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Collectin-12 (COLEC12) is a transmembrane scavenger receptor of the C-type lectin family. It possesses collagen-like sequences and a carbohydrate recognition domain, enabling it to bind carbohydrate antigens on microorganisms, thus facilitating their recognition and removal as part of the innate immune system[1][3][5]. Collectin-12 is also involved in the recognition, internalization, and degradation of oxidatively modified low-density lipoprotein (oxLDL) by vascular endothelial cells and can bind various carbohydrates such as galactose and fucose in a calcium-dependent manner, as well as sialyl Lewis X and asialo-orosomucoid[5][6]. It is expressed in several myeloid lineages, including microglia, and is implicated in the regulation of microglial phagocytic capability and possibly in the clearance of amyloid-beta, suggesting a role in neurodegenerative diseases such as Alzheimer disease[2][5]. Collectin-12 has been identified as a substrate of caspase-3 (CASP3), where cleavage leads to a soluble form that may function as a decoy receptor, modulating phagocytic responses in immune cells[2]. Genetic association studies link mutations in COLEC12 to certain intellectual developmental disorders[5][3].
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