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Osteomodulin (OMD) is a member of the small leucine-rich proteoglycan (SLRP) family, primarily found in mineralized tissues such as bone and dentin. It has high expression in osteoblasts and participates in extracellular matrix organization, specifically by binding collagen and influencing fibril shape, as well as regulating mineral deposition. OMD enhances bone morphogenetic protein 2 (BMP2)-induced osteogenesis by directly binding both BMP2 and its receptors and coordinating BMP/SMAD signaling. It can also bind to RANKL, inhibiting osteoclastogenesis and thus balancing bone formation and resorption. OMD serves as a mineralization marker, is downregulated in certain bone diseases such as osteoarthritis, and is linked to pathological calcification in vascular disease. There is current research interest in its possible therapeutic use for bone regeneration, but no drugs are known to target OMD directly.
Not applicable; OMD is not a direct drug target
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