{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC39A8 encodes the ZIP8 protein, a versatile transmembrane transporter that mediates the cellular uptake of several divalent metal ions—including manganese, zinc, iron, cadmium, and even selenium. ZIP8 function is tightly regulated by extracellular metal levels and post‐translational modifications, so that both loss‐of‐function mutations (which impair manganese uptake, enzyme activity, mitochondrial function, and glycosylation) and common coding variants (such as the A391T substitution) can disrupt metal homeostasis. These alterations are implicated in a spectrum of disorders, ranging from congenital disorders of glycosylation and Leigh-like mitochondrial disease to altered toxic metal handling and perturbed cellular metabolism."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nZIP8 is also a critical mediator of cellular responses to inflammatory and immune‐derived signals. Its expression is rapidly induced by proinflammatory mediators—including TNF‑α, interferon‑γ, and NF‑κB activation—in multiple cell types such as lung epithelia, macrophages, and T lymphocytes. In activated T cells, for example, ZIP8 promotes zinc flux from intracellular compartments that modulates key signaling cascades and transcription factor activities, thereby enhancing cytokine production and effector functions. Similarly, in macrophages and other immune cells, ZIP8 helps to temper excessive NF‑κB signaling and protect against inflammatory cytotoxicity, with dysregulated expression contributing to conditions such as sepsis, tuberculosis, and rheumatoid arthritis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its biochemical and immunologic roles, ZIP8 has emerged as a pleiotropic factor in human disease. Genome‐wide studies have linked SLC39A8 variation with altered lipid profiles, blood pressure, and cardiac biomarkers, while clinical and experimental investigations associate its defective metal transport with disorders of skeletal development (including severe adolescent idiopathic scoliosis), neuropsychiatric conditions such as schizophrenia, and aberrant glycosylation patterns evident in liver, intestinal, and placental tissues. In the lung and brain microvasculature, ZIP8 (often in concert with the closely related ZIP14) ensures proper manganese import essential for mitochondrial and antioxidant enzyme functions, and emerging evidence even suggests a role in selenium uptake. Collectively, these findings underscore the central role of SLC39A8/ZIP8 in mediating metal ion homeostasis across diverse tissues and its contribution to disease susceptibility and progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Chia-Yu Wang, Supak Jenkitkasemwong, Stephanie Duarte, et al. 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