Cartilage oligomeric matrix protein (COMP)

Cartilage oligomeric matrix protein (COMP) is a pentameric extracellular matrix glycoprotein and a member of the thrombospondin family, predominantly present in cartilage, meniscus, tendons, ligaments, and synovium[1][2][3]. COMP is structurally characterized by five identical arms containing coiled-coil domains, EGF-like repeats, calcium-binding domains, and a C-terminal globular domain[1][2][4]. It acts as a bridging molecule for ECM stability, interacting with various collagens, fibronectin, proteoglycans, cellular receptors, and growth factors such as TGF-β[1][2][3]. Mutations in COMP lead to pseudoachondroplasia and multiple epiphyseal dysplasia via impaired protein folding and retention within the chondrocyte endoplasmic reticulum, causing skeletal dysplasia and loss of bone growth[1][2][3][4]. COMP is essential in the assembly and stabilization of collagen fibers, maintenance of tissue mechanical properties, and regulation of cell signaling. It serves as a key biomarker for cartilage destruction in osteoarthritis and rheumatoid arthritis and is implicated in broader roles in fibrosis, cardiovascular disease, and malignancy[1][2][3]. While COMP supplementation may aid cartilage and vascular diseases, it could promote tissue fibrosis or cancer metastasis, highlighting the need for careful therapeutic consideration[1].

Other names

Thrombospondin-5TSP-5Multiple epiphyseal dysplasia proteinPseudoachondroplasia proteinEDM1MEDCTS2EPD1PSACHTHBS5

Not applicable (no direct inhibitors/agonists known)