Mouse Cartilage oligomeric matrix protein(COMP) ELISA kit

May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7.

1. COMP could normally have a protective role against PASMC phenotype switching PMID: 28860005
2. these findings revealed the essential role of COMP in retarding the development of vascular aging and vascular smooth muscle cell senescence. PMID: 27498005
3. COMP deficiency drove macrophages toward the atherogenic phenotype and thereby aggravated atherosclerotic calcification. PMID: 27151399
4. COMP forms a complex with collagens intracellularly that is a prerequisite for collagen secretion. PMID: 26746240
5. The accumulation and thereby the functionality of thrombospondin in extracellular matrix is controlled by concentration-dependent, intermolecular "matrix trapping" mechanism. PMID: 25995382
6. COMP deficiency shortened tail-bleeding and clotting time and accelerated ferric-chloride-induced thrombosis. COMP specifically inhibited thrombin-induced platelet aggregation, activation, and retraction and the thrombin-mediated cleavage of fibrinogen. PMID: 26045608
7. COMP immunoreactivity was observed in about half of the investigated plaques from the ApoE null mice, mainly located along the intima-medial border. Plaques in the brachiocephalic artery from ApoE mice lacking COMP were increased in size with 54%. PMID: 25133350
8. study will facilitate better awareness of the differential diagnoses that might be associated with the PSACH/MED spectrum and subsequent care of PSACH/MED patients PMID: 24312420
9. The lack of arthritis, together with high levels of COMP-specific antibodies, in COMP-deficient mice indicates that susceptibility to arthritis is COMP specific and that endogenous expression of COMP in wild-type mice tolerizes B cells in vivo. PMID: 23754310
10. results imply that COMP is not a key upstream mediator of the anabolic effects of ML on the skeleton. PMID: 23098652
11. Lack of COMP and matrilin 3 leads to increased deposition of TIMP-3, which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13. PMID: 22378539
12. A novel form of chondrocyte stress triggered by the expression of a human-like mutation in COMP is central to the pathogenesis of pseudoachondroplasia. PMID: 22006726
13. reducing steady state levels of COMP mRNA alleviates intracellular retention of other extracellular matrix proteins associated with the pseudoachondroplasia cellular pathology PMID: 20421976
14. Data show that cartilage oligomeric matrix protein (COMP) promotes cell attachment via independent mechanisms involving cell surface CD47 and alphaVbeta3 integrin and that cell attachment to COMP induces formation of fascin-stabilized actin microspikes. PMID: 20033473
15. Cartilage oligomeric matrix protein-deficient mice have normal skeletal development. PMID: 12024046
16. Comp was expressed in tendon clone cells. PMID: 12837285
17. Negative regulation of transcription is an important mechanism for chondrocyte-specific expression of the COMP gene PMID: 15183430
18. ADAMTS-7 is the first metalloproteinase found to bind directly to and degrade COMP PMID: 16585064
19. COMP appears to be required for granulin PC cell-derived growth factor-mediated chondrocyte proliferation PMID: 17307734
20. a mutation in the C-terminal domain of COMP exerts a dominant-negative effect on both intra- and extracellular processes. PMID: 17588960
21. contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected PMID: 18191556
22. COMP-deficient mice develop an early onset collagen-induced arthritis and more severe arthritis during the chronic phase. PMID: 19014566

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Secreted, extracellular space, extracellular matrix.

Thrombospondin family

Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues.

KEGG: mmu:12845

STRING: 10090.ENSMUSP00000003659

UniGene: Mm.45071