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Endogenous growth factors are a diverse group of naturally occurring proteins and peptides that act as signaling molecules to regulate fundamental cellular processes, including proliferation, differentiation, survival, and migration [1.3.1, 1.4.1]. They typically function by binding to specific high-affinity cell surface receptors, most notably receptor tyrosine kinases, to initiate intracellular signaling cascades such as the MAPK and PI3K/Akt pathways [1.2.1, 1.3.1]. In healthy physiology, these factors are critical for embryonic development, tissue homeostasis, and wound repair [1.3.2, 1.4.1]. However, their dysregulation is a hallmark of various pathologies; for instance, overproduction or constitutive activation of growth factor signaling is a primary driver of tumor growth and angiogenesis in cancer [1.2.4, 1.2.5]. Therapeutically, endogenous growth factors are utilized in two primary ways: as recombinant protein drugs to stimulate regeneration (e.g., in wound healing or growth hormone deficiency) and as targets for inhibition to treat diseases characterized by excessive growth (e.g., using monoclonal antibodies or tyrosine kinase inhibitors in oncology and ophthalmology) [1.2.1, 1.3.4]. While highly effective, targeting these pathways presents challenges, including the risk of promoting malignancy when using agonists and the potential for significant side effects when inhibiting factors essential for normal tissue maintenance [1.5.1, 1.5.2].
Drugs targeting endogenous growth factors function by either supplementing deficient levels with recombinant versions (agonism) to promote tissue repair and growth, or by blocking their activity (antagonism) using monoclonal antibodies or small molecule inhibitors to halt pathological processes like tumor angiogenesis and uncontrolled cell proliferation [1.2.1, 1.3.1].
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