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ADAMTS5 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Zusätzlich bieten wir Ihnen ADAMTS5 Kits (43) und ADAMTS5 Proteine (9) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige INS Antikörper) 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 (zeige ACAN Antikörper) and Vcan (zeige Vcan Antikörper) by an ADAMTS (zeige ADAMTS1 Antikörper) other than TS5.
Data suggest that ADAMTS-5 oligomerization is required for full aggrecanase (zeige ADAMTS4 Antikörper) 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 (zeige ACAN Antikörper) and brevican (zeige BCAN Antikörper) proteolysis is compensated in Adamts4 (zeige ADAMTS4 Antikörper)-/- or Adamts5-/- mice by ADAMTS (zeige ADAMTS1 Antikörper) proteoglycanase (zeige MMP3 Antikörper) family members but a threshold of versican (zeige Vcan Antikörper) proteolysis is sensitive to the loss of a single ADAMTS (zeige ADAMTS1 Antikörper) proteoglycanase (zeige MMP3 Antikörper) during spinal cord injury
The present study reveals ADAMT-5 expression by mast cells(MCs (zeige SMCP Antikörper)) 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 (zeige ADAMTS4 Antikörper)-generated proteoglycan (zeige Vcan Antikörper) fragments are produced after SCI.
RelA/p65 (zeige NFkBP65 Antikörper) is a potent transcriptional activator of ADAMTS5 in chondrocytes during osteoarthritis development.
Repair of biomechanically compromised tendons exhibiting midsubstance chondroid accumulation requires ADAMTS5.
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 (zeige COL11A1 Antikörper) 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 (zeige FST Antikörper).
Development of a monoclonal anti-ADAMTS-5 antibody that specifically blocks the interaction with LRP1 (zeige LRP1 Antikörper).
MMP-13 (zeige MMP13 Antikörper) may play a role on physiological turnover of cartilage extracellular matrix and that LRP1 (zeige LRP1 Antikörper) is a key modulator of extracellular levels of MMP-13 (zeige MMP13 Antikörper) and its internalization is independent of the levels of ADAMTS-4 (zeige ADAMTS4 Antikörper), -5 and TIMP-3 (zeige TIMP3 Antikörper).
The IL1B (zeige IL1B Antikörper)/AP-1 (zeige FOSB Antikörper)/miR (zeige MLXIP Antikörper)-30a/ADAMTS-5 axis regulates cartilage matrix degradation in osteoarthritis.
The findings suggest that miR (zeige MLXIP Antikörper)-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5 (zeige IGFBP5 Antikörper).
Results provide direct evidence indicating that Fibulin-2 (zeige FBLN2 Antikörper) 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 (zeige FBLN2 Antikörper) and the ADAMTSs metalloproteases.
Endoplasmic reticulum stress participates in the progress of senescence and apoptosis of osteoarthritic chondrocytes, which manifested in increased expression of ADAMTS5, MMP13 (zeige MMP13 Antikörper), and decreased COL2A1 (zeige COL2A1 Antikörper) expression.
The delayed activation of proMMPs and the relatively low cleavage efficiency of MMPs compared to ADAMTS5 (aggrecanase (zeige ADAMTS4 Antikörper)) explains the minor contribution of the MMP enzymes to aggrecan (zeige ACAN Antikörper) catabolism in vivo.
ADAMTS4 (zeige ADAMTS4 Antikörper) and ADAMTS5 are inhibited by alpha2-macroglobulin (zeige A2M Antikörper)
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 (zeige ADAMTS4 Antikörper) 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)