Description
Clonality: Monoclonal
Host: Rat
Purification: Supernatant
Reactivity: Human, Bovine
COMP â cartilage oligomeric matrix protein â is a prominent multidomain glycoprotein of cartilage, accounting for up to 1% of the wet weight of articular tissues and having an approximate Mr of 97 kDa. COMP may also be found in tendon, bone (i.e. osteoblasts), ligament, certain smooth muscles and synovium. In the ECM COMP is present in a pentameric, disulfide-bonded complex with a Mr of about 550 kDa. Although the function of COMP is not completely elucidated, it appears to mediate chondrocyte attachment via integrins and to stabilize the articular cartilage ECM via specific cation-dependent interactions with collagen types II and IX, aggrecan, fibronectin, and ECM protein 1. In addition, mutations in the human COMP gene have been linked to the development of pseudoachondroplasia and multiple epiphyseal dysplasia, which are autosomal-dominant forms of short-limb dwarfism. In chondrocytes of these patients, COMP remains frequently entrapped in intracellular vesicles. COMP is a substrate for a variety of ECM degrading enzymes, including MMP-1, MMP-13, MMP-19, MMP20 and ADAMTS-4, -7 and -12. Fragments of COMP have been detected in the diseased cartilage, synovial fluid, and serum of patients with knee injuries, post-traumatic and primary osteoarthritis and rheumatoid arthritis and have proposed to be diagnostic/prognostic of degenerative cartilage diseases.
References:
1) Di Cesare, et.al., 2000. Expression of cartilage oligomeric matrix protein (COMP) by embryonic and adult osteoblasts. J. Orthopaed. Res. 18, 713-720.
2) Di Cesare, et. Al., 2002. Matrix-matrix interactions of cartilage oligomeric matrix protein and fibronectin. Matrix Biol. 21, 461-465.
