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Insulin-like growth factor 1 and insulin-like growth factor 2 are peptide hormones structurally similar to insulin. IGF-1 is primarily produced by the liver in response to growth hormone stimulation, promoting cell growth, proliferation, differentiation, and survival; it acts systemically and locally in various tissues and is critical for postnatal growth, skeletal and muscle development, and neural maturation. IGF-2 is highly expressed during fetal development and is essential for embryonic and placental growth, as well as organogenesis in mammals. Both act by binding to IGF-1 receptor (IGF1R) and, for IGF-2, also to IGF-2 receptor (IGF2R), triggering intracellular signaling cascades leading to cell survival and proliferation. IGFs are tightly regulated by a family of high-affinity IGF binding proteins (IGFBPs), which control their bioavailability and activity. Dysregulation of IGF signaling is implicated in numerous pathologies, particularly cancer progression and metabolic diseases. Therapeutically, recombinant IGF-1 and agents targeting IGF pathways are used or investigated for growth disorders, metabolic dysfunction, and oncology indications.
Drugs may act by mimicking IGF-1 (agonism for growth/pediatric disease) Drugs may inhibit IGF-1/IGF-2 or block IGF-1 receptor signaling (antagonists for cancer) Drugs may modulate the bioavailability of IGFs by altering IGF binding proteins (IGFBPs)
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