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Growth factor receptors activated by platelet-rich plasma (PRP) encompass a diverse set of cell-surface proteins, primarily receptor tyrosine kinases (RTKs) and serine/threonine kinase receptors, that respond to the high concentration of signaling molecules found in PRP. Key receptors in this group include the Platelet-Derived Growth Factor Receptors (PDGFR), Vascular Endothelial Growth Factor Receptors (VEGFR), Transforming Growth Factor-beta Receptors (TGFBR), and Epidermal Growth Factor Receptors (EGFR) (Marx, 2001; Dhurat & Sukesh, 2014). These receptors play a fundamental role in the body's natural healing response by regulating cell proliferation, chemotaxis, and the production of extracellular matrix (Andia & Maffulli, 2013). In clinical practice, PRP is used as a therapeutic agent to deliver a concentrated dose of ligands to these receptors, thereby enhancing tissue repair in conditions like osteoarthritis, tendinopathy, and chronic skin ulcers (Alves & Grimalt, 2018). The therapeutic efficacy of targeting these receptors simultaneously lies in their synergistic ability to promote angiogenesis and collagen synthesis. However, the lack of standardization in PRP preparation leads to variability in receptor activation levels, which remains a significant challenge for clinical consistency (Eppley et al., 2006).
Activation of multiple transmembrane receptors (RTKs and Ser/Thr kinases) leading to downstream signaling cascades (MAPK, PI3K/Akt, SMAD) that promote cellular repair and regeneration (Andia & Maffulli, 2013).
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