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Lysine histone methylation is one of the most robust epigenetic marks and is essential for the regulation of multiple cellular processes. The methylation of H3-K4 seems to be of particular significance, as it is associated with active regions of the genome. H3-K4 methylation was considered irreversible until the identification of a large number of histone demethylases indicated that demethylation events play an important role in histone modification dynamics. So far at least 2 classes of H3-K4 specific histone demethylase, LSD1 (BHC110, KDM1) and JARIDs have been identified. LSD1 can remove di- and mono-methylation from H3-K4 by using an amine oxidase reaction. LSD1 is associated with complexes that function as both transcriptional inactivators and activators. It demethylates mono-/di-methyl H3-K4 when associated with the Co-REST complex at neuronal genes, or mono-/di-methyl H3-K9 when associated with the androgen receptor.