MiR-23a regulates TGF-β-induced epithelial-mesenchymal transition by targeting E-cadherin in lung cancer cells. 2012

Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
Department of Internal Medicine, Division of Pulmonary Medicine/Infection and Oncology, Nippon Medical School, Tokyo 113-8603, Japan.

Transforming growth factor-β (TGF-β)-induced epithelial-mesenchymal transition (EMT) has been shown to be related to the pathogenesis of various diseases including lung cancer. Recently, microRNAs (miRNA) have been recognized as a new class of genes involved in human tumorigenesis. MiR-23a/24/27a is a miRNA cluster located in chromosome 19p13.12, which can function as an oncogene in several human cancers. In this study, we analyzed miR-23a/24/27a expression in 10 non-small cell cancer (NSCLC) cell lines by real-time PCR analysis. Correlation between expression of these miRNAs and TGF-β/Smad signaling was evaluated. We found that miR-23a could be regulated by TGF-β1 in a Smad-dependent manner in A549 lung adenocarcinoma cells showing the EMT phenomenon. Knockdown of miR-23a partially restored E-cadherin expression under conditions of TGF-β1 stimulation. In contrast, overexpression of miR-23a could suppress E-cadherin expression and stimulate EMT. Furthermore, A549 cells with overexpressed miR-23a were more resistant to gefitinib compared to the parental cells. These findings suggest that miR-23a regulates TGF-β-induced EMT by targeting E-cadherin in lung cancer cells and may be useful as a new therapeutic target in NSCLC.

UI MeSH Term Description Entries
D008175 Lung Neoplasms Tumors or cancer of the LUNG. Cancer of Lung,Lung Cancer,Pulmonary Cancer,Pulmonary Neoplasms,Cancer of the Lung,Neoplasms, Lung,Neoplasms, Pulmonary,Cancer, Lung,Cancer, Pulmonary,Cancers, Lung,Cancers, Pulmonary,Lung Cancers,Lung Neoplasm,Neoplasm, Lung,Neoplasm, Pulmonary,Pulmonary Cancers,Pulmonary Neoplasm
D011799 Quinazolines A group of aromatic heterocyclic compounds that contain a bicyclic structure with two fused six-membered aromatic rings, a benzene ring and a pyrimidine ring. Quinazoline
D002289 Carcinoma, Non-Small-Cell Lung A heterogeneous aggregate of at least three distinct histological types of lung cancer, including SQUAMOUS CELL CARCINOMA; ADENOCARCINOMA; and LARGE CELL CARCINOMA. They are dealt with collectively because of their shared treatment strategy. Carcinoma, Non-Small Cell Lung,Non-Small Cell Lung Cancer,Non-Small Cell Lung Carcinoma,Non-Small-Cell Lung Carcinoma,Nonsmall Cell Lung Cancer,Carcinoma, Non Small Cell Lung,Carcinomas, Non-Small-Cell Lung,Lung Carcinoma, Non-Small-Cell,Lung Carcinomas, Non-Small-Cell,Non Small Cell Lung Carcinoma,Non-Small-Cell Lung Carcinomas
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000077156 Gefitinib A selective tyrosine kinase inhibitor for the EPIDERMAL GROWTH FACTOR RECEPTOR (EGFR) that is used for the treatment of locally advanced or metastatic NON-SMALL CELL LUNG CANCER. Iressa,N-(3-Chloro-4-fluorophenyl)-7-methoxy-6-(3-(4-morpholinyl)propoxy)-4-quinazolinamide,ZD 1839,ZD1839
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D015820 Cadherins Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body. Cadherin,E-Cadherins,Epithelial-Cadherin,Liver Cell Adhesion Molecules,N-Cadherins,Neural Cadherin,P-Cadherins,Uvomorulin,Cadherin-1,Cadherin-2,Cadherin-3,E-Cadherin,Epithelial-Cadherins,Liver Cell Adhesion Molecule,N-Cadherin,Neural Cadherins,P-Cadherin,Placental Cadherins,Cadherin 1,Cadherin 2,Cadherin 3,Cadherin, Neural,Cadherins, Neural,Cadherins, Placental,E Cadherin,E Cadherins,Epithelial Cadherin,Epithelial Cadherins,N Cadherin,N Cadherins,P Cadherin,P Cadherins
D016212 Transforming Growth Factor beta A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins. Bone-Derived Transforming Growth Factor,Platelet Transforming Growth Factor,TGF-beta,Milk Growth Factor,TGFbeta,Bone Derived Transforming Growth Factor,Factor, Milk Growth,Growth Factor, Milk
D045744 Cell Line, Tumor A cell line derived from cultured tumor cells. Tumor Cell Line,Cell Lines, Tumor,Line, Tumor Cell,Lines, Tumor Cell,Tumor Cell Lines
D058750 Epithelial-Mesenchymal Transition Phenotypic changes of EPITHELIAL CELLS to MESENCHYME type, which increase cell mobility critical in many developmental processes such as NEURAL TUBE development. NEOPLASM METASTASIS and DISEASE PROGRESSION may also induce this transition. Epithelial-Mesenchymal Transformation,Epithelial Mesenchymal Transformation,Epithelial Mesenchymal Transition,Transformation, Epithelial-Mesenchymal,Transition, Epithelial-Mesenchymal

Related Publications

Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
October 2014, Biochemical and biophysical research communications,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
June 2018, Molecular medicine reports,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
January 2018, Cancer cell international,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
February 2014, Molecular cancer therapeutics,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
January 2017, Cellular & molecular biology letters,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
November 2017, Biochemical and biophysical research communications,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
January 2019, Journal of Cancer,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
January 2020, Journal of Cancer,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
August 2018, Cancer letters,
Mengru Cao, and Masahiro Seike, and Chie Soeno, and Hideaki Mizutani, and Kazuhiro Kitamura, and Yuji Minegishi, and Rintaro Noro, and Akinobu Yoshimura, and Li Cai, and Akihiko Gemma
September 2016, Reproduction (Cambridge, England),
Copied contents to your clipboard!