A microplate assay specific for the enzyme aggrecanase

Analytical Biochemistry

Volumn 314, Issue 2, 2003, Pages 260-265

  Miller, Jeffery A ^a,c   Liu, Rui Qin ^a   Davis, Gary L ^a,d   Pratta, Michael A ^a,b   Trzaskos, James M ^a   Copeland, Robert A ^a,b  

^a BRISTOL MYERS SQUIBB   (United States)

^b GLAXOSMITHKLINE   (United States)

^c Pro virus   (United States)

^d Physiome Sciences   (United States)

Author keywords

Aggrecanase; Arthritis; Assay design; Drug discovery; High throughput screening; Inflammatory joint disease; Metalloprotease

Indexed keywords

DIAGNOSIS; DRUG PRODUCTS; ENZYMES; PROTEOLYSIS; SCREENING;

AGGRECANASE; ARTHRITIS; DRUG DISCOVERY; HIGH THROUGHPUT SCREENING; JOINT DISEASE; METALLO-PROTEASE;

PEPTIDES;

AGGRECAN; AGGRECANASE; AMINO ACID; ANTIBODY; MATRIX METALLOPROTEINASE; STREPTAVIDIN;

ANIMAL TISSUE; ARTICLE; BIOTINYLATION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN IMMOBILIZATION; SCREENING;

EID: 0037443923     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00638-3     Document Type: Article

References (17)

1. Sandy J.D., Flannery C.R., Neame P.J., Lohmander L.S. The structure of aggrecan fragments in human synovial fluid: evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu373-Ala 374 bond in the interglobular domain. J. Clin. Invest. 89:1992;1512-1516.
2. Fosang A.J., Neame T.J., Hardingham T.E., Murphy G., Hamilton J.A. Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins. J. Biol. Chem. 266:1991;15579-15582.
3. Nagase H., Fields C.G., Fields G.B. Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3). J. Biol. Chem. 269:1994;20952-20957.
4. Arner E.C., Decicco C.P., Cherney R., Tortorella M.D. Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase. J. Biol. Chem. 272:1997;9294-9299.
5. Fosang A.J., Last K., Neame P.J., Murphy G., Knauper V., Tschesche H., Hughers C.E., Caterson B., Hardingham T.E. Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan. Biochem. J. 304:1994;347-351.
6. Tortorella M.D.et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science. 284:1999;1664-1666.
7. Abbaszade I.et al. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J. Biol. Chem. 274:1999;23443-23450.
8. Hughes C.E., Caterson B., Fosang A.J., Roughley P.J., Mort J.S. Monoclonal antibodies that specifically recognize neoepitope sequences generated by aggrecanase and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro. Biochem. J. 305:1995;799-804.
9. Copeland R.A. Enzymes: A Practical Introduction to Structure, Mechanism and Data Analysis. second ed. 2000;Wiley, New York.
10. M. Pratta, unpublished results; R.A. Copeland, unpublished results and personal communications.
11. J.A. Miller et al., Assays and peptide substrate for determining aggrecan degrading metallo protease activity, US Patent 6,326162 B1, 2001.
12. Wilkens M., Krishnaswamy S. The contribution of factor Xa to exosite-dependent substrate recognition by prothrombinase. J. Biol. Chem. 277:2002;9366-9374.
13. C helix of ERK Biochemistry. 37:1998;8879-8885.
14. Dennis M.S.et al. Peptide exosite inhibitors of factor VIIa as anticoagulants. Nature. 404:2000;465-470.
15. Okada Y.et al. Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT-1080 human fibrosarcoma cells. J. Biol. Chem. 267:1992;21712-21719.
16. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-162.
17. Horber C., Buttner F.H., Kern C., Schmiedeknecht G., Bartnik E. 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. Matrix Biol. 19:2000;533-543.