Research Papers:
Identification of a new class of WNT1 inhibitor: Cancer cells migration, G-quadruplex stabilization and target validation
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Abstract
Lien-Cheng Chang1,2,3, Tsung-Chih Chen3, Shiag-Jiun Chen4, Chun-Liang Chen3, Chia-Chung Lee3, Shih-Hsiung Wu5, Yun Yen3, Hsu-Shan Huang3,4, Jing-Jer Lin1,6
1Institute of Biopharmaceutical Sciences, National Yang-Ming University, Taipei 112, Taiwan, ROC
2Food and Drug Administration, Ministry of Health and Welfare, Taipei 115, Taiwan, ROC
3Graduate Institute of Cancer Biology and Drug Discovery, College of Medical Science and Technology, Taipei Medical University, Taipei 110, Taiwan, ROC
4School of Pharmacy, National Defense Medical Center, Taipei 114, Taiwan, ROC
5Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, ROC
6Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei 100, Taiwan, ROC
Correspondence to:
Hsu-Shan Huang, email: [email protected]
Jing-Jer Lin, email: [email protected]
Keywords: Wnt1-mediated signaling pathway, G-quadruplex, 6-substituted 9-chloro-11H-indeno[1,2-c]quinolin-11-ones, reporter assay
Received: June 14, 2015 Accepted: November 16, 2015 Published: December 15, 2015
ABSTRACT
Developing the Wnt pathway inhibitors has been considered as a therapeutic approach for cancers and other Wnt-related diseases. Previously we found that the G-rich sequence of WNT1 promoter is capable of forming G-quadruplex structure and stabilizing agents for Wnt1-mediated signaling pathway. Using a established cell-based drug screen system that enabled the evaluation of WNT1 expression activity in a G-quadruplex structure dependent manner, we evaluated a series of 6-substituted 9-chloro-11H-indeno[1,2-c]quinolin-11-one derivatives that potentially inhibit the Wnt1-mediated signaling pathway. The most potent compound SJ26 showed repression of WNT1 activity in a G-quadruplex structure-dependent manner. Moreover, compound SJ26 inhibited the WNT1-mediated downstream signaling pathway and suppressed migration activity of cancer cells. Thus, we have identified a tetracyclic azafluorenone, SJ26, that is capable of binding to G-quadruplex DNA structure, repressing WNT1 expression, and inhibiting cell migration.
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