{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nS100A12 is a member of the S100 family of calcium‐binding proteins that acts as an “alarmin” in innate immunity. Predominantly secreted by activated neutrophils and monocytes, S100A12 functions in a dual manner: intracellularly, it participates in calcium‐dependent regulation of target proteins, while extracellularly it displays cytokine‐like properties. In its secreted form, S100A12 directly activates endothelial cells, lymphocytes, mononuclear phagocytes, and other immune cells by binding to the receptor for advanced glycation end products (RAGE) and, in some settings, Toll‐like receptor 4 (TLR4). This receptor engagement triggers intracellular signaling cascades (including MAP kinase and NF‐κB pathways), promotes chemotaxis via a specific hydrophobic “hinge” domain, and contributes to the recruitment of inflammatory cells at sites of tissue injury and infection."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a broad spectrum of human diseases, altered S100A12 expression is emerging as both a mediator and a biomarker of inflammation. Elevated levels have been detected in the serum, tissues, and even feces of patients with inflammatory bowel disease, Kawasaki disease, juvenile arthritis, coronary artery disease, atherosclerosis, and other chronic inflammatory as well as neurodegenerative disorders. Furthermore, studies have linked S100A12 to abnormal mucin production in airway epithelia, enhanced antimicrobial defense (by sequestering zinc and directly restricting bacterial virulence), and even modulation of viral gene transcription. Its dysregulated expression is also associated with diabetic vascular complications, osteoarthritic cartilage degradation, periodontitis, and certain malignancies. Collectively, these diverse clinical findings point to the diagnostic and prognostic potential of S100A12 in conditions ranging from autoimmune pathology to vascular and infectious diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "45"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its cytokine‐like activities and disease biomarker potential, detailed structural and regulatory studies have revealed key features that govern S100A12 function. Its calcium‐ and zinc‐dependent conformational changes promote oligomerization (from dimers to hexamers) and the generation of symmetric hydrophobic binding surfaces that drive specific interactions with RAGE. Such interactions are further modulated by the glycosylation state of RAGE, which can influence receptor clustering and downstream NF‐κB signaling. In addition, S100A12 not only contributes to inflammatory cell recruitment and cytokine induction but also exerts direct antimicrobial effects by sequestering zinc—thereby repressing bacterial virulence factors—and is subject to epigenetic regulation under hyperglycemic conditions. These mechanistic insights highlight the therapeutic promise of targeting S100A12 or its receptor partners in a variety of inflammatory settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "46", "end_ref": "48"}, {"type": "fg_f", "ref": "37"}, {"type": "fg_fs", "start_ref": "39", "end_ref": "41"}, {"type": "fg_f", "ref": "44"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "A M Cole, Y H Kim, S Tahk, et al. 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