{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nIGFBP‐4 serves as a critical modulator of insulin‐like growth factor (IGF) signaling with far‐reaching consequences for cell growth, survival, and therapeutic responsiveness. For instance, loss of IGFBP‐4 expression in certain cancer cells has been associated with derepressed IGF receptor signaling and resistance to EGFR–targeted therapies, emphasizing its role in maintaining appropriate growth regulation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDuring development, IGFBP‐4 exerts dual functions. It has been shown to act as a cardiogenic growth factor by inhibiting canonical Wnt signaling, thereby promoting cardiomyocyte differentiation independent of its IGF–binding activity, while in parallel, genetic models reveal that a deficiency in IGFBP‐4 disrupts normal prenatal and postnatal growth processes, highlighting its necessity for optimal IGF–mediated embryogenesis and metabolic homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "2", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nProteolytic processing of IGFBP‐4 is an important regulatory mechanism that finely tunes local IGF bioavailability. Studies using a protease–resistant IGFBP‐4 mutant demonstrate that blocking its cleavage leads to enhanced inhibition of cell growth, while protease activity (such as that mediated by PAPP–A) is required to release IGF from its inhibitory complex with IGFBP‐4, thereby promoting IGF–dependent anabolic responses."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn tissues involved in energy balance and structural integrity, IGFBP‐4 modulates adipose tissue expansion and skeletal growth. It regulates adipogenesis and fat depot development as evidenced by altered adipocyte differentiation and depot expansion in IGFBP‐4–deficient models, and it further influences bone formation and muscle adaptation—as seen in studies where electrical stimulation upregulates its expression to favor phenotype transitions—underscoring its multifaceted role in musculoskeletal and metabolic regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIGFBP‐4 also functions as a regulator of cell proliferation and tumor suppression. Transcriptional regulation by factors such as SOX9 leads to increased IGFBP‐4 expression, which in turn suppresses aberrant cell proliferation in the intestine. Furthermore, changes in proteolytic processing and expression levels of IGFBP‐4 have been implicated in mammary tumorigenesis and other cancer models, suggesting that maintaining its proper regulation is essential for preventing malignant cell growth."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in development and tumor suppression, IGFBP‐4 participates in senescence and neural regulation. As a component of the senescence–associated secretory phenotype (SASP), IGFBP‐4 mediates paracrine signaling that may contribute to aging processes, and altered expression in neural tissues has been linked with neurodegenerative conditions such as amyotrophic lateral sclerosis. Its expression in sensory structures like the cochlea further hints at specialized roles in neural differentiation and function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the gastrointestinal tract and during post–ischemic repair, IGFBP‐4 modulates the actions of hormones and growth factors to promote tissue regeneration. Specifically, its regulation is critical for GLP–2–induced intestinal growth and proper angiogenic responses following myocardial infarction, where synergistic interactions with factors like VEGF help reduce fibrosis and promote neovascularization."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies further highlight the diverse roles of IGFBP‐4 in paracrine and autocrine signaling pathways. Altered IGFBP‐4 expression influenced by HB–EGF can modulate growth rates, while its interplay with PAPP–A and other modulators contributes to pathologies such as diabetic nephropathy, intrahepatic cholangiocarcinoma, and breast cancer progression mediated by RNA–binding proteins like MEX3A."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Marta Guix, Anthony C Faber, Shizhen Emily Wang, et al. 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