Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes (Q40600622)

21 September 2017

title

Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes (English)

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21 September 2017

Micky D Tortorella

1

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21 September 2017

Elizabeth C Arner

2

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21 September 2017

Robert Hills

3

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21 September 2017

Alan Easton

4

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21 September 2017

Jennifer Korte-Sarfaty

5

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21 September 2017

Kam Fok

6

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21 September 2017

Arthur J Wittwer

7

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21 September 2017

Rui-Qin Liu

8

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21 September 2017

Anne-Marie Malfait

9

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21 September 2017

language of work or name

English

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publication date

7 January 2004

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Journal of Biological Chemistry

21 September 2017

number of pages

8

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based on heuristic

inferred from page(s)

published in

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21 September 2017

volume

279

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21 September 2017

issue

17

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21 September 2017

page(s)

17554-17561

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Extended and globular protein domains in cartilage proteoglycans

21 September 2017

cites work

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https://api.crossref.org/works/10.1074/JBC.M313041200

Mechanism of catabolism of aggrecan by articular cartilage

21 January 2018

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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.M313041200

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.M313041200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

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/10.1074/JBC.M313041200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

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/10.1074/JBC.M313041200

Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

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

21 January 2018

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https://api.crossref.org/works/10.1074/JBC.M313041200

Pathologic indicators of degradation and inflammation in human osteoarthritic cartilage are abrogated by exposure to n-3 fatty acids.

21 January 2018

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Expression and regulation of aggrecanase in arthritis: the role of TGF-beta

21 January 2018

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TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix

21 January 2018

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Protease inhibitors in inflammatory synovial effusions

21 January 2018

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https://api.crossref.org/works/10.1074/JBC.M313041200

α2‐Macroglobulin: A Sensor for Proteolysis

21 January 2018

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The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

21 January 2018

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Further characterization of the covalent linking reaction of α2-macroglobulin

21 January 2018

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https://api.crossref.org/works/10.1074/JBC.M313041200

ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage

21 January 2018

1 reference

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

21 January 2018

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Comparison of the inhibition of thrombin by three plasma protease inhibitors

21 January 2018

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Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

21 January 2018

1 reference

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The electrophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin molecule

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

ADAMTS4 cleaves at the aggrecanase site (Glu373-Ala374) and secondarily at the matrix metalloproteinase site (Asn341-Phe342) in the aggrecan interglobular domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

Autocatalytic cleavage of ADAMTS-4 (Aggrecanase-1) reveals multiple glycosaminoglycan-binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

Truncation of the amino-terminus of the recombinant aggrecan rAgg1mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

Molecular markers for osteoarthritis: the road ahead

21 January 2018

1 reference

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The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074/JBC.M313041200

21 January 2018

Identifiers

DOI

10.1074/JBC.M313041200

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21 September 2017

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