Search results for ADAMTS1

Showing 17 results out of 36

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Protein (15 results from a total of 34)

Identifier: R-HSA-3791292
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: ADAMTS1: Q9UHI8
Identifier: R-HSA-5173121
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q9UHI8
Identifier: R-HSA-5172971
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: ADAMTS1: Q9UHI8
Identifier: R-HSA-5173006
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q9UHI8
Identifier: R-HSA-5173249
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8WXS8
Identifier: R-HSA-5173148
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8TE57
Identifier: R-HSA-5172973
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8TE58
Identifier: R-HSA-5173034
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8TE56
Identifier: R-HSA-5173161
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8TE59
Identifier: R-HSA-5173116
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q8TE60
Identifier: R-HSA-5173241
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: P58397
Identifier: R-HSA-5173236
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q9H324
Identifier: R-HSA-5173292
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: Q76LX8
Identifier: R-HSA-3791290
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: ADAMTS18: Q8TE60
Identifier: R-HSA-3791308
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: ADAMTS16: Q8TE57

Reaction (2 results from a total of 2)

Identifier: R-NUL-2533988
Species: Bos taurus, Homo sapiens
Compartment: extracellular region
The majority of aggrecan fragments present in synovial fluid of OA patients are cleaved at Glu392-Ala393 (numbered here according to the human UniProt sequence, these residues referred to as Glu373-Ala374 in most literature) in the IGD (Sandy et al. 1992). ADAMTS5 (aggrecanase-2, Abbaszade et al. 1999) and to a lesser extent ADAMTS4 (aggrecanase-1, Tortorella et al. 1999) are primarrily responsible (Gendron et al. 2007).
Identifier: R-HSA-1592310
Species: Homo sapiens
Compartment: extracellular region
Aggrecan (large aggregating proteoglycan, chondroitin sulfate proteoglycan 1) is a major structural component of cartilage, particularly articular cartilage. The core protein has over 100 chains of chondroitin sulphate and keratan sulphate giving a MWt of about 250 kDa. The core protein has 2 N-terminal globular domains G1 and G2 and a C-terminal globular G3 domain. G2 and G3 are separated by a region heavily modified with negatively charged glycosaminoglycans (GAGs). The two main modifier moieties keratan sulfate (KS) and chondroitin sulfate (CS) are arranged into two CS regions and a KS-rich region. The 15-kDa interglobular linker (IGD) between the N-terminal G1 and G2 domains is particularly susceptible to proteolysis (Caterson et al. 2000). Degradation in this region is associated with the development of osteoarthritis (Troeberg & Nagase 2012). Members of the ADAM (A Disintegrin And Metalloprotease) protein family are responsible for this cleavage (East et al. 2007, Huang & Wu 2008).

Matrix metalloproteinase (MMP) 3 was the first protease found to degrade aggrecan. It preferentially cleaves the Asn341~Phe342 bond (Fosang et al. 1991). MMP2, 7, 9 (Fosang et al. 1992), 1, 8 (Fosang et al. 1993), 13 (Fosang et al. 1996) and 12 (Durigova et al. 2011) were all found to be able to cleave this site as well as others towards the C-terminus. However, the the majority of aggrecan fragments present in synovial fluid of OA patients are cleaved at Glu392-Ala373 (numbered here according to the UniProt sequence, these residues referred to as Glu373-Ala374 in most literature) in the IGD (Sandy et al. 1992). ADAMTS5 (aggrecanase-2, Abbaszade et al. 1999) and to a lesser extent ADAMTS4 (aggrecanase-1, Tortorella et al. 1999) are primarrily responsible (Gendron et al. 2007) though the preferred cleavage sites of these are in the CS-2 domain. ADAMTS1 (Kuno et al. 2000, Rodriques-Manzaneque et al. 2002), 9, (Somerville et al. 2003), 8 (Colins-Racie 2004), 16 and 18 (Zeng et al. 2006) can also degrade aggrecan in vitro.
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