Mouse A disintegrin and metalloproteinase with thrombospondin motifs 5(ADAMTS5) ELISA kit

Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that shows proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. Participates in the development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.

1. ADAMTS5 plays a functional role in development of brown adipose tissue and browning of white adipose tissue. PMID: 28702327
2. Energy expenditure and thermogenesis were not significantly different between KO and WT ADAMTS5-J mice (in contrast to somewhat enhanced levels in ADAMTS5-P mice). Insulin sensitivity was improved in the ADAMTS5-J KO mice, and they were protected against non-alcoholic steatohepatitis in the DIO model PMID: 29293679
3. Adamts5(-/-) mice were protected from hepatic mitochondrial dysfunction, as indicated by increased mitochondrial respiratory chain complex activity, higher ATP levels and higher expression of antioxidant enzymes. Absence of ADAMTS5 preserves liver integrity in a diet-induced obesity model. PMID: 27254774
4. research emphasises the importance of ADAMTS5 expression in the control of influenza virus infection and highlights the potential for development of ADAMTS5-based therapeutic strategies to reduce morbidity and mortality PMID: 27855162
5. TS5 protein functions to suppress glucose uptake in adipose-derived stromal cells and thereby inhibits the synthesis, and promotes the intracellular degradation of Acan and Vcan by an ADAMTS other than TS5. PMID: 25840345
6. Data suggest that ADAMTS-5 oligomerization is required for full aggrecanase activity in vitro and in situ (as seen in knee joint of mouse model of inflammatory arthritis); thus, blocking oligomerization inhibits ADAMTS-5 activity. PMID: 26668318
7. aggrecan and brevican proteolysis is compensated in Adamts4-/- or Adamts5-/- mice by ADAMTS proteoglycanase family members but a threshold of versican proteolysis is sensitive to the loss of a single ADAMTS proteoglycanase during spinal cord injury PMID: 25101296
8. The present study reveals ADAMT-5 expression by mast cells(MCs) and that MC activation regulates the expression of the protease, thus implicating the ADAMT-5 of protease in MC function. PMID: 23154421
9. Western blot analyses indicated that aggrecanase-generated proteoglycan fragments are produced after SCI. PMID: 23562508
10. RelA/p65 is a potent transcriptional activator of ADAMTS5 in chondrocytes during osteoarthritis development. PMID: 23963448
11. Repair of biomechanically compromised tendons exhibiting midsubstance chondroid accumulation requires ADAMTS5. PMID: 23754494
12. this study identified, for the first time, several genes that have an ADAMTS-5-independent role in osteoarthritis(OA), identifying them as possible OA initiation candidates. PMID: 23436205
13. The serine protease tissue plasminogen activator (tPA) and two matrix metalloproteinases, ADAMTS-4 and ADAMTS-5, were identified as Reelin cleaving enzymes. PMID: 23082219
14. Versican processing by ADAMTS5 and ADAMTS15 contribute to muscle fiber formation. PMID: 23233679
15. the first evidence implicating ADAMTS-5 in the regulation of proteoglycan turnover and lipoprotein retention in atherosclerosis. PMID: 22493487
16. The role of ADAMTS5 in tendon is to remove pericellular and interfibrillar aggrecan to maintain the molecular architecture responsible for normal tissue function. PMID: 21928430
17. Adamts5 induction in joint components other than cartilage, and its post-translational activation by PACE4 and/or furin may be important in the pathophysiology of arthritis. PMID: 21800360
18. Matrilin-4 is processed by ADAMTS-5 in late Golgi vesicles present in growth plate chondrocytes of defined differentiation state PMID: 21539915
19. a physiological function of ADAMTS5 in dermal fibroblasts is to maintain optimal versican content and PCM volume by continually trimming versican in hyaluronan-versican aggregates. PMID: 21828051
20. Altered versican cleavage in ADAMTS5 deficient mice; a novel etiology of myxomatous valve disease PMID: 21749862
21. ADAMTS5 ablation did not eliminate aggrecanase activity from the articular cartilage but blocked fibrosis and resulted in the accumulation of aggrecan in the articular cartilage. PMID: 21337391
22. extracellular matrix degrading enzyme PMID: 11831030
23. ADAMTS1, ADAMTS4, and ADAMTS5 are expressed in patterns that relate to the expression pattern of versican in granulosa cells of small follicles, expanded cumulus cell-oocyte complexes, and endothelial cells of the ovary. PMID: 15659705
24. After surgically induced joint instability, there was significant reduction in the severity of cartilage destruction in the ADAMTS5 knockout mice compared with wild-type mice PMID: 15800624
25. ADAMTS5 is the major aggrecanase in mouse cartilage, both in vitro and in a mouse model of inflammatory arthritis PMID: 15800625
26. ADAMTS-5 is entirely responsible for cleavage in the interglobular domain, but cleavage in the chondroitin sulfate-rich region may be driven by ADAMTS-4 PMID: 17255106
27. aggrecan loss with aggrecan processing in mice with single and double deletions of ADAMTS-4 and -5 activity (Deltacat) PMID: 17938173
28. Deletion of ADAMTS-4/5 provided significant protection against proteoglycan degradation ex vivo and decreased the severity of murine osteoarthritis PMID: 17968948
29. Data show that expression of Adamts5 during neuromuscular development and in smooth muscle cells coincides with the broadly distributed proteoglycan versican, an ADAMTS5 substrate. PMID: 19250981
30. Fibroblast growth factor 2 is an intrinsic chondroprotective agent that suppresses ADAMTS-5 and delays cartilage degradation in murine osteoarthritis. PMID: 19565481
31. The occurrence of less severe osteoarthritis-like cartilage destruction in both syndecan-4-deficient mice and syndecan-4-specific antibody-treated wild-type mice results from a marked decrease in ADAMTS-5 activity. PMID: 19684582
32. show that combinatorial mouse alleles for the secreted metalloproteases Adamts5, Adamts20 (bt), and Adamts9 result in fully penetrant soft-tissue syndactyly. PMID: 19922873

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Secreted, extracellular space, extracellular matrix.

Expressed in skeletal muscle.

KEGG: mmu:23794

STRING: 10090.ENSMUSP00000023611

UniGene: Mm.112933