ADAMTS proteinases: A multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis

Arthritis Research and Therapy

Volumn 7, Issue 4, 2005, Pages 160-169

  Jones, Gavin C ^a   Riley, Graham P ^a  

^a ADDENBROOKE S HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS PROTEINASE; ADAMTS 1 PROTEINASE; ADAMTS 10 PROTEINASE; ADAMTS 12 PROTEINASE; ADAMTS 15 PROTEINASE; ADAMTS 16 PROTEINASE; ADAMTS 17 PROTEINASE; ADAMTS 18 PROTEINASE; ADAMTS 19 PROTEINASE; ADAMTS 20 PROTEINASE; ADAMTS 4 PROTEINASE; ADAMTS 5 PROTEINASE; ADAMTS 6 PROTEINASE; ADAMTS 7 PROTEINASE; ADAMTS 8 PROTEINASE; ADAMTS 9 PROTEINASE; ADAMTS PROTEINASE; AGGRECAN; CARTILAGE OLIGOMERIC MATRIX PROTEIN; DECORIN; FIBROMODULIN; METALLOPROTEINASE; PROCOLLAGEN; PROCOLLAGEN N PROTEINASE; PROTEINASE; PROTEOGLYCAN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTHRITIS; BONE TURNOVER; CARBOXY TERMINAL SEQUENCE; ENZYME INHIBITION; EXTRACELLULAR MATRIX; GENE EXPRESSION REGULATION; HUMAN; MIXED CONNECTIVE TISSUE DISEASE; NONHUMAN; PATHOGENESIS; PHYLOGENY; PROTEIN BLOOD LEVEL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; RNA SPLICING; SEQUENCE ALIGNMENT;

ADAM PROTEINS; ANIMALS; ARTHRITIS, RHEUMATOID; EXTRACELLULAR MATRIX; HUMANS; MULTIGENE FAMILY; PROTEIN STRUCTURE, TERTIARY;

EID: 21644449866     PISSN: 14786354     EISSN: None     Source Type: Journal    
DOI: 10.1186/ar1783     Document Type: Review

References (93)

1. Kevorkian L, Young DA, Darrah C, Donell ST, Shepstone L, Porter S, Brockbank SM, Edwards DR, Parker AE, Clark IM: Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 2004, 50:131-141.
2. Tortorella MD, Burn TC, Pratta MA, Abbaszade I, Hollis JM, Liu R, Rosenfeld SA, Copeland RA, Decicco CP, Wynn R, et al.: Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 1999, 284:1664-1666.
3. Malfait AM, Liu RO, Ijiri K, Komiya S, Tortorella MD: Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage. J Biol Chem 2002, 277:22201-22208.
4. 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, 272:556-562.
5. MEROPS: the Peptidase Database [http://merops.sanger.ac.uk]
6. Barrett AJ, Rawlings ND, O'Brien EA: The MEROPS database as a protease information system. J Struct Biol 2001, 134:95-102.
7. Thompson JD, Higgins DG, Gibson TJ: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680.
8. Nicholson AC, Malik SB, Logsdon JM Jr, Van Meir EG: Functional evolution of ADAMTS genes: evidence from analyses of phylogeny and gene organization. BMC Evol Biol 2005, 5:11.
9. Flannery CR, Zeng W, Corcoran C, Collins-Racie LA, Chockalingam PS, Hebert T, Mackie SA, McDonagh T, Crawford TK, Tomkinson KN, et al.: Autocatalytic cleavage of ADAMTS-4 (aggrecanase-1) reveals multiple glycosaminoglycan-binding sites. J Biol Chem 2002, 277:42775-42780.
10. Wang P, Tortorella M, England K, Malfait AM, Thomas G, Arner EC, Pei D: Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (aggrecanase-1) in the trans-Golgi network. J Biol Chem 2004, 279:15434-15440.
11. Bode W, Gomis-Ruth FX, Stockler W: Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 1993, 331:134-140.
12. Rawlings ND, Barrett AJ: Evolutionary families of metallopeptidases. Methods Enzymol 1995, 248:183-228.
13. Huang TF: What have snakes taught us about integrins? Cell Mol Life Sci 1998, 54:527-540.
14. Bornstein P: Thrombospondins: structure and regulation of expression. FASEB J 1992, 6:3290-3299.
15. Guo NH, Krutzsch HC, Negre E, Zabrenetzky VS, Roberts DD: Heparin-binding peptides from the type I repeats of thrombospondin. Structural requirements for heparin binding and promotion of melanoma cell adhesion and chemotaxis. J Biol Chem 1992, 267:19349-19355.
16. 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. 273:13912-13917.
17. Somerville RP, Longpre JM, Apel ED, Lewis RM, Wang LW, Sanes JR, Leduc R, Apte SS: ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain. J Biol Chem 2004, 279: 35159-35175.
18. Somerville RP, Longpre JM, Jungers KA, Engle JM, Ross M, Evanko S, Wight TN, Leduc R, Apte SS: Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1. J Biol Chem 2003, 278:9503-9513.
19. Nardi JB, Martos R, Walden KK, Lampe DJ, Robertson HM: Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. Insect Biochem Mol Biol 1999, 29:883-897.
20. Zheng X, Chung D, Takayama TK, Majerus EM, Sadler JE, Fujikawa K: Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. J Biol Chem 2001, 276:41059-41063.
21. Bork P, Beckmann G: The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 1993, 231: 539-545.
22. Romero A, Romao MJ, Varela PF, Kolln I, Dias JM, Carvalho AL, Sanz L, Topfer-Petersen E, Calvete JJ: The crystal structures of two spermadhesins reveal the CUB domain fold. Nat Struct Biol 1997, 4:783-788.
23. 2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement. J Biol Chem 2003, 278:32157-32164.
24. Schechter I, Berger A: On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967, 27: 157-162.
25. 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, 266:8683-8685.
26. Nakamura H, Fujii Y, Inoki I, Sugimoto K, Tanzawa K, Matsuki H, Miura R, Yamaguchi Y, Okada Y: Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. J Biol Chem 2000, 275:38885-38890.
27. Kashiwagi M, Enghild JJ, Gendron C, Hughes C, Caterson B, Itoh Y, Nagase H: Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing. J Biol Chem 2004, 279: 10109-10119.
28. Llamazares M, Cal S, Quesada V, Lopez-Otin C: Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain. J Biol Chem 2003, 278:13382-13389.
29. 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 proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. J Clin Invest 1992, 89:1512-1516.
30. 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, 36:1214-1222.
31. 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, 358:615-626.
32. Pratta MA, Yao W, Decicco C, Tortorella MD, Liu RQ, Copeland RA, Magolda R, Newton RC, Trzaskos JM, Arner EC: Aggrecan protects cartilage collagen from proteolytic cleavage. J Biol Chem 2003, 278:45539-45545.
33. Samiric T, Ilic MZ, Handley CJ: Characterisation of proteoglycans and their catabolic products in tendon and explant cultures of tendon. Matrix Biol 2004, 23:127-140.
34. Glasson SS, Askew R, Sheppard B, Carito BA, Blanchet T, Ma HL, Flannery CR, Kanki K, Wang E, Peluso D, et al.: Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice. Arthritis Rheum 2004, 50:2547-2558.
35. Glasson SS, Askew R, Sheppard B, Carito B, Blanchet T, Ma HL, Flannery CR, Peluso D, Kanki K, Yang Z, et al.: Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 2005, 434:644-648.
36. Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, Little CB, Last K, Farmer PJ, Campbell IK, et al.: ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro . Nature 2005, 434:648-652.
37. Astrom M, Rausing A: Chronic Achilles tendinopathy. A survey of surgical and histopathologic findings. Clin Orthop 1995, 316:151-164.
38. Walsh DA: Angiogenesis and arthritis. Rheumatology (Oxford) 1999, 38:103-112.
39. Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML: 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 1999, 274: 23349-23357.
40. Kahn J, Mehraban F, Ingle G, Xin X, Bryant JE, Vehar G, Schoenfeld J, Grimaldi CJ, Peale F, Draksharapu A, et al.: Gene expression profiling in an in vitro model of angiogenesis. Am J Pathol 2000, 156:1887-1900.
41. Luque A, Carpizo DR, Iruela-Arispe ML: ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J Biol Chem 2003, 278:23656-23665.
42. Tolsma SS, Volpert OV, Good DJ, Frazier WA, Polverini PJ, Bouck N: Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity. J Cell Biol 1993, 122:497-511.
43. Iruela-Arispe ML, Carpizo D, Luque A: ADAMTS1: a matrix metalloprotease with angioinhibitory properties. Ann N Y Acad Sci 2003, 995:183-190.
44. Blelloch R, Anna-Arriola SS, Gao D, Li Y, Hodgkin J, Kimble J: The gon-1 gene is required for gonadal morphogenesis in Caenorhabditis elegans. Dev Biol 1999, 216:382-393.
45. Blelloch R, Kimble J: Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 1999, 399:586-590.
46. Rao C, Foernzler D, Loftus SK, Liu S, McPherson JD, Jungers KA, Apte SS, Pavan WJ, Beier DR: A defect in a novel ADAMTS family member is the cause of the belted white-spotting mutation. Development 2003, 130:4665-4672.
47. Shindo T, Kurihara H, Kuno K, Yokoyama H, Wada T, Kurihara Y, Imai T, Wang Y, Ogata M, Nishimatsu H, et al.: ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J Clin Invest 2000, 105:1345-1352.
48. Yokoyama H, Wada T, Kobayashi K, Kuno K, Kurihara H, Shindo T, Matsushima K: A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-1 null mutant mice develop renal lesions mimicking obstructive nephropathy. Nephrol Dial Transplant 2002, 17 Suppl 9:39-41.
49. Espey LL, Yoshioka S, Russell DL, Robker RL, Fujii S, Richards JS: Ovarian expression of a disintegrin and metalloproteinase with thrombospondin motifs during ovulation in the gonadotropin-primed immature rat. Biol Reprod 2000, 62:1090-1095.
50. Robker RL, Russell DL, Espey LL, Lydon JP, O'Malley BW, Richards JS: Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases. Proc Natl Acad Sci USA 2000, 97:4689-4694.
51. Boerboom D, Russell DL, Richards JS, Sirois J: Regulation of transcripts encoding ADAMTS-1 (a disintegrin and metalloproteinase with thrombospondin-like motifs-1) and progesterone receptor by human chorionic gonadotropin in equine preovulatory follicles. J Mol Endocrinol 2003, 31:473-485.
52. Russell DL, Doyle KM, Ochsner SA, Sandy JD, Richards JS: Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation. J Biol Chem 2003, 278:42330-42339.
53. Mort JS, Flannery CR, Makkerh J, Krupa JC, Lee ER: Use of antineoepitope antibodies for the analysis of degraclative events in cartilage and the molecular basis for neoepitope specificity. Biochem Soc Symp 2003, 70:107-114.
54. Colige A, Li SW, Sieron AL, Nusgens BV, Prockop DJ, Lapière CM: cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc Natl Acad Sci USA 1997, 94:2374-2379.
55. Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, Brenner MC, Takahara K, Greenspan DS: Transforming growth factor-beta induces secretion of activated ADAMTS-2. A pro-collagen III N-proteinase. J Biol Chem 2003, 278:19549-19557.
56. Colige A, Sieron AL, Li SW, Schwarze U, Petty E, Wertelecki W, Wilcox W, Krakow D, Cohn DH, Reardon 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 1999, 65:308-317.
57. Nusgens BV, Verellen-Dumoulin C, Hermanns-Lê T, De Paepe A, Nuytinck L, Piérard GE, Lapière CM: Evidence for a relationship between Ehlers-Danlos type VII C in humans and bovine dermatosparaxis. Nat Genet 1992, 1:214-217.
58. Li SW, Arita M, Fertala A, Bao Y, Kopen GC, Langsjo TK, Hyttinen MM, Helminen HJ, Prockop DJ: Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility. Biochem J 2001, 355:271-278.
59. Fernandes RJ, Hirohata S, Engle JM, Colige A, Cohn DH, Eyre DR, Apte SS: Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. J Biol Chem 2001, 276:31502-31509.
60. Colige A, Vandenberghe I, Thiry M, Lambert CA, Van Beeumen J, Li SW, Prockop DJ, Lapière CM, Nusgens BV: Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. J Biol Chem 2002, 277:5756-5766.
61. Fujikawa K, Suzuki H, McMullen B, Chung D: Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family. Blood 2001, 98:1662-1666.
62. Soejima K, Mimura N, Hirashima M, Maeda H, Hamamoto T, Nakagaki T, Nozaki C: A novel human metalloprotease synthesized in the liver and secreted into the blood: possibly, the von Willebrand factor-cleaving protease? J Biochem (Tokyo) 2001, 130:475-480.
63. Levy GG, Nichols WC, Lian EC, Foroud T, McClintick JN, McGee BM, Yang AY, Siemieniak DR, Stark KR, Gruppo R, et al.: Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature 2001, 413:488-494.
64. Scheiflinger F, Knobl P, Trattner B, Plaimauer B, Mohr G, Dockal M, Dorner F, Rieger M: Nonneutralizing IgM and IgG antibodies to von Willebrand factor-cleaving protease (ADAMTS-13) in a patient with thrombotic thrombocytopenic purpura. Blood 2003, 102:3241-3243.
65. Cal S, Arguelles JM, Fernandez PL, Lopez-Otin C: Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats. J Biol Chem 2001, 276:17932-17940.
66. Somerville RP, Jungers KA, Apte SS: ADAMTS10: discovery and characterization of a novel, widely expressed metalloprotease and its proteolytic activation. J Biol Chem 2004, 279:51208-51217.
67. Dagoneau N, Benoist-Lasselin C, Huber C, Faivre L, Megarbane A, Alswaid A, Dollfus H, Alembik Y, Munnich A, Legeai-Mallet L, et al.: ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome. Am J Hum Genet 2004, 75:801-806.
68. Bevitt DJ, Mohamed J, Catterall JB, Li Z, Arris CE, Hiscott P, Sheridan C, Langton KP, Barker MD, Clarke MP, et al.: Expression of ADAMTS metalloproteinases in the retinal pigment epithelium derived cell line ARPE-19: transcriptional regulation by TNFalpha. Biochim Biophys Acta 2003, 1626:83-91.
69. Sylvester J, Liacini A, Li WQ, Zafarullah M: Interleukin-17 signal transduction pathways implicated in inducing matrix metalloproteinase-3, -13 and aggrecanase-1 genes in articular chondrocytes. Cell Signal 2004, 16:469-476.
70. Satoh K, Suzuki N, Yokota H: ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes. Neurosci Lett 2000, 289:177-180.
71. Yamanishi Y, Boyle DL, Clark M, Maki RA, Tortorella MD, Arner EC, Firestein GS: Expression and regulation of aggrecanase in arthritis: the role of TGF-beta. J Immunol 2002, 168:1405-1412.
72. Koshy PJ, Lundy CJ, Rowan AD, Porter S, Edwards DR, Hogan A, Clark IM, Cawston TE: The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: a time-course study using real-time quantitative reverse transcription-polymerase chain reaction. Arthritis Rheum 2002, 46:961-967.
73. Vankemmelbeke MN, Holen I, Wilson AG, Ilic MZ, Handley CJ, Kelner GS, Clark M, Liu C, Maki RA, Burnett D, et al.: Expression and activity of ADAMTS-5 in synovium. Eur J Biochem 2001, 268:1259-1268.
74. Flannery CR, Little CB, Hughes CE, Caterson B: Expression of ADAMTS homologues in articular cartilage. Biochem Biophys Res Commun 1999, 260:318-322.
75. Pratta MA, Scherle PA, Yang G, Liu RQ, Newton RC: Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein. Arthritis Rheum 2003, 48:119-133.
76. Patwari P, Gao G, Lee JH, Grodzinsky AJ, Sandy JD: Analysis of ADAMTS4 and MT4-MMP indicates that both are involved in aggrecanolysis in interleukin-1-treated bovine cartilage. Osteoarthritis Cartilage 2005, 13:269-277.
77. Bevitt DJ, Li Z, Barker MD, Clarke MP, McKie N: Analysis of ADAMTS6 transcripts reveals complex alternative splicing and a potential role for the 5′ untranslated region in translational control. Gene, in press.
78. Hurskainen TL, Hirohata S, Seldin MF, Apte SS: ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. J Biol Chem 1999, 274: 25555-25563.
79. Clark ME, Kelner GS, Turbeville LA, Boyer A, Arden KC, Maki RA: ADAMTS9, a novel member of the ADAM-TS/metallospondin gene family. Genomics 2000, 67:343-350.
80. Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada V, Lopez-Otin C: Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene 2002, 283:49-62.
81. Apte SS: A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol 2004, 36:981-985.
82. Kozak M: Emerging links between initiation of translation and human diseases. Mamm Genome 2002, 13:401-410.
83. 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, 275:33471-33479.
84. 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, 277:11034-11041.
85. Gao G, Plaas A, Thompson VP, Jin S, Zuo F, Sandy JD: ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. J Biol Chem 2004, 279:10042-10051.
86. Soejima K, Matsumoto M, Kokame K, Yagi H, Ishizashi H, Maeda H, Nozaki C, Miyata T, Fujimura Y, Nakagaki T: ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage. Blood 2003, 102:3232-3237.
87. Sasisekharan R, Venkataraman G: Heparin and heparan sulfate: biosynthesis, structure and function. Curr Opin Chem Biol 2000, 4:626-631.
88. van Meurs J, van Lent P, Stoop R, Holthuysen A, Singer I, Bayne E, Mudgett J, Poole R, Billinghurst C, van der Kraan P, et al.: Cleavage of aggrecan at the Asn341-Phe342 site coincides with the initiation of collagen damage in murine antigen-induced arthritis: a pivotal role for stromelysin 1 in matrix metalloproteinase activity. Arthritis Rheum 1999, 42:2074-2084.
89. 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, 276:12501-12504.
90. Hashimoto G, Aoki T, Nakamura H, Tanzawa K, Okada Y: Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4). FEBS Lett 2001, 494: 192-195.
91. Yu WH, Yu S, Meng Q, Brew K, Woessner JF Jr: TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. J Biol Chem 2000, 275:31226-31232.
92. Kramerova IA, Kawaguchi N, Fessler LI, Nelson RE, Chen Y, Kramerov AA, Kusche-Gullberg M, Kramer JM, Ackley BD, Sieron AL, et al.: Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases. Development 2000, 127:5475-5485.
93. Hashimoto G, Shimoda M, Okada Y: ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan. J Biol Chem 2004, 279: 32483-32491.