MMP proteolysis of the human extracellular matrix protein aggrecan is mainly a process of normal turnover. (Q53164462)

12 May 2018

title

MMP proteolysis of the human extracellular matrix protein aggrecan is mainly a process of normal turnover. (English)

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12 May 2018

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André Struglics

1

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12 May 2018

Maria Hansson

series ordinal

2

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12 May 2018

language of work or name

English

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publication date

1 September 2012

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12 May 2018

number of pages

11

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based on heuristic

inferred from page(s)

published in

Biochemical Journal

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12 May 2018

volume

446

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12 May 2018

issue

2

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12 May 2018

page(s)

213-223

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12 May 2018

Mechanisms involved in cartilage proteoglycan catabolism

cites work

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https://api.crossref.org/works/10.1042%2FBJ20120274

Aggrecan protects cartilage collagen from proteolytic cleavage

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Synovial fluid level of aggrecan ARGS fragments is a more sensitive marker of joint disease than glycosaminoglycan or aggrecan levels: a cross-sectional study

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Western blot quantification of aggrecan fragments in human synovial fluid indicates differences in fragment patterns between joint diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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/10.1042%2FBJ20120274

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4).

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

A comparison of different purification methods of aggrecan fragments from human articular cartilage and synovial fluid

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by m-calpain

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Calpain is involved in C-terminal truncation of human aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Cathepsin B: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Identification of a novel HtrA1-susceptible cleavage site in human aggrecan: evidence for the involvement of HtrA1 in aggrecan proteolysis in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Mechanism of proteoglycan aggregate degradation in cartilage stimulated with oncostatin M.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Cathepsin D cleaves aggrecan at unique sites within the interglobular domain and chondroitin sulfate attachment regions that are also cleaved when cartilage is maintained at acid pH.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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/10.1042%2FBJ20120274

Simultaneous preparation and quantitation of proteoglycans by precipitation with alcian blue.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Estimation of the identity of proteolytic aggrecan fragments using PAGE migration and Western immunoblot.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

A human-specific polymorphism in the coding region of the aggrecan gene. Variable number of tandem repeats produce a range of core protein sizes in the general population

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

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

https://api.crossref.org/works/10.1042%2FBJ20120274

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20120274

21 January 2018

Identifiers

DOI

10.1042/BJ20120274

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12 May 2018

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12 May 2018