Mechanisms involved in cartilage proteoglycan catabolism

Matrix Biology

Volumn 19, Issue 4, 2000, Pages 333-344

  Caterson, Bruce ^a   Flannery, Carl R ^a   Hughes, Clare E ^a   Little, Chris B ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

Author keywords

ADAMTS; Aggrecanase; Arthritis; Matrix metalloproteinase; Neoepitope antibody

Indexed keywords

AGGRECAN; AGGRECANASE; ENZYME; MATRIX METALLOPROTEINASE; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

ARTICULAR CARTILAGE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; REVIEW;

EID: 0034253761     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(00)00078-0     Document Type: Short Survey

References (62)

1. Abbaszade I., Liu R.Q., Yang F. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J. Biol. Chem. 274:1999;23443-23450.
2. Arner E.C., Hughes C.E., Decicco C.P., Caterson B., Tortorella M.D. Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase. Osteoarthritis Cartilage. 6:1998;214-228.
3. Arner E.C., Pratta M.A., Trzaskos J.M., Decicco C.P., Tortorella M.D. Generation and characterization of aggrecanase. a soluble, cartilage-derived aggrecan-degrading activity. J. Biol. Chem. 274:1999;6594-6601.
4. Billinghurst R.C., Dahlberg L., Ionescu M. et al. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J. Clin. Invest. 99:1997;1534-1545.
5. Büttner F.H., Hughes C.E., Margerie D. et al. Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and MMP sites. Biochem. J. 333:1998;159-165.
6. Campbell M.A., Handley C.J. The effect of retinoic acid on proteoglycan turnover in bovine articular cartilage cultures. Arch. Biochem. Biophys. 258:1987;143-155.
7. Caterson B., Christner J.E., Baker J.B., Couchman J.R. Production and characterization of monoclonal antibodies directed against connective tissue proteoglycans. Federation Proc. 44:1985;386-393.
8. Cawston T.E., Curry V.A., Summers C.A. et al. The role of oncostatin M in animal and human connective tissue collagen turnover and its localization within the rheumatoid joint. Arthritis Rheum. 41:1998;1760-1771.
9. Colige A., Sieron A.L., Li S.W. et al. Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene. Am. J. Hum. Genet. 65:1999;308-317.
10. Curtis C.L., Hughes C.E., Flannery C.R., Little C.B., Harwood J.L., Caterson B. n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation. J. Biol. Chem. 275:2000;721-724.
11. Doege K.J., Sasaki M., Kimura T., Yamada Y. Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms. J. Biol. Chem. 266:1991;894-902.
12. Flannery C.R., Lark M.W., Sandy J.D. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at the site in vivo in human articular cartilage. J. Biol. Chem. 267:1992;1008-1014.
13. Flannery C.R., Little C.B., Caterson B. Molecular cloning and sequence analysis of the aggrecan interglobular domain from porcine, equine, bovine and ovine cartilage: comparison of proteinase-susceptible regions and sites of keratan sulfate substitution. Matrix Biol. 16:1998;507-511.
14. Flannery C.R., Little C.B., Caterson B., Hughes C.E. Effects of culture conditions and exposure to catabolic stimulators IL-1 and retinoic acid on the expression of matrix metalloproteinases MMPs and disintegrin metalloproteinases ADAMs by articular cartilage chondrocytes. Matrix Biol. 18:1999;225-237.
15. Fosang A.J., Last K., Gardiner P., Jackson D.C., Brown L. Development of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids. Biochem. J. 310:1995;337-343.
16. Fosang A.J., Last K., Maciewicz R.A. Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent. J. Clin. Invest. 98:1996;2292-2299.
17. Hardingham T.E., Fosang A.J. Proteoglycans: many forms and many functions. FASEB J. 6:1992;861-870.
18. Hascall V.C., Sandy J.D., Handley C.J. Regulation of proteoglycan metabolism in articular cartilage. Archer C.W., Caterson B., Benjamin M., Ralphs J.R. Biology of the Synovial Joint. 1999;101-120 Harwood Academic Publishers, The Netherlands.
19. Hering T.M., Kollar J., Hu T.D. Complete coding sequence of bovine aggrecan: comparative structural analysis. Arch. Biochem. Biophys. 345:1997;259-270.
20. Hollander A.P., Heathfield T.F., Webber C. et al. Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay. J. Clin. Invest. 93:1994;1722-1732.
21. Hughes C.E., Caterson B., White R.J., Roughley P.J., Mort J.S. Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation. Application to studies of human link protein cleavage by stromelysin. J. Biol. Chem. 267:1992;16011-16014.
22. 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.
23. Hughes C.E., Büttner F.H., 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. 272:1997;20269-20274.
24. Hughes C.E., Little C.B., Büttner F.H., Bartnik E., Caterson B. Differential expression on aggrecanase and matrix metalloproteinase activity in chondrocytes isolated from bovine and porcine articular cartilage. J. Biol. Chem. 273:1998;30576-30582.
25. Ilic M.Z., Handley C.J., Robinson H.C., Mok M.T. Mechanism of catabolism of aggrecan by articular cartilage. Arch. Biochem. Biophys. 294:1992;115-122.
26. Kozaci L.D., Buttle D.J., Hollander A.P. Degradation of type II collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures. Arthritis Rheum. 40:1997;164-174.
27. Kuno K., Kananda 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. 272:1997;556-562.
28. Kuno K., Matsushima K. ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type 1 motifs and its spacing region. J. Biol. Chem. 273:1998;13912-13917.
29. Lark M.W., Bayne E.K., Flanagan J. Aggrecan degradation in human cartilage. Evidence for both matrix metalloproteinase and aggrecanase activity in normal, osteoarthritic, and rheumatoid joints. J. Clin. Invest. 100:1997;93-106.
30. 374 is a primary event in proteolysis of the interglobular domain. J. Biol. Chem. 270:1995;2550-2556.
31. Little C.B., Flannery C.R., Hughes C.E. et al. Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro. Biochem. J. 344:1999;61-68.
32. Little C.B., Wang-Weigand S., Bohne R., Hughes C.E., Janusz M., Caterson B. Time dependent aggrecanase and matrix metalloproteinase degradation of cartilage aggrecan and link protein in response to IL-1 stimulation. Trans. Orthop. Res. Soc. 24:1999;683.
33. Lohmander L.S. Markers of cartilage matrix metabolism in arthrosis: a review. Acta Orthop. Scand. 62:1991;623-632.
34. Lohmander L.S., Ionescu M., Jugessur H., Poole A.R. Changes in joint cartilage aggrecan after knee injury and in osteoarthritis. Arthritis Rheum. 42:1999;534-544.
35. Lomander L., Neame P.J., Sandy J.D. 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. 36:1993;1214-1222.
36. Loulakis P., Shrikhande A., Davis G., Maniglia C.A. N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1 treated articular cartilage explant cultures. Biochem. J. 284:1992;589-593.
37. Maniglia C.A., Loulakis P.P., Shrikhande A.V., Davis G. IL-1 elevated PG degradation reveals NH2-terminal sequence homology. Trans. Orthop. Res. Soc. 16:1991;193.
38. Mankin H.J., Dorfman H., Lippiello L., Zarins A. Biochemical and metabolic abnormalities in articular cartilage from osteo-arthritic human hips. II. Correlation of morphology with biochemical and metabolic data. J. Bone Joint Surg. Am. 53:1971;523-537.
39. Otterness I.G., Downs J.T., Lane C. et al. Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody. Matrix Biol. 18:1999;331-341.
40. Price J.S., Till S.H., Bickerstaff D.R., Bayliss M.T., Hollander A.P. Degradation of cartilage type II collagen precedes the onset of osteoarthritis following anterior cruciate ligament rupture. Arthritis Rheum. 42:1999;2390-2398.
41. Price J.S., Wang-Weigand S., Bohne R., Kozaci L.D., Hollander A.P. Retinoic acid-induced type II collagen degradation does not correlate with matrix metalloproteinase activity in cartilage explant cultures. Arthritis Rheum. 42:1999;137-147.
42. Primakoff P., Myles D.G. The ADAM gene family. Surface proteins with adhesion and protease activity. Trends Genet. 16:2000;83-87.
43. Ratcliffe A., Tyler J.A., Hardingham T.E. Articular cartilage cultured with interleukin 1. Increased release of link protein, hyaluronate-binding region and other proteoglycan fragments. Biochem. J. 238:1986;571-580.
44. Roughley P.J., White R.J., Poole A.R. Identification of a hyaluronic acid-binding protein that interferes with the preparation of high-buoyant-density proteoglycan aggregates from adult human articular cartilage. Biochem. J. 231:1985;129-138.
45. Sandy J.D., Flannery C.R., Boynton R.E., Neame P.J. Isolation and characterization of disulfide-bonded peptides from the three globular domains of aggregating cartilage proteoglycan. J. Biol. Chem. 265:1990;21108-21113.
46. Sandy J.D., Boynton R.E., Flannery C.R. Analysis of the catabolism of aggrecan in cartilage explants by quantitation of peptides from the three globular domains. J. Biol. Chem. 266:1991;8198-8205.
47. Sandy J.D., Neame P.J., Boynton R.E., Flannery C.R. Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J. Biol. Chem. 266:1991;8683-8685.
48. 374 bond of the interglobular domain. J. Clin. Invest. 89:1992;1512-1516.
49. Sasaki T., Miosge N., Timpl R. Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 osteonectin, SPARC which are correlated to a higher affinity binding to collagens. Matrix Biol. 18:1999;499-508.
50. Singer I.I., Kawka D.W., Bayne E.K. et al. VDIPEN, a metalloproteinase-generated neoepitope, is induced and immunolocalized in articular cartilage during inflammatory arthritis. J. Clin. Invest. 95:1995;2178-2186.
51. Sugimoto K., Takahashi M., Yamamoto Y., Shimada K., Tanzawa K. Identification of aggrecanase activity in medium of cartilage culture (Tokyo). J. Biochem. 126:1999;449-455.
52. Sztrolovics R., Alini M., Roughley P.J., Mort J.S. Aggrecan degradation in human intervertebral disc and articular cartilage. Biochem. J. 326:1997;235-241.
53. Tortorella M.D., Burn T.C., Pratta M.A. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science. 284:1999;1664-1666.
54. Tortorella M.D., Pratta M., Liu R.Q., Austin J., Ross O.H., Abbaszade I., Burn T., Arner E. Sites of aggrecan cleavage by recombinant human aggrecanase-1 ADAMTS-4. J. Biol. Chem. 275:2000;18566-18573.
55. Tyler J.A. Chondrocyte-mediated depletion of articular cartilage proteoglycans in vitro. Biochem. J. 225:1985;493-507.
56. van Meurs J.B.J., van Lent P.L.E.M., Holthuysen A.E.M., Singer I.I., Bayne E.K., van den Berg W.B. Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis. Arthritis Rheum. 42:1999;1128-1139.
57. van Meurs J.B.J., van Lent P.L.E.M., van de Loo A.A.J. et al. Increased vulnerability of postarthritic cartilage to a second arthritic insult: accelerated MMP activity in a flare up of arthritis. Ann. Rheum. Dis. 58:1999;350-356.
58. Vankemmelbeke M., Dekeyser P.M., Hollander A.P., Buttle D.J., Demeester J. Characterization of helical cleavages in type II collagen generated by matrixins. Biochem. J. 330:1998;633-640.
59. Vazquez F., Hastings G., Ortega M.A. et al. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J. Biol. Chem. 274:1999;23349-23357.
60. Visco D.M., Johnstone B., Hill H.A., Jolly G.A., Caterson B. Immunohistochemical analysis of 3-B-3(-) and 7-D-4 epitope expression in canine and human osteoarthritis. Arthritis Rheum. 36:1993;1718-1725.
61. Yamada H., Watanabe K., Shimonaka M., Yamasaki M., Yamaguchi Y. cDNA cloning and the identification of an aggrecanase-like cleavage site in rat brevican. Biochem. Biophys. Res. Comm. 216:1995;957-963.
62. Zhang H., Kelly G., Zerillo C., Jaworski D.M., Hockfield S. Expression of a cleaved brain-specific extracellular matrix protein mediates glioma cell invasion in vivo. J. Neurosci. 18:1998;2370-2376.