Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein

Arthritis and Rheumatism

Volumn 48, Issue 1, 2003, Pages 119-133

  Pratta, Michael A ^a   Scherle, Peggy A ^b   Yang, Gengjie ^b   Liu, Rui Qin ^c   Newton, Robert C ^b  

^a Glaxo Smith Kline   (Mexico)

^b Experimental Station   (United States)

^c BRISTOL MYERS SQUIBB   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGRECANASE; AGGRECANASE 1; HEPARIN; INTERLEUKIN 1; N ACETYLGALACTOSAMINE 4 SULFATASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTHRITIS; ARTICLE; ARTICULAR CARTILAGE; CARTILAGE; CARTILAGE CELL; CATTLE; CELL CULTURE; CELL LYSATE; CONTROLLED STUDY; ENZYME ACTIVITY; EXTRACELLULAR MATRIX; FIBROBLAST; NONHUMAN; NOSE CARTILAGE; PRIORITY JOURNAL; PROTEIN INDUCTION; STAINING; WESTERN BLOTTING;

EID: 0037231877     PISSN: 00043591     EISSN: None     Source Type: Journal    
DOI: 10.1002/art.10726     Document Type: Article

References (53)

1. Hardingham TE, Fosang AJ, Dudhia J. Aggrecan, the chondroitin sulfate/keratan sulfate proteoglycan from cartilage. In: Kuettner KE, Schleyerbach R, Peyton JG, Hascall VC, editors. Articular cartilage and osteoarthritis. New York: Raven Press; 1992. p. 5-20.
2. Paulsson M, Morgelin M, Wiedemann H, Beardmore-Gray M, Dunham D, Hardingham T, et al. Extended and globular protein domains in cartilage proteoglycans. Biochem J 1987;245:763-72.
3. Mankin HJ, Lippiello L. Biochemical and metabolic abnormalities in articular cartilage from osteoarthritic human hips. J Bone Joint Surg Am 1970;52:424-34.
4. Fosang AJ, Neame PJ, Hardingham TE, Murphy G, Hamilton JA. Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins. J Biol Chem 1991;266:15579-82.
5. Flannery CR, Lark MW, Sandy JD. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan: evidence for proteoiysis at this site in vivo in human articular cartilage. J Biol Chem 1992;267:1008-14.
6. Fosang AJ, Last K, Knauper V, Neame PJ, Murphy G, Hardingham TE, et al. Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain. Biochem J 1993;295:273-6.
7. Fosang AJ, Neame PJ, Last K, Hardingham TE, Murphy G, Hamilton JA. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 1992;267:19470-4.
8. Fosang AJ, Last K, Knauper V, Murphy G, Neame PJ. Degradation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett 1996;380:17-20.
9. 342) in the aggrecan interglobular domain. J Biol Chem 2002;277:16059-66.
10. Tortorella MD, Burn TC, Pratta MA, Abbaszade I, Hollis JM, Liu R, et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999;284:1664-6.
11. Abbaszade I, Liu RQ, Yang F, Rosenfeld SA, Ross OH, Link JR, et al. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J Biol Chem 1999;274:23443-50.
12. Tang BL. ADAMTS: a novel family of extracellular matrix proteases. Int J Biochem Cell Biol 2001;33:33-44.
13. Nagase H. Aggrecanases in cartilage matrix breakdown. Connect Tissue Res 2001;33:27-32.
14. Sandy JD, Boynton RE, Flannery CR. Analysis of the catabolism of aggrecan in cartilage explants by quantitation of peptides from the three globular domains. J Biol Chem 1991;266:8198-205.
15. Sandy JD, Neame PJ, Boynton RE, Flannery CR. Catabolism of aggrecan in cartilage explants: identification of a major cleavage site within the interglobular domain. J Biol Chem 1991;266: 8683-5.
16. Loulakis P, Shrikhande A, Davis G, Maniglia CA. N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures: putative site(s) of enzymatic cleavage. Biochem J 1992;284:589-93.
17. Ilic MZ, Handley CJ, Robinson HC, Mok MT. Mechanism of catabolism of aggrecan by articular cartilage. Arch Biochem Biophys 1992;294:115-22.
18. Lark MW, Gordy JT, Weidner JR, Ayala J, Kimura JH, Williams HR, et al. Cell-mediated catabolism of aggrecan: evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain. J Biol Chem 1995;270:2550-6.
19. Sandy JD, Flannery CR, Neame PJ, Lohmander LS. The structure of aggrecan fragments in human synovial fluid: evidence for the involvement in osteoarthritis of a novel protease, which cleaves the Glu373-Ala374 bond of the interglobular domain. J Clin Invest 1992;89:1512-6.
20. Lohmander LS, Neame PJ, Sandy JD. The structure of aggrecan fragments in human synovial fluid: evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis. Arthritis Rheum 1993;36:1214-22.
21. Sandy JD, Verscharen C. 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 in vivo. Biochem J 2001;358:615-26.
22. Tortorella MD, Pratta M, Liu RQ, Austin J, Ross OH, Abbaszade I, et al. Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4). J Biol Chem 2000;275:18566-73.
23. Arner EC, Hughes CE, Decicco CP, Caterson B, Tortorella MD. Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase. Osteoarthritis Cartilage 1998;6:214-28.
24. Oike Y, Kimata K, Shinomura T, Suzuki S. Proteinase activity in chondroitin lyase (chondroitinase) and endo-β-D-galactosidase (keratanase) preparations and a method to abolish their proteolytic effect on proteoglycan. Biochem J 1980;191:203-7.
25. Hughes CE, Caterson B, Fosang AJ, Roughley PJ, Mort JS. 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 1995;305:799-804.
26. Tortorella MD, Pratta MA, Liu RQ, Abbaszade I, Ross H, Burn T, et al. The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J Biol Chem 2000;275:25791-7.
27. 1-[(1S, 2R)-2-hydroxy-2, 3-dihydro-1H-inden-1-yl] butane-diamide derivatives as potent, selective, and orally bioavailable aggrecanase inhibitors. J Med Chem 2001;44:3347-50.
28. Miller JA, Arner EC, Copeland RA, Davis GL, Pratta MA, Tortorella MD, inventors. Assays and peptide substrate for determining aggrecan-degrading metalloproteinase activity. US Patent WO 0005256. 1998.
29. Pratta MA, Ackerman NR, Arner EC. Effect of ebselen on IL-1-induced alterations in cartilage metabolism. Inflamm Res 1998;47:115-21.
30. Chin JE, Lin Y. Effects of recombinant human interleukin-1β on rabbit articular chondrocytes: stimulation of prostanoid release and inhibition of cell growth. Arthritis Rheum 1988;31:1290-6.
31. Ilic MZ, Vankemmelbeke MN, Holen I, Buttle DJ, Clem Robinson H, Handley CJ. Bovine joint capsule and fibroblasts derived from joint capsule express aggrecanase activity. Matrix Biol 2000;19:257-65.
32. Arner EC, Pratta MA, Trzaskos JM, Decicco CP, Tortorella MD. Generation and characterization of aggrecanase: a soluble, cartilage-derived aggrecan-degrading activity. J Biol Chem 1999;274: 6594-601.
33. Knight CG, Willenbrock F, Murphy GA. A novel coumarinlabelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett 1992;296:263-6.
34. Kuno K, Matsushima K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J Biol Chem 1998;273:13912-7.
35. Vankemmelbeke MN, Holen I, Wilson AG, Ilic MZ, Handley CJ, Kelner GS, et al. Expression and activity of ADAMTS-5 in synovium. Eur J Biochem 2001;268:1259-68.
36. Pratta MA, Tortorella MD, Arner EC. Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase. J Biol Chem 2000;275:39096-102.
37. Hughes CE, Buttner FH, Eidenmuller B, Caterson B, Bartnik E. Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems. J Biol Chem 1997;272:20269-74.
38. Gao G, Westling J, Thompson VP, Howell TD, Gottschall PE, Sandy JD. Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation. J Biol Chem 2002;277: 11034-41.
39. 1 inhibits IL-1-stimulated proteoglycan degradation by chondrocytes without affecting stromelysin synthesis. Arch Biochem Biophys 1995;316:827-35.
40. Tortorella MD, Malfait AM, Decicco C, Arner EC. The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation. Osteoarthritis Cartilage 2001;9: 539-52.
41. Arner EC, Pratta MA, Freimark B, Lischwe M, Trzaskos JM, Magolda RL, et al. Isothiazolones interfere with normal matrix metalloproteinase activation and inhibit cartilage proteoglycan degradation. Biochem J 1996;318:417-24.
42. Flannery CR, Little CB, Hughes CE, Caterson B. Expression of ADAMTS homologues in articular cartilage. Biochem Biophys Res Commun 1999;260:318-22.
43. Caterson B, Flannery CR, Hughes CE, Little CB. Mechanisms involved in cartilage proteoglycan catabolism. Matrix Biol 2000; 19:333-44.
44. Yu WH, Yu SC, Meng Q, Brew K, Woessner JF Jr. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. J Biol Chem 2000;275:31226-32.
45. Kashiwagi M, Tortorella M, Nagase H, Brew K. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem 2001;276:12501-4.
46. Kuno K, Kanada N, Nakashima E, Fujiki F, Ichimura F, Matsushima K. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J Biol Chem 1997;272:556-62.
47. Kuno K, Okada Y, Kawashima H, Nakamura H, Miyasaka M, Ohno H, et al. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan. FEBS Lett 2000;478:241-5.
48. 442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4. J Biol Chem 2001;276:13372-8.
49. Moldovan F, Pelletier JP, Mineau F, Dupuis M, Cloutier JM, Martel-Pelletier J. Modulation of collagenase 3 in human osteoarthritic cartilage by activation of extracellular transforming growth factor β: role of furin convertase. Arthritis Rheum 2000;43:2100-9.
50. Rodriguez-Manzaneque JC, Milchanowski AB, Dufour EK, Leduc R, Iruela-Arispe ML. Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms. J Biol Chem 2000;275:33471-9.
51. Fosang AJ, Last K, Stanton H, Weeks DB, Campbell IK, Hardingham TE, et al. Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage fragments. J Biol Chem 2000;275:33027-37.
52. Hughes CE, Little CB, Buttner FH, Bartnik E, Caterson B. Differential expression of aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage. J Biol Chem 1998;273:30576-82.
53. Little CB, Flannery CR, Hughes CE, Mort JS, Roughley PJ, Dent C, et al. Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro. Biochem J 1999;344:61-8.