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Laccase domain-containing protein 1 (LACC1, also called FAMIN) is an enzyme with oxidoreductase activity primarily expressed in cells of the innate immune system, such as macrophages, monocytes, dendritic cells, and neutrophils[1][2][3]. LACC1 plays a central role in regulating metabolic and immunological functions within macrophages by modulating purine nucleotide metabolism, enabling efficient fatty acid oxidation, promoting reactive oxygen species (ROS) production, and facilitating activation of the inflammasome, which is critical for antimicrobial defense[1][2][3]. The protein also contributes to mitochondrial function, associates with peroxisomes, and interacts with fatty acid synthase, and it can affect unfolded protein response under endoplasmic reticulum stress[2]. Genetic variants and loss-of-function mutations in LACC1 are strongly associated with inflammatory and autoimmune diseases, especially Crohn’s disease, ulcerative colitis, juvenile idiopathic arthritis, Behçet’s disease, and leprosy[1][2][3]. Despite its domain homology, LACC1 does not show classical laccase activity in mammalian cells[2]. There are currently no approved drugs directly targeting LACC1, but it may represent a future immunometabolic therapeutic target, with genetic variants serving as biomarkers for disease risk stratification and mechanistic studies in inflammatory disorders[1][2][3].
No approved drugs; mechanism is related to immunometabolic regulation in innate immune cells if targeted therapeutically
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