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ADAM metallopeptidase with thrombospondin type 1 motif, 4

aggrecanase, ADAMTS-4, aggrecanase-1
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 lacks a C-terminal TS motif. It is responsible for the degradation of aggrecan, a major proteoglycan of cartilage, and brevican, a brain-specific extracellular matrix protein. The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ADAMTS, Aggrecan, thrombospondin-1, IL-1beta, CAN
Papers on aggrecanase
The imbalance between TIMP3 and matrix-degrading enzymes plays an important role in intervertebral disc degeneration.
Zhao et al., Shanghai, China. In Biochem Biophys Res Commun, Feb 2016
Collagen and aggrecan are major components of ECM; the degradation of ECM in intervertebral discs (IVDs) is closely related to the activities of collagenase and aggrecanase.
Chondrocytic EphrinB2 promotes cartilage destruction by osteoclasts in endochondral ossification.
Sims et al., Melbourne, Australia. In Development, Feb 2016
Cultured chondrocytes from Osx1Cre.EfnB2(Δ/Δ) neonatal mice showed impaired support of osteoclastogenesis but no significant change in RANKL 9 (Tnsf11) levels; instead Adamts4 levels were significantly lowered.
Anti-ADAMTS5 monoclonal antibodies: implications for aggrecanase inhibition in osteoarthritis.
Apte, Cleveland, United States. In Biochem J, Feb 2016
This work, together with other antibodies targeting ADAMTS5, offers diverse, high-affinity and, as far as can be determined, selective aggrecanase inhibitors.
Insulin Suppresses TNF-dependent Early Osteoarthritic Changes Associated with Obesity and Type 2 Diabetes.
Mooney et al., Durham, United States. In Arthritis Rheumatol, Jan 2016
While TNF markedly increased expression and release of MMP1, MMP13, and ADAMTS4 by FLSs, insulin selectively inhibited the effects by >50%.
hsa-miR-15a exerts protective effects against osteoarthritis by targeting aggrecanase-2 (ADAMTS5) in human chondrocytes.
Weng et al., Beijing, China. In Int J Mol Med, Jan 2016
The expression levels of hsa-miR-15a and A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (ADAMTS5, also known as aggrecanase-2) were measured by reverse transcription-quantitative polymerase chain reaction (RT-qPCR) in both OA and normal chondrocytes.
Alendronate Prevents Intervertebral Disc Degeneration Adjacent to a Lumbar Fusion in Ovariectomized Rats.
Zhang et al., Tangshan, China. In Spine (phila Pa 1976), Nov 2015
ALN also significantly decreased Col-I, MMP-13, and ADAMTS-4 expression and increased Col-II and Aggrecan expression in the disc matrix (P < 0.05).
Advances in understanding cartilage remodeling.
Xu et al., Boston, United States. In F1000res, 2014
In this brief review, we focus on the discussion of some current "controversial" observations in articular cartilage degeneration: (1) the biological effect of transforming growth factor-beta 1 on developing and mature articular cartilages, (2) the question of whether aggrecanase 1 (ADAMTS4) and aggrecanase 2 (ADAMTS5) are key enzymes in articular cartilage destruction, and (3) chondrocytes versus chondron in the development of osteoarthritis.
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family.
Edwards et al., Norwich, United Kingdom. In Genome Biol, 2014
The human family includes 19 members that can be sub-grouped on the basis of their known substrates, namely the aggrecanases or proteoglycanases (ADAMTS1, 4, 5, 8, 9, 15 and 20), the procollagen N-propeptidases (ADAMTS2, 3 and 14), the cartilage oligomeric matrix protein-cleaving enzymes (ADAMTS7 and 12), the von-Willebrand Factor proteinase (ADAMTS13) and a group of orphan enzymes (ADAMTS6, 10, 16, 17, 18 and 19).
Current and emerging therapeutic strategies for preventing inflammation and aggrecanase-mediated cartilage destruction in arthritis.
McCulloch et al., Australia. In Arthritis Res Ther, 2013
Importantly, we highlight their potential to indirectly regulate ADAMTS aggrecanase activity through their targeting of inflammatory mediators, thus providing insight into a mechanism by which they might inhibit cartilage destruction to slow or halt radiographic progression of the disease.
Proteoglycans and diseases of soft tissues.
Halper, Athens, United States. In Adv Exp Med Biol, 2013
Degradation with aggrecanase is responsible for the appearance of different forms of aggrecan and versican in different parts of the tendon where these cleaved forms play different roles.
MMP proteolysis of the human extracellular matrix protein aggrecan is mainly a process of normal turnover.
Hansson et al., Lund, Sweden. In Biochem J, 2012
Data suggest that cleavage of aggrecan by matrix metalloproteinases in knee cartilage from injured or osteoarthritic subjects is low compared with cleavage by aggrecanase-1 (at least early in osteoarthritis, as suggested by other evidence).
Expression of ADAMTS-2, -3, -13, and -14 in culprit coronary lesions in patients with acute myocardial infarction or stable angina.
Park et al., Seoul, South Korea. In J Thromb Thrombolysis, 2012
ADAMTS-2, -3, and -13 expression, but not that of ADAMTS-14, are increased in plaques causing AMI compared those associated with stable angina.
Interleukin-6 upregulates expression of ADAMTS-4 in fibroblast-like synoviocytes from patients with rheumatoid arthritis.
Sawai et al., Morioka, Japan. In Int J Rheum Dis, 2012
Suggest IL-6 may participate in cartilage destruction in rheumatoid arthritis as an inducer of ADAMTS-4 expression from synoviocytes.
Association of serum a disintegrin and metalloproteinase with thrombospodin motif 4 levels with the presence and severity of coronary artery disease.
Cui et al., Jinan, China. In Coron Artery Dis, 2011
Serum ADAMTS4 levels are associated with the presence and the severity of coronary artery disease.
Regulation of aggrecanases from the ADAMTS family and aggrecan neoepitope formation during in vitro chondrogenesis of human mesenchymal stem cells.
Richter et al., Heidelberg, Germany. In Eur Cell Mater, 2011
Data show that the expression of ADAMTS4, 9, 16 and was up-regulated during chondrogenesis, ADAMTS1 and 5 were down-regulated.
Hypoxia-inducible factor-2alpha is a catabolic regulator of osteoarthritic cartilage destruction.
Chun et al., Kwangju, South Korea. In Nat Med, 2010
HIF-2alpha directly induces the expression in chondrocytes of genes encoding catabolic factors, including matrix metalloproteinases (MMP1, MMP3, MMP9, MMP12 and MMP13), aggrecanase-1 (ADAMTS4), nitric oxide synthase-2 (NOS2) and prostaglandin-endoperoxide synthase-2 (PTGS2).
Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis.
Pap et al., Hannover, Germany. In Nat Med, 2009
The mechanisms of ADAMTS-5 activation and their links to the pathogenesis of osteoarthritis remain poorly understood, but syndecans have been shown to be involved in the activation of ADAMTS-4 (ref.
ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.
Fosang et al., Melbourne, Australia. In Nature, 2005
Although ADAMTS4 and 5 are expressed in joint tissues, and are known to be efficient aggrecanases in vitro, the exact contribution of these two enzymes to cartilage pathology is unknown.
Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis.
Morris et al., Cambridge, United States. In Nature, 2005
Here we describe experiments with a genetically modified mouse in which the catalytic domain of ADAMTS5 (aggrecanase-2) was deleted.
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins.
Arner et al., Wilmington, United States. In Science, 1999
Aggrecanase-1 [a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4)] is a member of the ADAMTS protein family that cleaves aggrecan at the glutamic acid-373-alanine-374 bond.
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