NDLI: The DNA Methyltransferase DNMT1 and Tyrosine-Protein Kinase KIT Cooperatively Promote Resistance to 5-Aza-2′-deoxycytidine (Decitabine) and Midostaurin (PKC412) in Lung Cancer Cells

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The DNA Methyltransferase DNMT1 and Tyrosine-Protein Kinase KIT Cooperatively Promote Resistance to 5-Aza-2′-deoxycytidine (Decitabine) and Midostaurin (PKC412) in Lung Cancer Cells

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The DNA Methyltransferase DNMT1 and Tyrosine-Protein Kinase KIT Cooperatively Promote Resistance to 5-Aza-2′-deoxycytidine (Decitabine) and Midostaurin (PKC412) in Lung Cancer Cells

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shen, Na Molina, Julian R. Yang, Ping Pang, Jiuxia Yan, Fei Liu, Shujun
Description	Author Affiliation: Yan F ( From the Hormel Institute, University of Minnesota, Austin, Minnesota 55912 and.); Shen N ( From the Hormel Institute, University of Minnesota, Austin, Minnesota 55912 and.); Pang J ( From the Hormel Institute, University of Minnesota, Austin, Minnesota 55912 and.); Molina JR ( the Department of Medical Oncology and.); Yang P ( the Division of Epidemiology, Mayo Clinic, Rochester, Minnesota 55905.); Liu S ( From the Hormel Institute, University of Minnesota, Austin, Minnesota 55912 and sliu@hi.umn.edu.)
Abstract	Lung cancer cells are sensitive to 5-aza-2'-deoxycytidine (decitabine) or midostaurin (PKC412), because decitabine restores the expression of methylation-silenced tumor suppressor genes, whereas PKC412 inhibits hyperactive kinase signaling, which is essential for cancer cell growth. Here, we demonstrated that resistance to decitabine (decitabine(R)) or PKC412 (PKC412(R)) eventually results from simultaneously remethylated DNA and reactivated kinase cascades. Indeed, both decitabine(R) and PKC412(R) displayed the up-regulation of DNA methyltransferase DNMT1 and tyrosine-protein kinase KIT, the enhanced phosphorylation of KIT and its downstream effectors, and the increased global and gene-specific DNA methylation with the down-regulation of tumor suppressor gene epithelial cadherin CDH1. Interestingly, decitabine(R) and PKC412(R) had higher capability of colony formation and wound healing than parental cells in vitro, which were attributed to the hyperactive DNMT1 or KIT, because inactivation of KIT or DNMT1 reciprocally blocked decitabine(R) or PKC412(R) cell proliferation. Further, DNMT1 knockdown sensitized PKC412(R) cells to PKC412; conversely, KIT depletion synergized with decitabine in eliminating decitabine(R). Importantly, when engrafted into nude mice, decitabine(R) and PKC412(R) had faster proliferation with stronger tumorigenicity that was caused by the reactivated KIT kinase signaling and further CDH1 silencing. These findings identify functional cross-talk between KIT and DNMT1 in the development of drug resistance, implying the reciprocal targeting of protein kinases and DNA methyltransferases as an essential strategy for durable responses in lung cancer.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-07-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA (Cytosine-5-)-Methyltransferase Genetics Drug Resistance, Neoplasm Lung Neoplasms Proto-Oncogene Proteins C-kit Animals Azacitidine Administration & Dosage Analogs & Derivatives Cadherins Metabolism Cell Line, Tumor Cell Proliferation Drug Effects DNA Methylation Gene Expression Regulation, Neoplastic Drug Therapy Staurosporine Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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