{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTGFBI is a secreted extracellular matrix protein that plays a pivotal role in modulating cell–matrix interactions. Studies have shown that multiple domains within TGFBI, including its fasciclin‐1 regions and a conserved “YH” motif, mediate adhesion by interacting with distinct integrins (for instance, αvβ5, αvβ3, or α6β4) on various cell types. TGFBI can be covalently and noncovalently associated with major ECM components such as collagen VI and small leucine‐rich proteoglycans, thereby participating in the organization and stabilization of tissue microfibrils. Moreover, post‐secretion processing of TGFBI, which may release RGD‐containing peptides, has been implicated in promoting apoptosis via integrin‐dependent signals."}, {"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": "\nIn cancer, the function of TGFBI is multifaceted and context‐dependent. In certain settings such as prostate, lung, and breast cancer cells, upregulation of TGFBI can enhance cell adhesion and suppress migration and metastasis, with regulatory input from noncoding RNAs and epigenetic modifications. In contrast, overexpression of TGFBI in colon cancer and melanoma appears to promote extravasation and invasive behavior by modulating endothelial junctions—often via activation of integrin/kinase–dependent cascades—and its proteolytic cleavage by matrix metalloproteinase‐9 can release fragments that further alter cell adhesion and stimulate invasion. In ovarian and pancreatic cancers, altered TGFBI expression and methylation status correlate with chemotherapeutic responses and tumor aggressiveness, positioning TGFBI as both a potential prognostic biomarker and therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the eye, particularly in the context of corneal dystrophies and related disorders, mutations in the TGFBI gene lead to protein misfolding, altered stability, and abnormal deposition of TGFBI‐derived aggregates in the cornea. Detailed genotype–phenotype correlations have revealed that specific amino acid substitutions—especially within the fourth FAS1 domain—can dictate whether deposits will form as amyloid or nonamyloid aggregates, thereby determining the clinical course of corneal dystrophies such as lattice and granular dystrophies. In addition, variations in TGFBI have been associated with other corneal conditions including Fuchs’ endothelial dystrophy and keratoconus."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cell adhesion, cancer, and corneal pathology, TGFBI also contributes to inflammatory tissue remodeling. For example, in rheumatoid synovitis, uptake of apoptotic cells by macrophages stimulates TGFBI production, which in turn influences fibroblast function and collagen accumulation via downstream regulation of matrix metalloproteinases and transcription factors—a process that may contribute to the fibrotic response in chronic inflammation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jung-Eun Kim, Ha-Won Jeong, Ju-Ock Nam, et al. 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