decorin

Decorin is a small leucine-rich proteoglycan (SLRP) and an extracellular matrix protein encoded by the DCN gene. It is primarily known for its role in organizing collagen fibrils and maintaining connective tissue structure. Decorin binds to type I collagen and regulates fibrillogenesis as well as matrix assembly[3][6]. Beyond structural functions, decorin acts as a multifunctional signaling molecule that interacts with various receptor tyrosine kinases (RTKs), including EGFR (epidermal growth factor receptor), HER2, Met (hepatocyte growth factor receptor), VEGFR2 (vascular endothelial growth factor receptor 2), TLRs (Toll-like receptors), and IGFR[1][5][7]. Through these interactions it can inhibit tumor cell proliferation and metastasis by suppressing downstream signaling pathways involved in cell cycle progression and angiogenesis; it also induces autophagy/mitophagy in cancer cells[1][5]. Decorin antagonizes transforming growth factor-beta (TGF-β) activity by direct binding—attenuating fibrosis—and modulates immune responses via engagement of pattern recognition receptors such as TLR2/4 on macrophages[1][2]. It has been studied for potential therapeutic applications in cancer treatment due to its oncosuppressive properties; other roles include regulation of inflammation, wound healing, fibrosis inhibition, myokine activity promoting muscle hypertrophy via myostatin binding, modulation of angiogenesis through VEGFR2 inhibition/autophagic induction in endothelial cells[3][4].

Other names

decorin proteoglycandermatan sulphate proteoglycans 2proteoglycan II