mechanism. Result The results showed that circLETM1 was highly expressed in CRC cells, and was localized at the cytoplasm. Functional assays verified that overexpression of circLETM1 could facilitate, but circLETM1 downregulation could hamper proliferation, migration and invasion abilities of CRC cells. In addition, mechanism assays found that circLETM1 absorbed and reduced microRNA (miR)-143-3p expression to promote keratin 80 (KRT80). Rescue experiments proved that circLETM1 mediated CRC proliferation, migration and invasion through KRT80. Conclusion Taken together, our results suggested that circLETM1 promotes proliferation, migration and invasion through the miR-143-3p/KRT80 axis in CRC. Therefore, targeting circLETM1 may provide a novel option for CRC treatment.

研究领域: 肿瘤学 · 分子生物学 · 癌症研究
✓ 已验证 DOI 高影响因子
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BIOLOGICAL & PHARMACEUTICAL BULLETIN · 2023 ·Vol. 46 ·期 7 ·883-892 · IF 2

ELK3 Targeting AEG1 Promotes Migration and Invasion of Ovarian Cancer Cells under Hypoxia

Xiaoyu Yu,Chun Du,Yifei Cui,Yang Jiang,Di Feng

Ovarian cancer (OC) is one of the most common tumors in female reproductive organs with a five-year survival rate of less than 45%. Metastasis is a crucial contributor to OC development. ETS transcription factor (ELK3), as a transcriptional factor, have been involved in multiple tumor development. However, its role in OC remains elusive. In this study, we observed high expression of ELK3 and AEG1 in human OC tissues. OVCAR-3 and SKOV3 cells were treated with hypoxia to mimic tumor microenvironment in vivo. We found that the expression of ELK3 was significantly increased in cells under hypoxia compared with normoxia. ELK3 knockdown inhibited cell migration and invasion abilities under hypoxia. Moreover, ELK3 knockdown decreased β-catenin expression and inhibited the activation of Wnt/β-catenin pathway in SKOV3 cells under hypoxia. Astrocyte-elevated gene-1 (AEG1) has been reported to promote OC progression. Our results showed that the mRNA level of AEG1 was decreased when ELK3 knockdown under hypoxia. Dural luciferase assay confirmed that ELK3 bound to gene AEG1 promoter (−2005–+15) and enhanced its transcriptional activity under hypoxia. Overexpression of AEG1 increased the migration and invasion abilities of SKOV3 cell with ELK3 knockdown. In the absence of ELK3, the activation of β-catenin was recovered by AEG1 overexpression. To sum up, we conclude that ELK3 promotes AEG1 expression by binding to its promoter. ELK3 could promote migration and invasion of OC cells by targeting AEG1, which provides a potential basis for therapeutic approaches to OC.

CAS / MDL: 30525-89-4 47165-04-8
研究领域: 癌症生物学 · 分子生物学 · 细胞生物学
✓ 已验证 产品关联 DOI PubMed 高影响因子
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TROPICAL JOURNAL OF PHARMACEUTICAL RESEARCH · 2021 ·Vol. 18 ·期 12 ·2531-2538 · IF 0.533

Curcumin inhibits viability and promotes apoptosis by modulating miR-17/caspase-9 pathway in colorectal cancer

Jun Tang,Jingfang Yang

Purpose: To investigate the potential role of curcumin in osteosarcoma (OS) cell migration and invasion, and also to explore the underlying mechanism of action. Methods: OS cell lines, Saos-2 and U2OS, were treated with various concentrations of curcumin (0, 10, 20, 50 μM) for 48 h. Transwell assay was used to determine the migratory and invasive activities of human OS cells while miR-33b-5p expression levels were measured using quantitative real time polymerase chain reaction (qRT-PCR). Expressions of metastasis-related genes, such as matrix metalloproteinases (MMPs), were quantified by qRT-PCR or western blot. The interaction between miR33b-5p and Sirtuin 6 (SIRT6) was evaluated by luciferase assay. Results: Curcumin inhibited the migratory and invasive activities of huamn OS cells, and downregulated MMP2 and MMP9 (p < 0.05). Moreover, in curcumin-treated OS cells, miR-33b-5p expression was upregulated while SIRT6 expression was significantly downregulated (p < 0.05). Overexpression of miR-33b-5p downregulated SIRT6 mRNA and protein expression, whereas transfection with miR-33b-5p inhibitor upregulated SIRT6 expression in OS cells (p < 0.05). Furthermore, curcumin suppressed SIRT6 expression by upregulating miR-33b-5p expression in OS cells. Finally, overexpression of SIRT6 or miR-33b-5p inhibitor reversed the suppression of OS cell metastasis induced by curcumin (p < 0.05). Conclusion: Curcumin inhibits SIRT6 expression via upregulating miR-33b-5p expression, which leads to the inhibition of OS cell migration and invasion. Thus, curcumin is a potential therapeutic agent for the management of OS.

研究领域: 肿瘤学 · 分子生物学 · 药理学
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TECHNOLOGY IN CANCER RESEARCH & TREATMENT · 2020 · IF 2.074

LncRNA HOTAIR Influences the Growth, Migration, and Invasion of Papillary Thyroid Carcinoma via Affection on the miR-488-5p/NUP205 Axis

Feng Xia,Wei Xia,Xudong Yu

Objective:The study was aim to investigate the effect of HOX transcript antisense RNA (HOTAIR) on the growth, migration, and invasion of papillary thyroid carcinoma (PTC) and its underlying mechanisms.Methods:Cell growth, invasion, and migration was respectively investigated using the MTT assay, trans-well assay, and wound healing assay. The expression of genes and proteins was respectively determined by Western blot analysis and RT-PCR experiments.Results:It was demonstrated that high expression of HOTAIR in PTC cells (BCPAP) and tissues resulted in fast tumor growth and poor survival time of the PTC-bearing mice models. Moreover, overexpression of HOTAIR leaded to markedly enhanced proliferation, migration, and invasion of BCPAP cells. Increase the levels of HOTAIR in BCPAP cells signally down-regulated the miR-488-5p levels which was able of inhibiting the growth rate, increasing the apoptosis rate, and decreasing the invasion/migration ability of BCPAP cells. Further studies indicated that HOTAIR promoted BCPAP cell growth, invasion, and migration mainly through regulating the miR-488-5p/NUP205 axis and the levels of Bcl-2 as well.Conclusion:HOTAIR promoted the growth, migration, and invasion of papillary thyroid carcinoma mainly through regulating the miR-488-5p/NUP205 axis.

研究领域: 肿瘤学 · 分子生物学 · 遗传学
✓ 已验证 DOI PubMed 高影响因子
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DNA AND CELL BIOLOGY · 2022 ·Vol. 41 ·期 4 ·424-436 · IF 3.55

LINC00982 Inhibits the Proliferation, Migration, and Invasion of Breast Cancer Cells Through the miR-765/DPF3 Axis

Feng Chi,Fang Qiu,Xiaoming Jin,Long Chen,Guijin He,Sijia Han

Breast cancer (BC) is one of the most frequently occurring malignant tumors in female adults. The long intergenic nonprotein coding RNA 00982 (LINC00982) has been regarded as a cancer suppressor in several human cancers. However, the function and the underlying mechanisms of LINC00982 have not been studied in BC. The present study found that LINC00982 was significantly downregulated in BC tumor tissues, and the low LINC00982 level predicts a poor prognosis of BC. Through the overexpression and suppression of LINC00982 in two BC cell lines, we found that LINC00982 could inhibit cell proliferation, migration, and invasion by suppressing the activity of the signal transducer and activator of transcription 3 (STAT3)/nuclear factor kappa B (NF-κB) signal pathway. Furthermore, luciferase reporter assay has been used to verify that LINC00982 functions as a molecular sponge for miR-765, which could target DPF3. The relative expression of miR-765 decreased with LINC00982 overexpressing, and DPF3 increased at the same time.In addition, the suppression of cell malignant phenotype caused by overexpression of LINC00982 can be reversed by inhibition of DPF3. To verify the function of LINC00982 in vivo, the BC cells were implanted in nude mice and the results suggested the tumor growth and malignant phenotype were suppressed by LINC00982. In this study, we prove that LINC00982 regulates the growth and development of BC through STAT3/NF-κB signal pathway, mediated by the miR-765/DPF3 axis. LINC00982 may function as a target molecule to take part in the prognosis and therapy of BC.

CAS / MDL: 47165-04-8
研究领域: 肿瘤学 · 分子生物学 · 癌症研究
✓ 已验证 产品关联 DOI PubMed 高影响因子
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GENOMICS · 2023 · IF 4.4

Hsa_circ_0002019 promotes cell proliferation, migration, and invasion by regulating TNFAIP6/NF-κB signaling in gastric cancer

Dan Chen,Li Shi,Dingfu Zhong,Ying Nie,Yi Yang,Dong Liu

Background Gastric cancer (GC) is a common cancer with a high incidence and mortality rate. Herein, the role of hsa_circ_0002019 (circ_0002019) in GC was investigated. Methods The molecular structure and stability of circ_0002019 were identified by RNase R, and Actinomycin D treatment. Molecular associations were verified by RIP. Proliferation, migration, and invasion were detected by CCK-8, EdU, and Transwell, respectively. The effect of circ_0002019 on tumor growth was analyzed in vivo. Results Circ_0002019 was elevated in GC tissues and cells. Circ_0002019 knockdown inhibited the proliferation, migration, and invasion. Mechanically, circ_0002019 activated NF-κB signaling by increasing TNFAIP6 mRNA stability by PTBP1. Activation of NF-κB signaling limited the antitumor effect of circ_0002019 silencing in GC. Circ_0002019 knockdown inhibited tumor growth in vivo by reducing TNFAIP6 expression. Conclusions Circ_0002019 accelerated the proliferation, migration, and invasion by regulating TNFAIP6/NF-κB pathway, suggesting circ_0002019 could be a key regulatory factor in GC progression.

CAS / MDL: 9012-76-4 9005-38-3
研究领域: 肿瘤学 · 分子生物学 · 癌症遗传学
✓ 已验证 产品关联 DOI PubMed 高影响因子
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Journal of Cancer · 2024 ·Vol. 15 ·期 17 ·5810-5827 · IF 3.3

Daphnoretin inhibits glioblastoma cell proliferation and metastasis via PI3K/AKT signaling pathway inactivation

Lei Jiaming,Zhou Hong,Cheng Shijiao,Yu Wenwen,Yang Meiting,Lin Li

Glioblastoma (GBM) was the most malignant intracranial tumor with high mortality rates and invariably poor prognosis due to its limited clinical treatments. The urgent need to develop new therapeutic drugs for GBM treatment is evident. As a coumarin derivative, daphnoretin's favorable pharmacological activities have been widely documented. However, the potential inhibitory effects of daphnoretin on GBM have not been explored. In this study, we aimed to investigate the effects of daphnoretin on GBM and elucidate its anti-GBM mechanisms for the first time. It was observed that daphnoretin inhibited GBM cell proliferation, migration, and invasion in vitro and suppressed tumor growth without significant drug toxicity in GBM xenograft tumor models in vivo. Mechanistically, daphnoretin was predicted to target the PI3K/AKT signaling pathway through network pharmacology and molecular docking analysis. Subsequently, it was further verified by Biacore assay for surface plasmon resonance (SPR) experiments. Experimentally, daphnoretin induced apoptosis in GBM cells via the PI3K/AKT signaling pathway. Moreover, the effects of daphnoretin on GBM cells could be reversed by the AKT activator SC79. These results suggest that daphnoretin holds potential as a therapeutic drug against GBM and provides new insights into GBM treatment.Keywords: daphnoretin, glioblastoma, PI3K/AKT, apoptosis, proliferation Glioblastoma (GBM) is the most common and malignant primary brain tumor in adults. Despite aggressive management involving maximal safe surgical resection followed by external beam radiation therapy with concomitant and adjuvant temozolomide (TMZ), approximately 90% of WHO grade IV gliomas (GBM) recur locally within 2 years [1, 2]. Currently, no standard of care exists for patients with recurrent GBM, despite available post-neurosurgical treatment options such as temozolomide, radiotherapy, and some targeted drugs. Consequently, the prognosis for GBM patients remains bleak [3]. Thus, exploring potential drugs for clinical treatment is urgently needed.In recent years, with the rapid development of natural medicine, traditional Chinese medicine monomers have garnered increasing attention due to their potent antitumor effects [4]. Daphnoretin, a primary active ingredient of Daphne giraldii Nitsche, exhibits various pharmacological effects, including antitumor, antioxidative, and anti-inflammatory properties [5]. Daphnetin, chemically known as 7-hydroxyl-6-methoxy-3,7'-dicoumarylether, with molecular formula of C19H12O7 and molecular weight of 352.29. Daphnetin has shown a broad application prospect in the field of medicine due to its unique biochemical and molecular properties [6]. Daphnoretin has attracted significant interest due to these unique pharmacological effects. Studies have demonstrated its substantial antitumor activity across various cancers, including inhibition of proliferation, induction of apoptosis, and cell cycle arrest [7-9]. However, research on the therapeutic effects and mechanisms of daphnoretin in GBM remains limited. As a coumarin derivative, daphnoretin possesses diverse pharmacological activities, yet its potential inhibitory effect on GBM has not been thoroughly investigated. Our findings suggest that daphnoretin may offer a promising therapeutic option for GBM patients.In the present study, we extensively investigated daphnoretin's effects on GBM. Daphnoretin exhibits pharmacological activities that inhibit GBM cell proliferation, colony formation, migration, and invasion in vitro, and suppresses tumor growth with no significant adverse effects in vivo.In summary, this study systematically evaluates the potential of daphnoretin in GBM treatment and explores its anti-tumor mechanism. We aim to identify new drug candidates and treatment strategies for GBM, ultimately improving therapeutic outcomes and enhancing patients' quality of life.Daphnoretin (CAS: 2034-67-9) and Temozolomide (TMZ) (CAS: 85622-93-1) were purchased from Chinese Shanghai Yuanye Bio-Technology Co., Ltd and Chinese Shanghai Aladdin Biochemical Technology Co., Ltd, respectively. AKT agonist SC79 (CAS: 305834-79-1) was obtained from MedChemExpress Co., Ltd. All chemicals were diluted with dimethyl sulfoxide (DMSO) (CAS: 67-68-5; Sigma-Aldrich Corp., Darmstadt, Germany), unless otherwise specified. Human GBM cell lines U87 and U251, and human brain glial cell line (normal) HEB were procured from Procell Life Science & Technology Co., Ltd (Wuhan, Hubei, China). U87, U251, and HEB cells were cultured in high-glucose Dulbecco's modified Eagle's medium (DMEM) (Gibco, Waltham, MA, USA), supplemented with 10% fetal bovine serum (FBS) (Gibco, Waltham, MA, USA) and 1% penicillin-streptomycin (Gibco, Waltham, MA, USA). All cells were maintained in a 5% CO2 humidified incubator at 37°C under 95% air.Cell viability was assessed using the MTT assay to determine the half maximal inhibitory concentration (IC50) values. U87, U251, and HEB cells (9 × 104) were seeded into 96-well plates (Costar, Corning, NY, USA) and cultured for 24 and 48 hours in the incubator. Cells were treated with inhibitors or various concentrations of daphnoretin. Subsequently, 10 μL of MTT solution was added to each well, followed by a 4-hour incubation period. After incubation, 100 μL of DMSO was added to dissolve the formazan crystals. The plates were vortexed for 10 minutes at room temperature, and absorbance was measured at 450 nm using the Bio-Tek ELx800 Multi-Mode Reader (BioTek Instruments, Inc., Winooski, VT, USA).U87 and U251 cells were seeded at 1,000 cells per well in 6-well culture plates (Costar, Corning, NY, USA) and treated with DMSO or daphnoretin (10 and 20 μM) for 7-14 days. Cells were fixed with 4% paraformaldehyde for 15 minutes and stained with 0.5% crystal violet solution for another 15 minutes. Colonies (>100 cells/colony) were manually counted.GBM cell proliferation was assessed using the Cell-Light EdU kit (C0071S, Beyotime, Shanghai, China). U87 and U251 cells (5 × 103) were seeded in 24-well plates (Costar, Corning, NY, USA) for the EdU assay. Cells were treated with daphnoretin at concentrations of 0, 10, 20, and 40 μM. EdU reagent (10 μM) was added to cells during DNA synthesis for 2 hours. After fixation with 4% formaldehyde and permeabilization with 0.5% Triton X-100, cell nuclei were stained with Hoechst 33342. Images were captured using an X71 fluorescence microscope (200× magnification; Olympus Corporation, Tokyo, Japan) in five randomly selected fields.U87 and U251 cells in the logarithmic growth phase were detached, resuspended, and 3 × 105 cells were seeded per well in 6-well plates (Costar, Corning, NY, USA). When cells reached 95% confluence, a 200 μL pipette tip was used to create scratches. After washing twice with PBS, cells were treated with daphnoretin solutions at different concentrations. Images were taken at various time points. After 24 hours, cells were fixed with 4% paraformaldehyde, washed with PBS, and photographed.Cells (5 × 104) in 200 μL serum-free medium were seeded into the upper chamber of a 24-well Transwell insert (Costar, Corning, NY, USA). The lower chamber was filled with 600 μL of DMEM supplemented with 10% FBS and the indicated concentrations of daphnoretin. For invasion assays, Matrigel (1:8 dilution; Corning BioCoat, #356234, NY, USA) was applied to the bottom of the Transwell insert before cell seeding. After 24 hours of incubation, cells that migrated or invaded through the membrane were fixed with 4% paraformaldehyde (Solarbio, Beijing, China) for 20 minutes and stained with 1% crystal violet for another 20 minutes. Stained cells were counted under an X71 fluorescence microscope (Olympus Corporation, Tokyo, Japan).Intracellular ROS levels were assessed using 2',7′-dichlorofluorescin diacetate (DCFDA; Sigma-Aldrich) to measure its fluorescent oxidized product, dichlorofluorescein (DCF). U251 and U87 cells (2.5 × 104) were seeded in 24-well plates (Costar, Corning, NY, USA) and pretreated with 3 μM N-acetyl-L-cysteine (Sigma-Aldrich) or vehicle for 6 hours. Following cotreatment with daphnoretin for 18 hours, cells were incubated with 2 μM DCFDA in fresh complete medium for 60 minutes at 37°C in the dark. DCF fluorescence intensity was measured using an Olympus Fluorescence Microscope. Additionally, cells were stained with the JC-1 probe (Biosharp, Shanghai, China) for 30 minutes at 37°C in the dark, washed with pre-cold PBS, and suspended in 500 µL PBS. The percentage of apoptotic cells was evaluated using the X71 fluorescence microscope (Olympus Corporation, Tokyo, Japan).U251 and U87 cells (2.5 × 104) were treated with various concentrations of daphnoretin for 24 hours in 24-well plates (Costar, Corning, NY, USA). Cells were harvested, centrifuged, and resuspended in PBS. After re-suspending in binding buffer, cells were stained using the Annexin V-FITC/PI kit (C1067M, Beyotime, Shanghai, China) for 20 minutes at 37°C. The percentage of apoptotic cells was determined using an X71 fluorescence microscope (Olympus Corporation, Tokyo, Japan).Following daphnoretin treatment, cells were collected and washed three times with ice-cold PBS. Cell lysis was performed using RIPA buffer (Beyotime Biotechnology Co., Ltd., Shanghai, China) supplemented with protease and phosphatase inhibitors for 30 minutes. After centrifugation, supernatants containing total cellular proteins were collected. Protein concentration was determined using a BCA assay kit. Samples were denatured with loading buffer at 100°C for 10 minutes and separated by 8%-12% SDS-PAGE. Proteins were then transferred onto PVDF membranes, which were subsequently blocked. After blocking, membranes were incubated overnight at 4°C with specific primary antibodies. Following primary antibody incubation, membranes were probed with HRP-conjugated secondary antibodies, and protein expression was visualized using ECL plus reagents (Beyotime Biotechnology Co., Ltd.). GAPDH was used as a loading control. Antibodies used were: Bcl-2 (1:1000, R23309), Bax (1:1000, R22708), Caspase 3 (1:1000, R23315), Cleaved-caspase 3 (1:1000, 341034), p-AKT (1:1000, 381555), AKT (1:1000, 342529), p-PI3K (1:1000, 301245), PI3K (1:1000, 343830), Caspase 9 (1:1000, 381336), Cleaved-caspase 9 (1:1000, 381238), and GAPDH (1:1000, 380626) (Zhengneng Biotechnology Co., Ltd., Chengdu, China).All animal experiments conducted in this study were approved by the Animal Ethics Committee of Hubei University of Science and Technology and were performed in accordance with institutional and international guidelines for animal care and use. GL261 cells were used to establish the GBM mouse xenograft model. Five-week-old male C57BL/6 mice weighing approximately [insert weight range] were subcutaneously injected with GL261 cells (5 × 106 cells in 100 μL sterile PBS) on the back of each mouse. Once tumors reached an average volume of approximately 100 mm^3, mice were randomly assigned to the following groups: Control, TMZ group, low-dose daphnoretin group (Daphnoretin-L), and high-dose daphnoretin group (Daphnoretin-H). Tumor volumes were measured every 2 days using the formula: volume = a × b2 × 0.52 (where a is length and b is width in mm), and body weights were recorded daily. After 14 days, mice were euthanized, and xenograft samples from all groups were collected for further analysis.Dehydrated tissues fixed in 4% paraformaldehyde were paraffin-embedded and sectioned into 4 μm slices. Tissue blocks were deparaffinized, rehydrated, and stained with HE (BL700A, Biosharp, Shanghai, China). The stained sections were mounted on coverslips and viewed under a microscope. For immunohistochemical staining, tissue sections were deparaffinized, rehydrated, and treated with 3% hydrogen peroxide to quench endogenous peroxidase activity. Antigen retrieval was performed in citrate buffer (pH 6.0). Sections were then blocked and permeabilized with 0.1% Triton X-100 and incubated overnight at 4°C with primary antibodies against CD31 (1:100, #3528, Cell Signaling Technology, MA, USA), Ki-67 (1:100, AF1738, Beyotime, Shanghai, China), PCNA (1:100, #13110, Cell Signaling Technology, MA, USA), p-AKT (1:100, 381555), AKT (1:100, 342529), p-PI3K (1:100, 301245), and PI3K (1:100, 343830) (Zhengneng Biotechnology Co., Ltd., Chengdu, China). After washing, sections were incubated with an HRP-conjugated secondary antibody for 1 hour at room temperature. Antibody binding was visualized using diaminobenzidine (DAB P0202, Beyotime, Shanghai, China) substrate, and sections were counterstained with hematoxylin (BL700A, Biosharp, Shanghai, China).The molecular structure of daphnoretin was obtained from PubChem (https://pubchem.ncbi.nlm.nih.gov/) in Simplified Molecular-Input Line-Entry System (SMILES) format. The SwissTargetPrediction database (www.swisstargetprediction.ch/) was utilized to predict potential targets of daphnoretin for Homo sapiens based on its chemical structure. Disease-related targets associated with glioblastoma (GBM) were retrieved from the GeneCards database (https://www.GeneCards.org/) using the keyword "glioblastoma". Predicted protein targets of daphnoretin against GBM were filtered and analyzed using Venny 2.1.0 (https://bioinfogp.cnb.csic.es/tools/venny/). Functional and pathway enrichment analyses of the overlapping daphnoretin-GBM targets were performed using R (v.3.6.3) software, incorporating Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) annotations. A protein-protein interaction (PPI) network of the identified targets was constructed using STRING (https://string-db.org/) and visualized with Cytoscape v3.8.0 software.The compound name, molecular weight, and 3D structure of daphnoretin were obtained from the PubChem database, and the 3D structure was further downloaded from the RCSB Protein Data Bank (http://www.rcsb.org/). AutoDock software was used to prepare the ligands and proteins required for molecular docking. For each target protein, the crystal structure was processed to remove water molecules, hydrogenate, optimize amino acids, adjust energy parameters, and generate low-energy conformations of the ligand structure. Docking simulations were performed between daphnoretin and the selected target proteins, and the Binding Energy (kcal/mol) values were calculated to assess binding affinities. Lower binding energies indicate more stable interactions between the ligand and receptor. The results of molecular docking were analyzed using Discovery Studio software to visualize and interpret the binding modes, and the best docking poses based on binding energies were selected for further analysis.To validate the direct interaction between daphnoretin and AKT1, the Biacore T200 instrument (GE Healthcare) was utilized. Following expression, soluble protein was obtained through sonication and centrifugation, and subsequently incubated with anti-His beads to isolate the fusion protein. The protein was further concentrated using an ultrafiltration centrifuge tube, and its concentration was determined. For SPR analysis, a CM5 sensor chip was utilized. His-tagged AKT1 was immobilized via His antibody in parallel-flow channels of the CM5 sensor chip. Daphnoretin was injected at various concentrations into the flow system to assess its interaction with AKT1. Experiments were conducted in PBS buffer, and a dissociation time of 600 seconds was allowed. To correct for solvent effects, PBS with 5% DMSO was used.Data are presented as mean ± SD. Statistical significance between control and experimental groups was assessed using paired Student's t-tests. A p-value < 0.05 was considered statistically significant.The chemical structure of daphnoretin, identified by the CAS number 85622-93-1, with a molecular formula of C19H12O7 and a molecular weight of 352.3 Da, was depicted in Fig. 1A. The proliferation of HEB, U87 and U251 cells was assessed using the MTT assay across different concentrations (0, 10, 20, 40, 80, 100 μM) of daphnoretin, as depicted in Fig. 1B, C amd D. Microscopic examination after 24 h revealed a concentration-dependent inhibition of GBM cell proliferation by daphnoretin.Furthermore, colony formation assays were conducted to evaluate the long-term inhibitory effects of daphnoretin on GBM cell proliferation. The results demonstrated a significant dose-dependent reduction in colony numbers in both U87 and U251 cells.To further validate the anti-proliferative capacity of daphnoretin, DNA synthesis was quantified using the EdU incorporation assay. Compared to the control group, daphnoretin-treated U87 and U251 cells exhibited a marked decrease in EdU-positive cells (Fig. 2B), indicating that daphnoretin effectively inhibits GBM cell proliferation.Collectively, these findings underscore the potent anti-tumor effects of daphnoretin on GBM cells by impeding proliferation through multiple assays. Daphnoretin inhibits the viability of GBM cells. (A) Medical material morphology, chemical structure, molecular formula and weight of daphnoretin. (B) Daphnoretin at different concentrations (0, 10, 20, 40, 80, 160 µM) treated HEB cells for 24 and 48 h. (C) Daphnoretin at different concentrations (0, 10, 20, 40, 80, 160 µM) treated HEB cells for 24 and 48 h. (D) Daphnoretin at different concentrations (0, 10, 20, 40, 80, 160 µM) treated HEB cells for 24 and 48 h. Scale bar = 50 µm. Data were presented as mean ± SD or as a representative image of triplicate experiments, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 by one-way ANOVA with Tukey's post-hoc test.The lateral migration ability of GBM cells was evaluated using a wound healing assay, as depicted in Fig. 2A. Following 24 hours of treatment with varying concentrations of daphnoretin, both U87 and U251 cells exhibited a significant dose-dependent decrease in migration ability. Compared to the control group, the gap distance widened progressively with increasing daphnoretin concentration, indicating effective inhibition of lateral migration by daphnoretin.Additionally, migration and invasion capabilities of U87 and U251 cells were assessed using Transwell assays (Fig. 2B). After 24 hours of treatment, daphnoretin-treated cells showed marked reductions in both migration and invasion compared to untreated cells. These effects were dose-dependent, further demonstrating daphnoretin's ability to inhibit the migration and invasion of GBM cells.DCFH-DA staining was employed to assess the impact of daphnoretin on cellular ROS generation (Fig. 4A). Quantification of fluorescent images revealed a significant increase in ROS levels in cells treated with daphnoretin, indicating heightened oxidative stress.The effect of daphnoretin on apoptosis in GBM cells was assessed using the mitochondrial membrane potential detection kit (JC-1), with results depicted in Fig. 4B. Carbonyl cyanide 3-chlorophenylhydrazone (CCCP), an apoptosis inducer that uncouples mitochondrial oxidative phosphorylation, served as a positive control to demonstrate mitochondrial membrane potential reduction. Increasing concentrations of daphnoretin resulted in an increase in the JC-1 monomer (green fluorescence) and a decrease in the JC-1 aggregate (red fluorescence), indicating an early apoptotic phenotype. These findings confirm that daphnoretin induces apoptosis in GBM cells.To elucidate the specific cell death mechanism induced by daphnoretin in GBM, Annexin V-FITC/PI staining was performed and observed under fluorescence microscopy (Fig. 5A). The proportion of apoptotic cells increased significantly with rising concentrations of daphnoretin.Furthermore, the effect of daphnoretin on the expression levels of apoptosis-related proteins in U87 and U251 cells was examined using western blotting (Fig. 5B). After 24 hours of treatment, daphnoretin dose-dependently down-regulated Bcl-2 expression while up-regulating Bax expression. Moreover, there was a notable increase in the levels of Cleaved-caspase 9 and Cleaved-caspase 3, further supporting daphnoretin's induction of apoptosis in GBM cells.To further confirm the inhibitory effect of daphnoretin on GBM in vivo, we administered daphnoretin in mouse xenograft models, with TMZ used as a positive control group. Results demonstrated that both low (Daphnoretin-L, 20 mg/kg) and high (Daphnoretin-H, 40 mg/kg) doses of daphnoretin significantly reduced tumor size, volume, and weight compared to the control group, as shown in Fig. 6A, B, and C, highlighting daphnoretin's promising anti-GBM efficacy in vivo. Assessing drug toxicity is crucial for effective drug development. Daphnoretin-treated mice exhibited no significant differences in liver morphology or liver/body ratio compared to the control group, as depicted in Fig. 6E and F. Furthermore, histological analysis of vital organs including the heart, liver, spleen, lung, and kidney revealed no notable abnormalities upon daphnoretin treatment (Fig. 6G, HE staining), indicating favorable biosafety of daphnoretin in vivo.The mechanism of daphnoretin's inhibition of GBM cell proliferation was initially explored using network pharmacology. Four hundred ninety-two potential targets of daphnoretin were identified through GeneCards and SwissTargetPrediction databases, while 8,554 targets associated with GBM were predicted from comprehensive analyses of GeneCards and TCGA databases. A Venn diagram depicting the overlap between daphnoretin and GBM targets revealed 272 shared targets, suggesting potential targets for daphnoretin treatment against GBM (Fig. 7A). Protein-protein interaction (PPI) analysis identified AKT1, VEGFR, HSP90AA1, BCL2, and SRC as hub genes potentially pivotal in the treatment of GBM (Fig. 7B). GO enrichment analysis of biological processes (BP), cellular components (CC), and molecular functions (MF) among common drug-disease targets, along with top ten disease targets, conducted via Cytoscape 3.8.0, indicated that intracellular redox states, such as phosphorylation and protein phosphorylation, played critical roles in GBM under daphnoretin treatment (Fig. 7C). KEGG pathway analysis highlighted the PI3K-AKT signaling pathway as central to daphnoretin's effects against GBM (Fig. 7D). Daphnoretin inhibits proliferation of GBM cells in dose-dependent manner. (A) Clone formation assay using U87, U251 cells. (B) The cell proliferation of U87and U251 cells with indicated daphnoretin treatment were subjected to EdU assay. Scale bar = 100 µm. Data were presented as mean ± SD or as a representative image of triplicate experiments, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 by one-way ANOVA with Tukey's post-hoc test. Daphnoretin inhibits migration and invasion of GBM cells in dose-dependent manner. (A) Measurement of wound healing in U87 and U251 cells exposed to daphnoretin. Scale bar = 50 µm. (B) The vertical migration and invasion of U87 and U251 cells after daphnoretin treatment was measured by Transwell assay. Scale bar =200 µm. Data were presented as mean ± SD or as a representative image of triplicate experiments, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 by one-way ANOVA with Tukey's post-hoc test. Effects of daphnoretin on GBM cells ROS level and apoptosis. (A) The ROS level was detected after U87 and U251 cells were treated with different concentrations of daphnoretin. Scale bar = 200 μm. (B) Fluorescence microscopy was used to detect changes in the mitochondrial membrane potential of U87 and U251 cells treated with daphnoretin for 24 h. Scale bar = 200 µm. Data were presented as mean ± SD or as a representative image of triplicate experiments, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 by one-way ANOVA with Tukey's post-hoc test.Additionally, molecular docking of five key target structures with daphnoretin revealed binding energies (kcal/mol) that demonstrated stable ligand-receptor interactions, with lower values indicating stronger binding (Fig. 7E). To validate the above hypothesis, the interaction between daphnoretin and AKT was first evaluated using SPR analysis, and daphnoretin was injected over immobilized recombinant human AKT on a chip surface to determine the kinetics of the binding reaction. Visualization of molecular docking analysis between daphnoretin and the PI3K/AKT pathway (Fig. 7G) underscored a robust binding affinity, suggesting daphnoretin's potential to target PI3K/AKT-related pathways involved in cell apoptosis and GBM attenuation, as indicated by network pharmacology and docking analyses. Daphnoretin triggered mitochondria-dependent apoptosis in GBM cells. (A) U87 and U251 cells were treated with the specified dose of daphnoretin for 24 h, stained with Annexin V-FITC/PI, and detected by fluorescence microscopy. Scale bar = 200 µm. (B) Western blot of Bcl-2, Bax, Caspase 9, Cleaved-caspase 9, Caspase 3 and Cleaved-caspase 3 in U87 and U251 cells treated with daphnoretin. Data were presented as mean ± SD or as a representative image of triplicate experiments, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 by one-way ANOVA with Tukey's post-hoc test. Daphnoretin suppresses the tumor growth of GBM subcutaneous xenograft in vivo. (A) Images of subcutaneous xenograft tumors in 4 groups (Control group, TMZ group, Daphnoretin-L group and Daphnoretin-H group). (B) Statistical graph of tumor weights in mice during treatment days. (C) Statistical graph of body weight in mice during treatment days. (D) Statistical graph of tumor volumes in mice during treatment days. (E) Liver images of the TMZ-treated and vary concentration of daphnoretin-treated xenograft mice. (F) Liver/body ratio of the TMZ-treated and vary concentration of daphnoretin-treated xenograft mice. (H) HE staining of heart, liver, spleen, lung and kidney of the TMZ-treated and vary concentration of daphnoretin-treated xenograft mice. Data were presented as mean ± SD or as a representative image, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 vs. the control group by oneway ANOVA with Tukey's post-hoc test or two-way RM ANOVA with Sidak's multiple comparisons test. Effects of daphnoretin on AKT based on network pharmacology and molecular docking analysis. (A) The overlapped daphnoretin-GBM targets were screened out by Venny 2.1.0. (B) The PPI network of the Daphnoretin-GBM targets were conducted by STRING database. (C) The GO functional enrichments of overlapped Daphnoretin-GBM targets were analyzed by R (v.3.6.3) software. (D) The KEGG pathway enrichments of overlapped Daphnoretin-GBM targets were performed by R (v.3.6.3) software. (E) The binding energy with PDB id of 5 combining conformations. The smaller of the binding energy value, the higher the accuracy. (F) Molecular docking results of daphnoretin with AKT1 was obtained by Autodock-VINA and Pymol software. (G) Different concentrations of daphnoretin associated with AKT as measured by SPR analysis. Data were presented as mean ± SD or as a representative image, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 vs. the control group by oneway ANOVA with Tukey's post-hoc test or two-way RM ANOVA with Sidak's multiple comparisons test.Based on the pivotal regulatory role of PI3K/AKT signaling molecules in cell proliferation, we assessed the levels of these molecules in daphnoretin-treated GBM cells. Our findings revealed significant downregulation of p-PI3K and p-AKT levels in U87 cells following daphnoretin treatment, suggesting daphnoretin's ability to modulate U87 cell proliferation via the PI3K/AKT pathway. Similarly, decreased levels of p-PI3K and p-AKT were observed in daphnoretin-treated U251 cells (Fig. 8A).To further investigate the role of the PI3K/AKT pathway, we conducted rescue experiments using SC79, an AKT agonist. Pretreatment with SC79 for 1 hour abolished the effects of daphnoretin (20 μM) on cell proliferation, apoptosis, and PI3K/AKT signaling in GBM cells (Fig. 8B). These results underscore the essential role of the PI3K/AKT signaling cascade in mediating daphnoretin's anti-tumor effects in GBM cells.Additionally, IHC analysis was performed to assess cell proliferation (Ki-67 and PCNA), apoptosis (p-PI3K, PI3K, p-AKT, AKT), and tumor angiogenesis (CD31). Figure 9 demonstrates a significant decrease in Ki-67, PCNA, and CD31 expression levels, accompanied by an increase in p-PI3K and p-AKT expression levels with increasing doses of daphnoretin. These findings indicate that daphnoretin promotes apoptosis, inhibits cell proliferation, and suppresses tumor angiogenesis in vivo.GBM stands out as one of the most aggressive and lethal malignant tumors affecting the central nervous system. The treatment of GBM has long posed a significant challenge in neuro-oncology [10, 11]. Despite advancements in comprehensive treatment modalities such as surgery, radiotherapy, and chemotherapy in recent years, the prognosis for GBM patients remains poor, with an extremely low 5-year survival rate [12]. Therefore, identifying new therapeutic targets and drugs to enhance the efficacy of GBM treatment is of paramount importance.Daphnoretin has demonstrated antitumor activity against various cancer cell lines including colon cancer HCT116 cells, cervical cancer HeLa cells, oral epidermoid carcinoma KB cells, lung cancer A549 cells, and NCI-H187 cells [13-16]. In our study, we observed that daphnoretin significantly inhibits proliferation, migration, and invasion while inducing apoptosis in GBM cells, effects that are closely associated with the PI3K/AKT pathway.Apoptosis represents a critical and multistep biological process essential for maintaining cellular homeostasis [17, 18]. Key regulators of apoptosis include the pro-apoptotic Bax family proteins and the antiapoptotic Bcl-2 family molecules. The balance between Bcl-2 and Bax levels serves as a crucial indicator of cancer cell apoptosis induced by chemotherapy and radiation [18]. Disruption of this balance alters mitochondrial membrane permeability (MMP), leading to cytochrome C release into the cytoplasm and subsequent upregulation of Cleaved-caspase 9 and Cleaved-caspase 3 levels [20-22]. In our study, daphnoretin significantly increased apoptotic rates in GBM cells. We observed downregulation of Bcl-2 levels and upregulation of Bax, Cleaved-caspase 9, and Cleaved-caspase 3 levels in both daphnoretin-treated U87 and U251 cells. These findings suggest that daphnoretin induces cell apoptosis through the mitochondrial apoptotic pathway in GBM. Daphnoretin triggers programmed cell death in cancer cells through the activation of the intrinsic apoptotic pathway. It upregulates pro-apoptotic factors such as Bax and downregulates anti-apoptotic proteins like Bcl-2, leading to mitochondrial dysfunction and activation of caspases. It impairs cell cycle progression by influencing cyclins and cyclin-dependent kinases, thereby halting cancer cell proliferation at various phases of the cell cycle [5, 6].Daphnoretin is known to exert potent anti-tumor effects through various signaling cascades, including MEK, PI3K/AKT, and NF-κB pathways [23]. In the field of anti-cancer, daphnoretin showed strong anti-tumor activity. Studies have shown that daphnetin can significantly inhibit the proliferation of a variety of tumor cells. Its anti-cancer mechanism mainly involves the regulation of key signaling pathways. For example, daphnoretin can play a tumor suppressor role by up-regulating the expression of p53 protein. p53 is an important tumor suppressor gene, which inhibits tumor growth by regulating cell cycle, promoting tumor cell senescence and apoptosis, inhibiting angiogenesis and tumor metastasis [24]. Further studies revealed that daphnetin may inhibit the differentiation of osteoclasts through the NF-κB pathway, thereby exerting anti-inflammatory effects. NF-κB is an important transcription factor, which is involved in the regulation of the expression of a variety of inflammation-related genes [25]. Daphnetin inhibits the activity of NF-κB by promoting the expression of IκB-α (NF-κB), thereby down-regulating the expression of transcription factors NFATc-1 and c-Fos closely related to osteoclast differentiation, and ultimately inhibiting osteoclast differentiation. Daphnoretin triggers PI3K/AKT-dependent apoptotic pathway in vitro. (A) U87 and U251 cells were treated with increasing doses of daphnoretin, and the proteins related to PI3K / AKT signaling pathway were analyzed by Western blot. (B) After pretreatment with SC79 for 1 h, the expression levels of PI3K, p-PI3K, AKT and p-AKT. Data were presented as mean ± SD or as a representative image, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001 vs. the control group by oneway ANOVA with Tukey's post-hoc test or two-way RM ANOVA with Sidak's multiple comparisons test. Daphnoretin suppresses the PI3K/AKT

CAS / MDL: 85622-93-1
研究领域: 肿瘤学 · 药理学 · 分子生物学 · 细胞生物学
✓ 已验证 产品关联 DOI PubMed 高影响因子
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Molecular Medicine Reports · 2022 ·Vol. 26 ·期 1 ·1-1 · IF 3.423

IGF2BP3‑stabilized SIX4 promotes the proliferation, migration, invasion and tube formation of ovarian cancer cells

Jinbiao Han,Xia Hu

The mortality rate of ovarian cancer (OC) is the highest among the different types of female reproductive system cancers. SIX homeobox 4 (SIX4), a member of the homeobox family, subfamily SIX, fulfills an important role in metastasis and angiogenesis in a variety of types of cancer. The aim of the present study was to investigate both the effects and the underlying mechanism of SIX4 on angiogenesis in OC. The Gene Expression Profiling Interactive Analysis and Encyclopedia of RNA Interactomes databases were employed to predict the expression levels of SIX4 in OC tissues, and its association with the overall survival (OS) rate of patients with OC. The expression levels of SIX4 in OC cell lines were detected by reverse transcription‑quantitative PCR (RT‑qPCR) and western blot analysis. Following silencing of SIX4, the proliferation, invasion, migration and angiogenesis of OC cells were investigated via Cell Counting Kit‑8, colony formation, wound healing, Transwell and tube formation assays. Subsequently, the levels of insulin‑like growth factor 2 mRNA binding protein 3 (IGF2BP3) in OC cell lines were detected by RT‑qPCR and western blot analysis. The ability of IGF2BP3 to bind to SIX4 mRNA was detected via an RNA immunoprecipitation assay, and the stability of SIX4 mRNA was assessed by RT‑qPCR following Actinomycin D treatment. Finally, the effects of transfection of sh‑SIX4 and overexpression of IGF2BP3 simultaneously were examined to further delineate the mechanism involved. It was revealed that SIX4 was highly expressed in OC tissues and cells, and its expression was associated with low OS rates in patients with OC. SIX4 knockdown with short hairpin RNA inhibited the proliferation, migration and invasion of cells, as well as angiogenesis. In addition, IGF2BP3 overexpression led to an improvement in the stability of SIX4 mRNA. Overexpression of IGF2BP3 also reversed the inhibitory effect of SIX4 interference on the malignant phenotypes of OC cells. Taken together, the results of the present study demonstrated that IGF2BP3‑stabilized SIX4 promoted the proliferation, metastasis and angiogenesis of SKOV3 cells.

CAS / MDL: 98-10-2
研究领域: 肿瘤学 · 分子生物学 · 细胞生物学
✓ 已验证 产品关联 DOI PubMed 高影响因子
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CELLULAR SIGNALLING · 2023 · IF 4.8

Aberrant expression of PELI1 caused by Jagged1 accelerates the malignant phenotype of pancreatic cancer

Wenyang Zhou,Yuying Hu,Baosheng Wang,Lina Yuan,Jia Ma,Xiangpeng Meng

Pancreatic cancer is one of the most aggressive cancers. PELI1 has been reported to promote cell survival and proliferation in multiple cancers. As of now, the role of PELI1 in pancreatic cancer is largely unknown. Here, we found that the PELI1 mRNA was higher expressed in pancreatic tumor tissues than in adjacent normal tissues, and the high PELI1 level in pancreatic cancer patients had a short survival time compared with the low level. Moreover, the results showed that PELI1 promoted cell proliferation, migration, and invasion, and inhibited apoptosis in vitro. Xenograft tumor experiments were used to determine the biological function of PELI1, and the results showed that PELI1 promoted tumor growth in vivo. Additionally, we found that Jagged1 activated PELI1 transcription in pancreatic cancer cells. To sum up, our results show that PELI1 affects the malignant phenotype of pancreatic cancer.

CAS / MDL: 30525-89-4
研究领域: 肿瘤学 · 分子生物学 · 癌症研究
✓ 已验证 产品关联 DOI PubMed 高影响因子
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iScience · 2024 · IF 4.6

The NF-κB/NUAK2 signaling axis regulates pancreatic cancer progression by targeting SMAD2/3

Ruobing Wang,Dan Su,Yueze Liu,Hua Huang,Jiangdong Qiu,Zhe Cao,Gang Yang,Hao Chen,Wenhao Luo,Jinxin Tao,Guihu Weng,Taiping Zhang

Summary Nuclear factor kappa B (NF-κB) plays a pivotal role in the development of pancreatic cancer, and its phosphorylation has previously been linked to the regulation of NUAK2. However, the regulatory connection between NF-κB and NUAK2, as well as NUAK2’s role in pancreatic cancer, remains unclear. In this study, we observed that inhibiting NUAK2 impeded the proliferation, migration, and invasion of pancreatic cancer cells while triggering apoptosis. NUAK2 overexpression partially resisted apoptosis and reversed the inhibitory effects of the NF-κB inhibitor. NF-κB transcriptionally regulated NUAK2 transcription by binding to the promoter region of NUAK2. Mechanistically, NUAK2 knockdown remarkably reduced the expression levels of p -SMAD2/3 and SMAD2/3, resulting in decreased nuclear translocation of SMAD4. In SMAD4-negative cells, NUAK2 knockdown impacted FAK signaling by downregulating SMAD2/3. Moreover, NUAK2 knockdown heightened the sensitivity of pancreatic cancer cells to gemcitabine, suggesting that NUAK2 inhibitors could be a promising strategy for pancreatic cancer treatment.

研究领域: 肿瘤学 · 分子生物学 · 细胞生物学
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Experimental and Therapeutic Medicine · 2019 ·Vol. 18 ·期 3 ·1793-1799 · IF 1.448

Cadmium induces A549 cell migration and invasion by activating ERK

Huijuan Zhai,Teng Pan,Haiyan Yang,Haiyu Wang,Yadong Wang

Cadmium (Cd) is an established carcinogen that is involved in the progression of lung cancer. However, the mechanisms underlying this Cd‑induced process have yet to be fully elucidated. The present study explored the potential roles of phosphorylated (p)‑ERK in the Cd‑induced migration and invasion of lung cancer cells. An MTT assay was performed to evaluate cell viability whilst western blot analysis and reverse transcription‑quantitative PCR were used to detect the expression of protein and mRNA, respectively. Migration and invasion assays were performed to assess cell migratory and invasive abilities. The results demonstrated that exposure to Cd increased the expression of p‑ERK in A549 cells. Cd also enhanced the migration and invasion of A549 cells, which could be blocked via U0126 treatment (an inhibitor of mitogen activated protein kinase). In addition, it was identified that Cd‑induced expression of matrix metalloproteinases 2 mRNA was mediated by p‑ERK. In conclusion, the present findings indicated that Cd induced A549 cell migration and invasion by activating ERK, and it was hypothesized that p‑ERK could serve as a target in the clinical treatment of Cd‑induced lung cancer.

CAS / MDL: 7790-78-5
研究领域: 肿瘤学 · 细胞生物学 · 分子生物学
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CELL CYCLE · 2022 · IF 5.173

CircCDR1 sponges miR-1290 to regulate cell proliferation, migration, invasion, and apoptosis in esophageal squamous cell cancer

Yong Fang,Jun Yin,Yaxing Shen,Hao Wang,Han Tang,Xiaosang Chen

Since circCDR1 was abnormally expressed in esophageal squamous cell cancer (ESCC), the current study explored whether circCDR1 affected ESCC. Detailedly, circCDR1 expression in ESCC and linear isoform and stability of circCDR1 were detected by RT-qPCR. The location of circCDR1 was detected by fluorescence in situ hybridization (FISH). After transfection, the cell biological functions were detected by wound-healing, CCK-8, colony formation, and flow cytometry assays. The target of circCDR1 was predicted by bioinformatics, FISH, RNA pull-down, and dual-luciferase reporter assays. The correlation between circCDR1 and miR-1290 was analyzed by Pearson’s correlation analysis. A subcutaneous-xenotransplant tumor model in BALB/c nude mice was established and the levels of circCDR1, miR-1290, and apoptosis/metastasis/proliferation-related factors in the cancer cells and tissues were detected by immunohistochemical analysis, western blot, or RT-qPCR. As a result, circCDR1 was low-expressed in ESCC tissues and cells, while miR-1290 was high-expressed. CircCDR1 was regulated and was negatively correlated with miR-1290. CircCDR1, located in cytoplasm, inhibited the viability, proliferation, migration, and invasion of the cancer cells and the expressions of Bcl-2, N-cadherin, and Vimentin, but enhanced cell apoptosis and the expressions of C caspase-3, Bax, E-cadherin, IGFBP4, LHX6 and NFIX. In vivo, circCDR1 promoted xenotransplanted tumor weight and volume, and the expressions of C caspase-3 and Bax yet suppressed the levels of Bcl-2, miR-1290, and Ki-67 in tumor tissues. The effects of circCDR1 on both cancer cells and tissues were opposite to and reversed by miR-1290 mimic. Collectively, circCDR1 sponged miR-1290 to regulate the progression of ESCC both in vitro and in vivo.

研究领域: 肿瘤学 · 分子生物学 · 细胞生物学
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