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ADAMTS5 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Additionally we are shipping ADAMTS5 Kits (43) and ADAMTS5 Proteins (9) and many more products for this protein.
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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 (show INS Antibodies) sensitivity was improved in the ADAMTS5-J KO mice, and they were protected against non-alcoholic steatohepatitis in the DIO model
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.
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
TS5 protein functions to suppress glucose uptake in adipose-derived stromal cells and thereby inhibits the synthesis, and promotes the intracellular degradation of Acan (show ACAN Antibodies) and Vcan (show Vcan Antibodies) by an ADAMTS (show ADAMTS1 Antibodies) other than TS5.
Data suggest that ADAMTS-5 oligomerization is required for full aggrecanase (show ADAMTS4 Antibodies) activity in vitro and in situ (as seen in knee joint of mouse model of inflammatory arthritis); thus, blocking oligomerization inhibits ADAMTS-5 activity.
aggrecan (show ACAN Antibodies) and brevican (show BCAN Antibodies) proteolysis is compensated in Adamts4 (show ADAMTS4 Antibodies)-/- or Adamts5-/- mice by ADAMTS (show ADAMTS1 Antibodies) proteoglycanase (show MMP3 Antibodies) family members but a threshold of versican (show Vcan Antibodies) proteolysis is sensitive to the loss of a single ADAMTS (show ADAMTS1 Antibodies) proteoglycanase (show MMP3 Antibodies) during spinal cord injury
The present study reveals ADAMT-5 expression by mast cells(MCs (show SMCP Antibodies)) and that MC activation regulates the expression of the protease, thus implicating the ADAMT-5 of protease in MC function.
Western blot analyses indicated that aggrecanase (show ADAMTS4 Antibodies)-generated proteoglycan (show Vcan Antibodies) fragments are produced after SCI.
RelA/p65 (show NFkBP65 Antibodies) is a potent transcriptional activator of ADAMTS5 in chondrocytes during osteoarthritis development.
Repair of biomechanically compromised tendons exhibiting midsubstance chondroid accumulation requires ADAMTS5.
Data suggest that 3prime untranslated region of ADAMTS5 mRNA contains 'seedmatched-sequence' for hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-140-3p (microRNA-140-3p); in chondrocytes from articular cartilage of patients with knee osteoarthritis, interleukin-1beta up-regulates expression of ADAMTS5 and down-regulates expression of hsa (show CD24 Antibodies)-miR (show MLXIP Antibodies)-140-3p. (ADAMTS5 = ADAM metallopeptidase with thrombospondin type 1 motif 5 A)
A novel genetic variant in ADAMTS5 is associated with bicuspid aortic valve disease.
expression by synovial cells induced by hemoglobin at low doses, suggesting a possible role for hemoglobin in cartilage damage after intra-articular hemorrhage
The SNPs rs1337185 in COL11A1 (show COL11A1 Antibodies) and rs162509 in ADAMTS5 are associated with susceptibility to lumbar disc degeneration. The C allele of rs1337185 is risky for patients who are affected by lumbar pathologies such as disc herniation, stenosis and spondylolisthesis. The G allele of rs16250 represents a risk factor for the development of disc herniation.
ADAMTS5 is hypermethylated and inhibits cancer cells invasion and migration in colorectal cancer, and correlates with OS and DFS (show FST Antibodies).
Development of a monoclonal anti-ADAMTS-5 antibody that specifically blocks the interaction with LRP1 (show LRP1 Antibodies).
MMP-13 (show MMP13 Antibodies) may play a role on physiological turnover of cartilage extracellular matrix and that LRP1 (show LRP1 Antibodies) is a key modulator of extracellular levels of MMP-13 (show MMP13 Antibodies) and its internalization is independent of the levels of ADAMTS-4 (show ADAMTS4 Antibodies), -5 and TIMP-3 (show TIMP3 Antibodies).
The IL1B (show IL1B Antibodies)/AP-1 (show FOSB Antibodies)/miR (show MLXIP Antibodies)-30a/ADAMTS-5 axis regulates cartilage matrix degradation in osteoarthritis.
The findings suggest that miR (show MLXIP Antibodies)-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5 (show IGFBP5 Antibodies).
Results provide direct evidence indicating that Fibulin-2 (show FBLN2 Antibodies) is a novel substrate of ADAMTS-5 and that this proteolysis could alter the cellular microenvironment affecting the balance between protumor and antitumor effects associated to both Fibulin-2 (show FBLN2 Antibodies) and the ADAMTSs metalloproteases.
The delayed activation of proMMPs and the relatively low cleavage efficiency of MMPs compared to ADAMTS5 (aggrecanase (show ADAMTS4 Antibodies)) explains the minor contribution of the MMP enzymes to aggrecan (show ACAN Antibodies) catabolism in vivo.
ADAMTS4 (show ADAMTS4 Antibodies) and ADAMTS5 are inhibited by alpha2-macroglobulin (show A2M Antibodies)
identified multiple conserved amino acids within regions N- and C-terminal to the site of scission that may influence enzyme-substrate recognition, and may interact with exosites on ADAMTS-4 (show ADAMTS4 Antibodies) and ADAMTS-5
Co-culture of mechanically injured cartilage with joint capsule tissue alters chondrocyte expression patterns and increases ADAMTS5 production.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage.
ADAM metallopeptidase with thrombospondin type 1 motif, 5
, a disintegrin and metalloproteinase with thrombospondin motifs 5-like
, A disintegrin and metalloproteinase with thrombospondin motifs 5
, ADAM-TS 5
, a disintegrin and metalloproteinase with thrombospondin motifs 11
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2)
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2)