2. Academic Validation
  3. Lysine demethylase 5B (KDM5B): A potential anti-cancer drug target

Lysine demethylase 5B (KDM5B): A potential anti-cancer drug target

  • Eur J Med Chem. 2019 Jan 1:161:131-140. doi: 10.1016/j.ejmech.2018.10.040.
Yi-Chao Zheng 1,  Jiao Chang 2,  Lin-Chen Wang 2,  Hong-Mei Ren 2,  Jing-Ru Pang 2,  Hong-Min Liu 3
Affiliations

Affiliations

  • 1 Zhengzhou Research Base, State Key Laboratory of Cotton Biology, Zhengzhou University, Zhengzhou, 450000, China; Key Laboratory of Advanced Pharmaceutical Technology, Ministry of Education of China, Co-innovation Center of Henan Province for New Drug R & D and Preclinical Safety, School of Pharmaceutical Sciences, Institute of Drug Discovery and Development, Zhengzhou University, 100 Kexue Avenue, Zhengzhou, Henan, 450001, China; National Center for International Research of Micro-nano Molding Technology & Key Laboratory for Micro Molding Technology of Henan Province, Zhengzhou University, 100 Kexue Avenue, Zhengzhou, Henan, 450001, China; Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang, 455000, China.
  • 2 Key Laboratory of Advanced Pharmaceutical Technology, Ministry of Education of China, Co-innovation Center of Henan Province for New Drug R & D and Preclinical Safety, School of Pharmaceutical Sciences, Institute of Drug Discovery and Development, Zhengzhou University, 100 Kexue Avenue, Zhengzhou, Henan, 450001, China.
  • 3 Key Laboratory of Advanced Pharmaceutical Technology, Ministry of Education of China, Co-innovation Center of Henan Province for New Drug R & D and Preclinical Safety, School of Pharmaceutical Sciences, Institute of Drug Discovery and Development, Zhengzhou University, 100 Kexue Avenue, Zhengzhou, Henan, 450001, China. Electronic address: [email protected].
PMID: 30343192 DOI: 10.1016/j.ejmech.2018.10.040
Abstract

Lysine demethylase 5B (KDM5B) is a Histone Demethylase identified in 2007, which is responsible for erasing H3K4me2/3 activation marker. It participates in multiple repressive transcriptional complexes around target gene promoters and performs wide regulatory effects on chromatin structure. Until now, there is growing evidence for the oncogenic function of KDM5B. As the H3K4me2/3 residue represents the transcription initiation site of the active transcription gene, and demethylation of H3K4 is associated with transcriptional repression, making it a potential participant in inhibiting the expression of tumor suppressors. Therefore, KDM5B is considered as a promising drug target for Cancer therapy, and many medicinal chemists are trying to design and synthesize potent and selective KDM5B inhibitors with the aid of high-throughput screening, structure based drug design, and structure activity relationship studies. This review focuses on the basic biochemical and physiological function of KDM5B and its involved mechanisms in cancers, a comprehensive overview of KDM5B inhibitors is also introduced.

Keywords

Cancer; Histone modification; Inhibitor; KDM5B.

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