Lysine-specific histone demethylase 1A (LSD1) also known as lysine (K)-specific demethylase 1A (KDM1A) is a protein that in humans is encoded by the KDM1A gene. [5] LSD1 is a flavin-dependent monoamine oxidase, which can demethylate mono- and di-methylated lysines, specifically histone 3, lysine 4 (H3K4).

Dec 25, 2024 · KDM1A (Lysine Demethylase 1A) is a Protein Coding gene. Diseases associated with KDM1A include Cleft Palate, Psychomotor Retardation, And Distinctive Facial Features and Acth-Independent Macronodular Adrenal Hyperplasia 3 .

Mar 7, 2024 · Kdm1a is a histone demethylase linked to intellectual disability with essential roles during gastrulation and the terminal differentiation of specialized cell types, including neurons, that...

Lysine-specific demethylase 1A (KDM1A) is a histone demethylation enzyme and a crucial epigenetic factor for multiple pathological pathways that mediate carcinogenesis and immunogenicity. Although increasing evidence supposes the association between ...

Feb 19, 2025 · KDM1A is the first germline autosomal dominant predisposition gene identified in multiple myeloma and provides new insights into multiple myeloma etiology and the mechanistic role of KDM1A as a tumor suppressor during post-germinal center B-cell differentiation.

In this review, we discuss the microenvironment of KDM1A in cancer progression that enables this protein to activate or repress target gene expression, thus making it an important epigenetic modifier that regulates the growth and differentiation potential of cells.

What is KDM1A? KDM1A or LSD1 is an important gene in the field of epigenetics, as it was the first known histone demethylase. This means that it has a key role in regulating other genes.

Lysine specific demethylase 1 (LSD1/KDM1A) plays a well-established role in the normal hematopoietic and neuronal stem cells. Overexpression of LSD1 has been documented in a variety of cancers, where the enzyme is, usually, associated with the …

Loss of ZNF750 or KDM1A in human keratinocytes or mice resulted in sustained and excessive inflammation resembling psoriatic skin, which could be restored to homeostatic conditions upon silencing of TLR3. Our findings explain how the skin’s surface prevents excessive inflammation through ZNF750- and KDM1A-mediated suppression of PRRs.

KDM1A catalyzes amine oxidation by oxidative cleavage of the α-carbon bond of methylated lysine to form an imine intermediate, which is hydrolyzed to form formaldehyde, releasing one molecule of H 2 O 2 and the demethylated lysine in the histone H3 peptide.