Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage (Q34123993)

31 July 2017

title

Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage (English)

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31 July 2017

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Anne-Marie Malfait

1

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31 July 2017

Rui-Qin Liu

2

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31 July 2017

Kosei Ijiri

3

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31 July 2017

Setsuro Komiya

4

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31 July 2017

Micky D Tortorella

5

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31 July 2017

language of work or name

English

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publication date

15 April 2002

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Journal of Biological Chemistry

31 July 2017

number of pages

8

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based on heuristic

inferred from page(s)

published in

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31 July 2017

volume

277

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31 July 2017

issue

25

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31 July 2017

page(s)

22201-22208

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Extended and globular protein domains in cartilage proteoglycans

31 July 2017

cites work

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https://api.crossref.org/works/10.1074/JBC.M200431200

Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Mechanism of catabolism of aggrecan by articular cartilage

21 January 2018

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https://api.crossref.org/works/10.1074/JBC.M200431200

Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Characterization of aggrecan retained and lost from the extracellular matrix of articular cartilage. Involvement of carboxyl-terminal processing in the catabolism of aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan

21 January 2018

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Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)

21 January 2018

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The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1.

21 January 2018

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https://api.crossref.org/works/10.1074/JBC.M200431200

Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints

21 January 2018

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Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing i

21 January 2018

1 reference

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Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro

21 January 2018

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Development of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids

21 January 2018

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Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue.

21 January 2018

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ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

21 January 2018

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n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation

21 January 2018

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Development and reversal of a proteoglycan aggregation defect in normal canine knee cartilage after immobilization

21 January 2018

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Cartilage proteoglycan alterations in an experimentally induced model of rabbit osteoarthritis

21 January 2018

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Ongoing trials with matrix metalloproteinase inhibitors

21 January 2018

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The clinical potential of matrix metalloproteinase inhibitors in the rheumatic disorders

21 January 2018

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Thirty-six years in the clinic without an MMP inhibitor. What hath collagenase wrought?

21 January 2018

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Metalloproteinase inhibitors: new opportunities for the treatment of rheumatoid arthritis and osteoarthritis

21 January 2018

1 reference

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Design and synthesis of a series of (2R)-N(4)-hydroxy-2-(3-hydroxybenzyl)-N(1)- [(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide derivatives as potent, selective, and orally bioavailable aggrecanase inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M200431200

21 January 2018

Identifiers

DOI

10.1074/JBC.M200431200

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31 July 2017

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