Results 11 to 20 of about 15,848 (207)
ADAMTS expression in colorectal cancer. [PDF]
PLoS ONE, 2015 ADAMTSs are a family of secreted proteinases that share the metalloproteinase domain with matrix metalloproteinases (MMPs). By acting on a large panel of extracellular substrates, they control several cell functions such as fusion, adhesion ...
Serafula Filou +8 more
doaj +5 more sources
Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3 [PDF]
Journal of Biological Chemistry, 2002 The processing of amino- and carboxyl-propeptides of fibrillar collagens is required to generate collagen monomers that correctly assemble into fibrils. Mutations in the ADAMTS2 gene, the aminopropeptidase of procollagen I and II, result in the accumulation of non-fully processed type I procollagen, causing human Ehlers-Danlos syndrome type VIIC and ...
Colige, Alain +8 more
openaire +3 more sources
Regulation of ADAMTS Proteases [PDF]
Frontiers in Molecular Biosciences, 2021 A disintegrin and metalloprotease with thrombospondin type I motifs (ADAMTS) proteases are secreted metalloproteinases that play key roles in the formation, homeostasis and remodeling of the extracellular matrix (ECM).
Keron W. J. Rose +3 more
doaj +3 more sources
ADAMTS-9 in Mouse Cartilage Has Aggrecanase Activity That Is Distinct from ADAMTS-4 and ADAMTS-5 [PDF]
International Journal of Molecular Sciences, 2019 A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 are the principal aggrecanases in mice and humans; however, mice lacking the catalytic domain of both enzymes (TS-4/5∆cat) have no skeletal phenotype, suggesting there is an alternative aggrecanase for modulating normal growth and development in these mice.
Fraser M. Rogerson +6 more
openaire +5 more sources
ADAMTS-15 Has a Tumor Suppressor Role in Prostate Cancer
Biomolecules, 2020 Extracellular matrix remodeling has emerged as an important factor in many cancers. Proteoglycans, including versican (VCAN), are regulated via cleavage by the proteolytic actions of A Disintegrin-like And Metalloproteinase domain with Thrombospondin-1 ...
Marley J. Binder +4 more
doaj +2 more sources
Expression of ADAMTS-1, ADAMTS-4, ADAMTS-5 and TIMP3 by hepatocellular carcinoma cell lines
International Journal of Oncology, 2012 Little is known about the expression or role of ADAMTS-1, -4 and -5 and their endogenous inhibitor TIMP3 in the liver in physiological and pathological conditions. Their expression was, therefore, investigated in the hepatocellular carcinoma cell lines HepG2 and HuH-7 using qRT-PCR and western blotting, and their cellular localisation by ...
Sharon L, Turner +4 more
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ADAMTS-5: The story so far [PDF]
European Cells & Materials, 2008 The recent discovery of ADAMTS-5 as the major aggrecanase in mouse cartilage came as a surprise. A great deal of research had focused on ADAMTS-4 and much less was known about the regulation, expression and activity of ADAMTS-5. Two years on, it is still
A J Fosang +3 more
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The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
Open Access Rheumatology: Research and Reviews, 2009 Edward A Lin1, Chuan-ju Liu1,21Department of Orthopaedic Surgery, 2Department of Cell Biology, New York University School of Medicine, New York, NY, USAAbstract: The a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) comprise a ...
Edward A Lin, Chuan-ju Liu
doaj +6 more sources
Purification and Activity Determination of ADAMTS-4 and ADAMTS-5 and Their Domain Deleted Mutants [PDF]
, 2019 A disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-4 (ADAMTS-4) and ADAMTS-5 are zinc-dependent metalloproteinases that are involved in the maintenance of cartilage extracellular matrix (ECM) and are currently considered the major aggrecanases in the development of osteoarthritis.
Fowkes, MM, Lim, NH
core +5 more sources
Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4.
The Journal of biological chemistry, 2007 Aggrecanases have been characterized as proteinases that cleave the Glu373-Ala374 bond of the aggrecan core protein, and they are multidomain metalloproteinases belonging to the ADAMTS (adamalysin with thrombospondin type 1 motifs) family. The first aggrecanases discovered were ADAMTS-4 (aggrecanase 1) and ADAMTS-5 (aggrecanase 2).
Gendron, Christi +7 more
openaire +4 more sources