{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMicrofibrillar‐associated protein 4 (MFAP4) is a secreted extracellular matrix glycoprotein that localizes predominantly to elastic fibers and plays a key role in organizing the extracellular architecture. It directly binds components of the elastic fiber network—including tropoelastin, fibrillin‐1 and ‐2, and type I collagen—and its assembly into defined oligomeric complexes (such as trimers, hexamers, and octamers) is critical for proper elastic fiber formation and maturation. Structural studies, including cryo‐electron microscopy and site‐directed mutagenesis, have delineated specific amino acid residues and nonpolar interfaces that govern these multimerization events, while post‐translational modifications like C‐mannosylation further modulate MFAP4’s ligand‐binding properties and integrin interactions via its N‐terminal arginine–glycine–aspartate motif."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its structural roles, MFAP4 is emerging as a robust biomarker and potential mediator in a wide spectrum of clinical conditions. Genomic deletions that encompass MFAP4 have been associated with phenotypic variability in multisystem disorders such as Smith–Magenis syndrome, while altered circulating levels of MFAP4 reflect the degree of extracellular matrix remodeling in cardiovascular disease—including stable atherosclerotic disorders, peripheral artery disease, abdominal aortic aneurysm, and even microvascular complications in type 1 diabetes. Similarly, increased serum MFAP4 has been linked to hepatic fibrosis and cirrhosis, and its expression pattern in joint tissues implicates MFAP4 in the pathogenesis of rheumatoid arthritis and in the degradation processes observed in photoaged skin. In addition, distinct glycoforms of MFAP4—including those decorated with tumor‐associated carbohydrate motifs like sialyl–Lewis x—have been identified in pancreatic ductal adenocarcinoma and oral squamous cell carcinoma, while enrichment of MFAP4 in juvenile chondrocytes hints at a role in cartilage repair and stem cell function. Recent investigations further highlight its involvement in chronic pulmonary conditions through innate immune interactions as well as regulatory mechanisms acting at the promoter level."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTherapeutically, the multifaceted roles of MFAP4 in tissue remodeling and cell signaling point to new intervention strategies. Its capacity to interact with integrins and modulate TGF‐β pathways renders it an attractive target for mitigating pathological remodeling in fibrotic, vascular, and inflammatory diseases. Moreover, MFAP4’s direct binding to lung surfactant proteins and its ability to promote tropoelastin self‐assembly underpin emerging opportunities for addressing pulmonary emphysema and photo‐induced dermal damage. Advances in glycoproteomic profiling and high‐resolution structural elucidation are now paving the way for exploiting MFAP4 both as a prognostic biomarker in various cancers and as a molecular target for future therapeutic development."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Bartosz Pilecki, Anne T Holm, Anders Schlosser, et al. 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