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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 Antibodies (122) and ADAMTS5 Kits (38) 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 Proteins) 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 Proteins) and Vcan (show Vcan Proteins) by an ADAMTS (show ADAMTS1 Proteins) other than TS5.
Data suggest that ADAMTS-5 oligomerization is required for full aggrecanase (show ADAMTS4 Proteins) 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 Proteins) and brevican (show BCAN Proteins) proteolysis is compensated in Adamts4 (show ADAMTS4 Proteins)-/- or Adamts5-/- mice by ADAMTS (show ADAMTS1 Proteins) proteoglycanase (show MMP3 Proteins) family members but a threshold of versican (show Vcan Proteins) proteolysis is sensitive to the loss of a single ADAMTS (show ADAMTS1 Proteins) proteoglycanase (show MMP3 Proteins) during spinal cord injury
The present study reveals ADAMT-5 expression by mast cells(MCs (show SMCP Proteins)) 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 Proteins)-generated proteoglycan (show Vcan Proteins) fragments are produced after SCI.
RelA/p65 (show NFkBP65 Proteins) is a potent transcriptional activator of ADAMTS5 in chondrocytes during osteoarthritis development.
Repair of biomechanically compromised tendons exhibiting midsubstance chondroid accumulation requires ADAMTS5.
Development of a monoclonal anti-ADAMTS-5 antibody that specifically blocks the interaction with LRP1 (show LRP1 Proteins).
MMP-13 (show MMP13 Proteins) may play a role on physiological turnover of cartilage extracellular matrix and that LRP1 (show LRP1 Proteins) is a key modulator of extracellular levels of MMP-13 (show MMP13 Proteins) and its internalization is independent of the levels of ADAMTS-4 (show ADAMTS4 Proteins), -5 and TIMP-3 (show TIMP3 Proteins).
The IL1B (show IL1B Proteins)/AP-1 (show FOSB Proteins)/miR (show MLXIP Proteins)-30a/ADAMTS-5 axis regulates cartilage matrix degradation in osteoarthritis.
The findings suggest that miR (show MLXIP Proteins)-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5 (show IGFBP5 Proteins).
Results provide direct evidence indicating that Fibulin-2 (show FBLN2 Proteins) 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 Proteins) 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 (show MMP13 Proteins), and decreased COL2A1 (show COL2A1 Proteins) expression.
Single Nucleotide Variants of Candidate Genes in Aggrecan (show ACAN Proteins) Metabolic Pathway Are Associated with Lumbar Disc Degeneration and Modic Changes
RREB1 cooperates with noncoding RNA linc-ADAMTS5 to inhibit ADAMTS5 expression, thereby affecting degeneration of the extracellular matrix (ECM (show MMRN1 Proteins)) of the intervertebral disc.
Matrilin 2 (show MATN2 Proteins) accumulation associated with relative ADAMTS5 deficiency may contribute to the mechanism underlying calcific aortic valve disease progression.
In osteoarthritis (OA) chondrocytes, hydrostatic pressure (HP) restores the expression levels of some miRNAs, downregulates MMP-13 (show MMP13 Proteins), ADAMTS-5, and HDAC-4 (show HDAC4 Proteins), and modulates the Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) pathway activation.
The delayed activation of proMMPs and the relatively low cleavage efficiency of MMPs compared to ADAMTS5 (aggrecanase (show ADAMTS4 Proteins)) explains the minor contribution of the MMP enzymes to aggrecan (show ACAN Proteins) catabolism in vivo.
ADAMTS4 (show ADAMTS4 Proteins) and ADAMTS5 are inhibited by alpha2-macroglobulin (show A2M Proteins)
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 Proteins) 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)