Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein (Q24528169)

2

G

Murphy

1 reference

20 October 2023

C E Hughes

3

C E

Hughes

1 reference

20 October 2023

J S Mort

4

J S

Mort

1 reference

20 October 2023

P J Roughley

5

P J

The primary structure of human cartilage link protein

Roughley

1 reference

20 October 2023

language of work or name

English

0 references

publication date

15 October 1993

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published in

Biochemical Journal

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volume

295 ( Pt 2)

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page(s)

595-8

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cites work

1 reference

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage

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Degradation of proteoglycan aggregate by a cartilage metalloproteinase. Evidence for the involvement of stromelysin in the generation of link protein heterogeneity in situ

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Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins

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The matrix-degrading metalloproteinases

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The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B

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Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage

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The role of link-protein in the structure of cartilage proteoglycan aggregates

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Neutral metalloproteases and age related changes in human articular cartilage

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Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities

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The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.

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Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage

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Metalloproteinase digestion of cartilage proteoglycan. Pattern of cleavage by stromelysin and susceptibility to collagenase

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Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).

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Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin.

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Monoclonal antibodies as probes for determining the microheterogeneity of the link proteins of cartilage proteoglycan

29 November 2018

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Polypeptides of the tail fibres of bacteriophage T4

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12 December 2020

The heterogeneity of link proteins isolated from human articular cartilage proteoglycan aggregates

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12 December 2020

Assay of proteoglycan populations using agarose-polyacrylamide gel electrophoresis

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12 December 2020

Link protein interactions with hyaluronate and proteoglycans. Characterization of two distinct domains in bovine cartilage link proteins

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12 December 2020

Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage

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12 December 2020