GSK-LSD1 Dihydrochloride

Lysine-specific demethylase 1 (LSD1) belongs to the family of flavin adenine dinucleotide (FAD)-dependent amine oxidases that include monoamine oxidases (MAOs) and polyamine oxidase (PAO).¹ LSD1 specifically demethylates mono- and dimethylated histone H3 lysine 4, resulting in transcriptional repression.² It also controls the tumor suppressor activity of p53 by demethylating a specific p53 lysine residue (LYS³⁷⁰).³ GSK-LSD1 is an irreversible, mechanism-based inhibitor of LSD1 (IC₅₀ = 16 nM) that is >1,000-fold selective over the closely related FAD-utilizing enzymes LSD2, MAO-A, and MAO-B.⁴ GSK-LSD1 induces gene expression changes in various cancer cell lines, inhibiting their proliferation (EC₅₀s <5 nM).⁴ See the Structural Genomics Consortium (SGC) website for more information.

1.Shi, Y., Lan, F., Matson, C., et al.Histone demethylation mediated by the nuclear amine oxidase homolog LSD1Cell119(7)941-953(2004) 2.Forneris, F., Binda, C., Vanoni, M.A., et al.Human histone demethylase LSD1 reads the histone codeJ. Biol. Chem.280(50)41360-41365(2005) 3.Huang, J., Sengupta, R., Espejo, A.B., et al.p53 is regulated by the lysine demethylase LSD1Nature449105-108(2007) 4.Epigenetics probes collection(2014)