OncoTargets and Therapy

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ISSN / EISSN : 11786930 / 11786930
Current Publisher: Dove Medical Press Ltd. (10.2147)
Total articles ≅ 4,319
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Published: 19 February 2020
OncoTargets and Therapy; doi:10.2147/ott

Abstract:An international, peer-reviewed journal focusing on the pathological basis of all cancers, potential targets for therapy and treatment protocols employed to improve the management of cancer patients. In terms of therapy, palliative care is also included as part of the overall patient care process.
Yudi Ding, Nana Qi, Ke Wang, Yiming Huang, Jinling Liao, Hongxue Wang, Aihua Tan, Lihua Liu, Zhenqiang Zhang, Jinlong Li, et al.
Published: 18 February 2020
OncoTargets and Therapy, Volume 13, pp 1461-1470; doi:10.2147/ott.s231914

Abstract:FTO Facilitates Lung Adenocarcinoma Cell Progression by Activating Cell Migration Through mRNA Demethylation Yudi Ding,1,* Nana Qi,2,* Ke Wang,1,* Yiming Huang,2 Jinling Liao,1 Hongxue Wang,3 Aihua Tan,3 Lihua Liu,1 Zhenqiang Zhang,1 Jinlong Li,1 Jinliang Kong,1 Shouming Qin,1 Yonghua Jiang2,4,5 1Pulmonary and Critical Care Medicine, The First Affiliated Hospital of Guangxi Medical University, Nanning, Guangxi 530021, People’s Republic of China; 2Center for Genomic and Personalized Medicine, Guangxi Medical University, Nanning, Guangxi 530021, People’s Republic of China; 3Department of Chemotherapy, The Affiliated Tumor Hospital of Guangxi Medical University, Nanning, Guangxi 530021, People’s Republic of China; 4Guangxi Key Laboratory of Genomic and Personalized Medicine, Nanning, Guangxi 530021, People’s Republic of China; 5Guangxi Collaborative Innovation Center for Genomic and Personalized Medicine, Nanning, Guangxi 530021, People’s Republic of China*These authors contributed equally to this workCorrespondence: Yonghua Jiang; Shouming Qin Tel +86 13978695898; +86 18275710900Email [email protected]; [email protected]: The fat mass and obesity-associated protein (FTO) was identified as a critical demethylase involved in regulating cellular mRNA stability by removing N6-methyladenosine (m6A) residues from mRNA. Emerging evidence has revealed that FTO is deeply implicated in lung cancer. However, knowledge of the function of FTO in lung adenocarcinoma (LUAC) is limited.Methods: FTO and FTO R96Q (R96Q), an FTO missense mutant lacking demethylase activity, were ectopically overexpressed, and FTO was knocked down via siRNA in A549 and H1299 cells. The relationships between FTO with cell characteristics and mRNA m6A levels were explored. Furthermore, RNA sequencing was performed on A549 cells.Results: FTO overexpression enhanced the proliferation, migration, and invasion ability of A549 and H1299 cells, decreased mRNA m6A levels. Interestingly, overexpression of R96Q, blunted the effects of FTO overexpression on cell proliferation and invasion. Through RNA sequencing analysis of A549 cells overexpressing FTO or R96Q and control A594 cells, 45 genes were identified as affected by m6A mRNA demethylation. Most of these genes were related to lung cancer, such as laminin γ 2, thrombospondin 1, nerve growth factor inducible, integrin alpha11, and proprotein convertase subtilisin/kexin type 9. Gene ontology and Kyoto Encyclopedia of Genes and Genomes analyses suggested that these genes are fundamental to cancer development processes, such as cell migration and extracellular matrix organization.Conclusion: Our research shows that FTO facilitates LUAC cell progression by activating cell migration through m6A demethylation; however, further research on the mechanism underlying FTO activity in LUAC is necessary.Keywords: FTO, lung adenocarcinoma, m6A demethylase
Fei Luo, Zunyan Zhou, Jun Cai, Wei Du
Published: 18 February 2020
OncoTargets and Therapy, Volume 13, pp 1447-1460; doi:10.2147/ott.s230577

Abstract:DUB3 Facilitates Growth and Inhibits Apoptosis Through Enhancing Expression of EZH2 in Oral Squamous Cell Carcinoma
Xiong Guo, Yang Zhang, Ling Liu, Weiming Yang, Qi Zhang
Published: 18 February 2020
OncoTargets and Therapy, Volume 13, pp 1507-1518; doi:10.2147/ott.s231249

Abstract:HNF1A-AS1 Regulates Cell Migration, Invasion and Glycolysis via Modulating miR-124/MYO6 in Colorectal Cancer Cells
Shan Zhang, Weiwei Shi, Wei Hu, Ding Ma, Dongliang Yan, Kuanyong Yu, Guang Zhang, Yin Cao, Junhua Wu, Chunping Jiang, et al.
Published: 18 February 2020
OncoTargets and Therapy, Volume 13, pp 1481-1496; doi:10.2147/ott.s229055

Abstract:DEP Domain-Containing Protein 1B (DEPDC1B) Promotes Migration and Invasion in Pancreatic Cancer Through the Rac1/PAK1-LIMK1-Cofilin1 Signaling Pathway Shan Zhang,1,2,* Weiwei Shi,1,2,* Wei Hu,3,4,* Ding Ma,1,2 Dongliang Yan,4 Kuanyong Yu,4 Guang Zhang,1,2,4,4 Yin Cao,1,2,4,4 Junhua Wu,2 Chunping Jiang,1,2,4,4 Zhongxia Wang1,2,4,4 1Department of Hepatobiliary Surgery, The Affiliated Drum Tower Hospital of Nanjing University Medical School, Nanjing, Jiangsu 210008, People’s Republic of China; 2Jiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing University, Nanjing, Jiangsu 210093, People’s Republic of China; 3Department of Hepatobiliary Surgery, Lianyungang Clinical College of Nanjing Medical University, Lianyungang, Jiangsu 222001, People’s Republic of China; 4Department of Hepatobiliary Surgery, Drum Tower Clinical College of Nanjing Medical University, Nanjing, Jiangsu 210008, People’s Republic of China*These authors contributed equally to this workCorrespondence: Zhongxia Wang; Chunping Jiang 321 Zhongshan Road, Nanjing, Jiangsu 210008, People’s Republic of ChinaTel +86 15950451723; +86 13851818663Fax +86 25-83307115; +86 25-83307115Email [email protected]; [email protected]: With increasing incidence, pancreatic cancer (PC) is one of the most common digestive tract tumors. However, the prognosis of PC is particularly dismal due to the highly invasive and metastatic behavior of this deadly disease. DEP domain-containing protein 1B (DEPDC1B), which is overexpressed in multiple tumors, such as breast cancer, oral cancer and non-small cell lung cancer, plays a significant role in cell movement, cell cycle and cytoskeleton reorganization. However, the function of DEPDC1B in PC remains poorly understood.Methods: The function of DEPDC1B in the migration and invasion of PC was evaluated by wound healing and Transwell assays in vitro and PC-derived liver metastasis models in vivo. The molecular mechanisms of DEPDC1B were investigated through cell line establishment, Western blotting, qRT-PCR, immunoprecipitation, histological examination and immunohistochemistry analysis.Results: DEPDC1B was overexpressed in PC cell lines. DEPDC1B regulated cell migration and invasion. DEPDC1B regulated the Rac1/PAK1-LIMK1-cofilin1 signaling pathway by interacting with Rac1. Rac1 inhibition suppressed DEPDC1B-induced migration and invasion in PC in vitro and DEPDC1B-induced liver metastasis in vivo.Conclusion: DEPDC1B promoted cell migration and invasion by activating the Rac1/PAK1-LIMK1-cofilin1 signaling pathway, thus providing a potential therapeutic target against PC.Keywords: pancreatic cancer, DEP domain-containing protein 1B, migration, invasion, Rac1/PAK1-LIMK1-cofilin1 signaling
Ke Jiang, GenPeng Li, Wenjie Chen, Linlin Song, Tao Wei, Zhihui Li, Rixiang Gong, Jianyong Lei, Hubing Shi, Jingqiang Zhu
Published: 13 February 2020
OncoTargets and Therapy, Volume 13, pp 1311-1319; doi:10.2147/ott.s231361

Abstract:Plasma Exosomal miR-146b-5p and miR-222-3p are Potential Biomarkers for Lymph Node Metastasis in Papillary Thyroid Carcinomas
Jing Luo, Xing Luo, Xin Liu, Zhenqiang Fang, Jie Xu, Longkun Li
Published: 13 February 2020
OncoTargets and Therapy, Volume 13, pp 1321-1330; doi:10.2147/ott.s239407

Abstract:DUSP9 Suppresses Proliferation and Migration of Clear Cell Renal Cell Carcinoma via the mTOR Pathway
Jiejin Qian, Xianbo Huang, Yinyin Zhang, Xiujin Ye, Wenbin Qian
Published: 12 February 2020
OncoTargets and Therapy, Volume 13, pp 1265-1276; doi:10.2147/ott.s230873

Abstract:Gamma-Catenin Overexpression in AML Patients May Promote Tumor Cell Survival via Activation of the Wnt/Beta-Catenin Axis Jiejin Qian,1,* Xianbo Huang,1,* Yinyin Zhang,1,2 Xiujin Ye,1 Wenbin Qian1,2 1Department of Hematology, The First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou 310003, People’s Republic of China; 2Malignant Lymphoma Diagnosis and Therapy Center, The First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou 310003, People’s Republic of China*These authors contributed equally to this workCorrespondence: Wenbin Qian; Xiujin YeInstitute of Hematology, The First Affiliated Hospital, College of Medicine, Zhejiang University, 79# Qingchun Road, Hangzhou 310003, People’s Republic of ChinaTel +86-571-87235983; +86-571-87235875Fax +86-571-87235560Email [email protected]; [email protected]: Canonical Wnt/β-catenin signaling is frequently dysregulated in acute myeloid leukemia (AML) and has been implicated in leukemogenesis. γ-catenin was previously demonstrated to be associated with the nuclear localization of β-catenin, the central mediator, and to exert oncogenic effects in AML; however, the underlying mechanisms remain unclear. Our study aimed to investigate the expression characteristics of γ-catenin in AML patients, explore the mechanisms by which γ-catenin regulates β-catenin, and discuss the feasibility of targeting γ-catenin for AML treatment.Methods: The mRNA expression levels of γ-catenin in AML patients were measured by qRT-PCR. Cell proliferation was examined via Cell Counting Kit-8 (CCK-8) assays. The expression levels of related proteins were measured via Western blotting. Specific siRNA was used to modulate the expression level of the γ-catenin gene. Apoptosis and cell cycle distribution were quantified by flow cytometry. The subcellular localization of γ-catenin and β-catenin was examined via immunofluorescence with a confocal laser scanning microscope.Results: Overexpression of γ-catenin was frequently observed in AML and correlated with poor prognosis. Consistent with this finding, suppression of γ-catenin in the AML cell line THP-1 induced growth inhibition, promoted apoptosis and blocked β-catenin nuclear translocation. Interestingly, γ-catenin knockdown sensitized THP-1 cells to cytotoxic chemotherapeutic agents such as cytarabine and homoharringtonine and further inhibited β-catenin nuclear localization. Moreover, our data implied the relationship between γ-catenin and GSK3β (whose effect on β-catenin is mediated by its own phosphorylation), which may be the principal mechanism underlying the anti-AML effect of γ-catenin inhibition.Conclusion: Taken together, our results revealed a potential role of γ-catenin in AML pathogenesis–mainly through the inhibition of GSK3β-mediated nuclear localization of β-catenin–and indicate that targeting γ-catenin might offer new AML treatments.Keywords: acute myeloid leukemia, γ-catenin, β-catenin, chemotherapy
Liangchun Yang, FangHua Ye, Li Zeng, Yanling Li, Wenwen Chai
Published: 12 February 2020
OncoTargets and Therapy, Volume 13, pp 1187-1198; doi:10.2147/ott.s234530

Abstract:Knockdown of HMGB1 Suppresses Hypoxia-Induced Mitochondrial Biogenesis in Pancreatic Cancer Cells
Yanhua Yu, Fang Yu, Pijiang Sun
Published: 11 February 2020
OncoTargets and Therapy, Volume 13, pp 1245-1253; doi:10.2147/ott.s234276

Abstract:MicroRNA-1246 Promotes Melanoma Progression Through Targeting FOXA2