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Decorin is a small leucine-rich proteoglycan (SLRP) that plays a critical role in the extracellular matrix (ECM) of connective tissues. It binds type I collagen fibrils, regulates growth factor activity (TGF-beta, etc.), antagonizes receptor tyrosine kinases (EGFR, HER2/ErbB2, Met/HGFR, VEGFR2/KDR/Flk1), inhibits angiogenesis, and promotes autophagy. It acts as a "guardian from the matrix," exerting potent antitumorigenic effects. Mutations or dysregulation are associated with connective tissue disorders and corneal dystrophy. Decorin has also been identified as a myokine.
Direct binding to receptor tyrosine kinases (EGFR, HER2/ErbB2, Met/HGFR, VEGFR2/KDR/Flk1), leading to transient activation followed by downregulation via internalization/degradation pathways. Sequestration of growth factors like TGF-beta, angiopoietins, HGF, and PDGF. Binding to myostatin.
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