Kdm1a, also known as LSD1 (lysine-specific demethylase 1), is a histone demethylase. It contains a flavin adenine dinucleotide (FAD)-dependent amine oxidase domain and demethylates histone 3 lysine 4 and histone 3 lysine 9 (H3K4me1/2 and H3K9me1/2). It has emerged as an epigenetic developmental regulator and is involved in multiple biological processes, and its dysregulation is associated with carcinogenesis [5].

Kdm1a promotes the progression of various cancers. In thyroid cancer, it maintains cancer stem cell stemness through the Wnt/β-catenin signaling pathway by down-regulating APC2 and DKK1, antagonists of the canonical Wnt pathway [1]. In acute myeloid leukemia (AML), it is a key regulator of stem cell potential, and its inhibitor ORY-1001 can induce blast differentiation and reduce leukemic stem cell capacity [2]. In gastric cancer, inhibition of Kdm1A causes organoid growth retardation, and its cancer-supporting functions center on repression of NDRG1, whose de-repression leads to inhibition of Wnt signaling and G1 cell cycle arrest [3]. In breast cancer, KDM1A acts as a transcriptional activator of PIAS4, which facilitates the SUMOylation of SLC7A11, and Tanshinone IIA can promote ferroptosis by suppressing the KDM1A/PIAS4/SLC7A11 axis [4]. In ovarian cancer, KDM1A is highly overexpressed, and its knockdown or inhibition sensitizes cancer cells to chemotherapy drugs, reducing cell viability, clonogenic survival, and inducing apoptosis [6].

In conclusion, Kdm1a is an important epigenetic regulator involved in cancer development and progression. Studies using loss-of-function models have revealed its role in multiple cancer-related biological processes, highlighting its potential as a therapeutic target for cancer treatment.