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Collectin-11 (CL-11), encoded by the COLEC11 gene, is a soluble pattern-recognition molecule and member of the collectin family of C-type lectins[1][2][3]. It contains both collagen-like domains and carbohydrate recognition domains, enabling it to bind a variety of sugar moieties, particularly fucose and mannose, found on microbial surfaces and on apoptotic or stressed host cells[1][3]. CL-11 is secreted and plays a dual role: in embryonic development, it is particularly involved as a guidance cue for migrating neural crest cells, with deficiency causing craniofacial dysmorphism and multiple congenital anomalies (as seen in 3MC syndrome-2)[2][3]. In the immune system, CL-11 can initiate the lectin pathway of complement activation by associating with MASP (MBL-associated serine proteases), promoting opsonization and clearance of pathogens as well as mediating inflammatory responses[1][3]. Although crucial for both development and immunity, it is not established as a direct pharmacological therapeutic target, and there are no currently known drugs or specific safety concerns related to COLEC11 modulation[1][2][3].
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