A review of the ADAMTS family, pharmaceutical targets of the future

Current Pharmaceutical Design

Volumn 15, Issue 20, 2009, Pages 2359-2374

  Tortorella, Micky D ^a   Malfait, Fransiska ^b   Barve, Ruteja A ^a   Shieh, Huey Sheng ^a   Malfait, Anne Marie ^a  

^a PFIZER INC   (United States)

^b GHENT UNIVERSITY HOSPITAL   (Belgium)

Author keywords

ADAMTS; Aggrecanase; Metalloproteinase

Indexed keywords

A DISINTEGRIN AND METALLOPROTEINASE 33 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 12 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 13 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 16 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 20 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 7 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 9 PROTEIN; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS PROTEIN; ADAM PROTEIN; AGGRECANASE; AGGRECANASE 1; AGGRECANASE 1 INHIBITOR; AGGRECANASE 2; COLLAGEN; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; STROMELYSIN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTHRITIS; ATHEROSCLEROSIS; CARBOXY TERMINAL SEQUENCE; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; DOWN SYNDROME; DRUG BINDING SITE; DRUG DESIGN; DRUG TARGETING; EHLERS DANLOS SYNDROME; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; GLIOMA; HUMAN; NONHUMAN; OSTEOARTHRITIS; PATHOGENESIS; PHYLOGENETIC TREE; PICK PRESENILE DEMENTIA; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEFECT; PROTEIN FAMILY; PROTEIN PROCESSING; PROTEIN TARGETING; REVIEW; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; THROMBOTIC THROMBOCYTOPENIC PURPURA; WEILL MARCHESANI SYNDROME;

ADAM PROTEINS; AMINO ACID SEQUENCE; ENZYME ACTIVATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 69249153030     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209788682433     Document Type: Review

References (147)

1. 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.
2. Kuno K, Terashima Y, Matsushima K. ADAMTS-1 Is an Active Metalloproteinase Associated with the Extracellular Matrix. J Biol Chem 1999; 274: 18821-6.
3. Arner E, Burn T, Copeland R, Decicco C, Liu C, Magolda R, et al. Aggrecan degrading Metallo Proteases. WO/1999/005291 1999 (priority date 1997).
4. Bode W, Grams F, Reinemer P, Gomis-Ruth F, Baumann U, McKay D, et al. The metzincins: A superfamily of structurally related metalloproteinases. Zoology 1995; 99: 237-46.
5. Apte S. A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: The ADAMTS family. Int J Biochem Cell Biol 2004; 36: 981-5.
6. Gomis-Rüth FX. Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotechnol 2003; 24: 157-202.
7. Colige A, Sieron A, Li S, Schwarze U, Petty E, Wertelecki 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: 308-17.
8. Fosang AJ, Little CB. Drug insight: Aggrecanases as therapeutic targets for osteoarthritis. Nat Clin Pract 2008; 4: 420-7.
9. Tsai HM. Thrombotic thrombocytopenic purpura: A thrombotic disorder caused by ADAMTS13 deficiency. Hematol Oncol Clin North Am 2007: 609-32.
10. Van Wart H, Birkedal-Hansen H. The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990; 87: 5578-82.
11. Majerus E, Zheng X, Tuley E, Sadler J. Cleavage of the ADAMTS13 propeptide is not required for protease activity. J Biol Chem 2003; 278: 46643-8.
12. Flannery C, Zeng W, Corcoran C, Collins-Racie L, Chockalingam P, Hebert T, et al. Autocatalytic cleavage of ADAMTS-4 (Aggrecanase-1) reveals multiple glycosaminoglycan-binding sites. J Biol Chem 2002; 277: 42775-80.
13. Black RA. Tumor necrosis factor-alpha converting enzyme. Int J Biochem Cell Biol 2002; 34: 1-5.
14. Silverstein RL, Febbraio M. CD36-TSP-HRGP interactions in the regulation of angiogenesis. Curr Pharm Des 2007; 13: 3559-67.
15. Tortorella M, Pratta M, 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.
16. Kashiwagi M, Enghild J, Gendron C, Hughes C, Caterson B, Itoh Y, et al. Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing. J Biol Chem 2004; 279: 10109-19.
17. Clark M, Kelner G, Turbeville L, Boyer A, Arden K, Maki R. ADAMTS9, a novel member of the ADAM-TS/metallospondin gene family. Genomics 2000; 67: 343-50.
18. Somerville R, Longpre J, Jungers K, Engle J, Ross M, Evanko S, et al. Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1. J Biol Chem 2003; 278: 9503-13.
19. Nardi J, Martos R, Walden K, Lampe D, Robertson H. Expression of lacunin, a large multidomain extracellular matrix protein, accompanies morphogenesis of epithelial monolayers in Manduca sexta. Insect Biochem Mol Biol 1999; 10: 883-97.
20. Zhou A, Webb G, Zhu X, Steiner DF. Proteolytic processing in the secretory pathway. J Biol Chem 1999; 274: 20745-8.
21. Blelloch R, Kimble J. Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 1999; 399: 586-90.
22. Moake JL. von Willebrand factor, ADAMTS-13, and thrombotic thrombocytopenic purpura. Semin Hematol 2004; 41: 4-14.
23. Zhou Z, Jing H, Tao Z, Choi H, Aboulfatova K, Moake J, et al. Effects of naturally occurring mutations in CUB-1 domain on synthesis, stability, and activity of ADAMTS-13. Thrombo Res 2008 Nov 20;(Epub ahead of print)
24. 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: 11-5.
25. Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, et al. Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. Protein Sci 2008; 17: 16-21.
26. Gerhardt S, Hassall G, Hargreaves D, Ting A, Hawtin P, Flavell L, et al. Crystal structure of the catalytic domain of the human aggrecanase ADAMTS-1. Transactions of the 53rd Annual Meeting of the Orthopedic Research Society 2007: Paper 0081.
27. Shieh H, Mathis K, Williams J, Hills R, Wiese J, Benson T, et al. High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2). J Biol Chem 2008; 283: 1501-7.
28. Seidah N, Prat A. Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem 2002; 38: 79-94.
29. Longpre J, Leduc R. Identification of pro-domain determinants involved in ADAMTS-1 biosynthesis. J Biol Chem 2004; 279: 33237-45.
30. Wang P, Tortorella M, England K, Malfait AM, Thomas G, Arner EC, et al. Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network. J Biol Chem 2004; 279: 15434-40.
31. Malfait A, Arner E, Song R, Alston J, Markosyan S, Staten N, et al. Proprotein convertase activation of aggrecanases in cartilage in situ. Arch Biochem Biophys 2008; 478: 43-51.
32. Longpre JM, McCulloch DR, Koo BH, Alexander JP, Apte SS, Leduc R. Characterization of proADAMTS5 processing by proprotein convertases. Int J Biochem Cell Biol 2009; 41: 1116-26.
33. Koo BH, Longpre JM, Somerville PT, Alexander JP, Leduc R, Apte SS. Cell-surface processing of pro-ADAMTS9 by furin. J Biol Chem 2006; 281: 12485-94.
34. Somerville RP, Longpre JM, Apel ED, Lewis RM, Wang LW, Leduc R, et al. ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulphate-proteoglycan containing a mucin domain. J Biol Chem 2004; 279: 35159-75.
35. Somerville RP, Jungers KA, Apte SS. Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation. J Biol Chem 2004; 279: 51208-17.
36. Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science 2002; 295: 2387-92.
37. Porter S, Clark I, Kevorkian L, Edwards D. The ADAMTS metalloproteinases. Biochem J 2005; 386: 15-27.
38. Iozzo RV, Murdoch AD. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J 1996; 10: 598-614.
39. Patwari P, Kurz B, Sandy JD, Grodzinsky AJ. Mannosamine inhibits aggrecanase-mediated changes in the physical properties and biochemical composition of articular cartilage. Arch Biochem Biophys 2000; 374: 79-85.
40. 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.
41. 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.
42. 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.
43. Collins-Racie LA, Flannery C, Zeng W, Corr M, Annis-Freeman B, Agostino MJ, et al. ADAMTS-8 exhbits aggrecanase activity and is expressed in human articular cartilage. Matric Biol 2004; 23: 219-30.
44. Flannery C. MMPs and ADAMTSs: Functional studies. Front Biosci 2006; 11: 544-69.
45. Tortorella MD, Malfait AM. Will the real aggrecanase(s) step up: evaluating the criteria that define aggrecanase activity in osteoarthritis. Curr Pharm Biotechnol 2008; 9: 16-23.
46. Little C, Mittaz L, Belluoccio D, Rogerson F, Campbell IK, Meeker CT, et al. ADAMTS-1 knockout mice do not exhibit abnormalities inaggrecan turnover in vitro ir in vivo. Arthritis Rheum 2005; 52: 1461-72.
47. Glasson SS, Askew R, Sheppard B, Carito bA, Blanchet T, Ma HL, et al. Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice. Arthritis Rheum 2004; 50: 2547-58.
48. Glasson S, Askew R, Sheppard, B, Carito B, Blanchet T, Ma H, et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 2005; 434: 644-8.
49. Majumdar MK, Askew R, Schelling S, Stedman N, Blanchet T, Hopkins B, et al. Double-knockout of ADAMTS-4 and ADAMTS-5 in mice results in physiologically normal animals and prevents the progression of osteoarthritis. Arthritis Rheum 2007; 56: 3670-4.
50. Botter SM, Glasson SS, Hopkins B, Clockaerts S, van Leeuwen JP, Weinans H, et al. ADAMTS5-/- mice have less subchondral bone changes after induction of osteoarthritis through surgical instability: Implications for a link between cartilage and subchondral bone changes. Osteoarthritis Cartilage 2008; Oct 17 [ePub ahead of publication].
51. Song RH, Tortorella MD, Malfait AM, Yang Z, Alston JT, Arner EC, et al. Aggrecan Degradation in Human Articular Cartilage Explants is Mediated by Both ADAMTS-4 and ADAMTS-5. Arthritis Rheum 2007; 56: 575-85.
52. Kevorkian L, Young D, Darrah C, Donell S, Shepstone L, Porter S, et al. Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 2004;50: 131-41.
53. Davidson R, Waters J, Kevorkian L, Darrah C, Cooper A, Donell S, et al. Expression profiling of metalloproteinases and their inhibitors in synovium and cartilage. Arthritis Res Ther 2006; 8: R124.
54. Rodriguez-Lopez J, Mustafa Z, Pombo-Suarez M, Malizos K, Rego I, Blanco F, et al. Genetic variation including nonsynonymous polymorphisms of a major aggrecanase, ADAMTS-5, in susceptibility to osteoarthritis. Arthritis Rheum 2008; 58: 435-41.
55. Rodriguez-Lopez J, Pombo-Suarez M, Loughlin J, Tsezou A, Blanco F, Meulenbelt I, et al. Association of a nsSNP in ADAMTS14 to some osteoarthritis phenotypes. Osteoarthritis Cartilage 2008; 3: 321-7.
56. Sandy J, Westling J, Kenagy R, Iruela-Arispe M, Verscharen C, Rodriguez-Manzaneque J, et al. Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4. J Biol Chem 2001; 276: 13372-8.
57. Westling J, Gottschall P, Thompson V, Cockburn A, Perides G, Zimmermann D, et al. ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein Biochem J 2004; 377: 787-95.
58. Silver DL, Hou L, Somerville R, Young ME, Apte SS, Pavan WJ. The secreted metalloprotease ADAMTS20 is required for melanoblast survival. PLoS Genet 2008; 4(2): E1000003.
59. Kenagy RD, Plaas AH, Wight TN. Versican degradation and vascular disease. Trends Cardiovasc Med 2006; 6: 209-15.
60. Worley J, Baugh M, Hughes D, Edwards D, Hogan A, Sampson M, et al. Metalloproteinase expression in PMA-stimulated THP-1 cells. Effects of peroxisome proliferator-activated receptor-gamma (PPAR gamma) agonists and 9-cis-retinoic acid. J Biol Chem 2003; 278: 51340-6.
61. Wagsater D, Bjork H, Zhu C, Bjorkegren J, Valen G, Hamsten A, et al. ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques. Atherosclerosis 2008; 196: 514-22.
62. Richards JS, Hernandez-Gonzalez I, Gonzalez-Robayna I, Teuling E, Lo Y, Boerboom D, et al. Regulated expression of ADAMTS family members in follicles and cumulus oocyte complexes: Evidence for specific and redundant patterns during ovulation. Biol Reprod 2005; 72: 1241-55.
63. 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: 177-80.
64. Medina-Flores R, Wang G, Bissel S, Murphey-Corb M, Wiley C. Destruction of extracellular matrix proteoglycans is pervasive in simian retroviral neuroinfection. Neurobiol Dis 2004; 16: 604-1.
65. Miguel RF, Pollak A, Lubec G. Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimer's and Pick's disease. Brain Res 2005; 133: 1-5.
66. Haddock G, Cross AK, Plumb J, Surr J, Buttle DJ, Bunning RA, et al. Expression of ADAMTS-1, -4, -5 and TIMP-3 in normal and multiple sclerosis CNS white matter. Multi Scler 2006; 12(4): 386-96.
67. Matthews R, Gary S, Zerillo C, Pratta M, Solomon K, Arner E, et al. Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member. J Biol Chem 2000; 275: 22695-703.
68. Nakamura H, Fujii Y, Inoki I, Sugimoto K, Tanzawa K, Matsuki H, et al. Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. J Biol Chem 2000; 275: 38885-90.
69. Nakada M, Miyamori H, Kita D, Takahashi T, Yamashita J, Sato H, et al. Human glioblastomas overexpress ADAMTS-5 that degrades brevican. Acta Neuropathol 2005; 110: 239-46.
70. Iruela-Arispe ML, Carpizo D, Luque A. ADAMTS1: A matrix metalloprotease with angioinhibitory properties. Ann NY Acad Sci 2003 ; 995: 183-90
71. Liu Y, Xu Y, Yu Q. Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively. Oncogene 2006; 25: 2452-67.
72. Jungers KA, Le Goff C, Somerville RP, Apte SS. Adamts9 is widely expressed during mouse embryo development. Gene Expr Patterns 2005; 5: 609-17.
73. Kleivi K, Lind G, Diep C, Meling G, Brandal L, Nesland J, et al. Gene expression profiles of primary colorectal carcinomas, liver metastases, and carcinomatoses. Mol Cancer 2007; 6: 2.
74. Lung HL, Lo PH, Xie D, Apte SS, Cheung AK, Cheng Y, et al. Characterization of a novel epigenetically-silenced, growth-suppressive gene, ADAMTS9, and its association with lymph node metastases in nasopharyngeal carcinoma. Int J Cancer 2008; 123: 401-8.
75. Zeggini E, Scott LJ, Saxena R, Voight BF, Marchini JL, Hu T, et al. Meta-analysis of genome-wide association data and large-scale replication identifies additional susceptibility loci for type 2 diabetes. Nat Genet 2008; 40: 638-45.
76. Rao C, Foernzler D, Loftus SK, Liu S, McPherson JD, Jungers KA, et al. A defect in a novel ADAMTS family member is the cause of the belted white-spotting mutation. Development 2003; 130: 4665-72.
77. Kessler E, Takahara K, Biniaminov L, Brusel M, Greenspan DS. Bone morphogenetic protein-1: The type I procollagen C-proteinase. Science 1996; 271: 360-2.
78. Li SW, Sieron AL, Fertala A, Hojima Y, Arnold WV, Prockop DJ. The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. Proc Natl Acad Sci USA 1996 ;93: 5127-30.
79. Scott IC, Blitz IL, Pappano WN, Imamura Y, Clark TG, Steiglitz BM, et al. Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis. Dev Biol 1999; 213: 283-300.
80. Nusgens B, Verellen-Dumoulin C, Hermanns-Lê T, De Paepe A, Nuytinck L, Piérard G, et al. Evidence for a relationship between Ehlers-Danlos type VII C in humans and bovine dermatosparaxis. Nat Genet 1992;1: 214-7.
81. Colige A, Nuytinck L, Hausser I, van Essen AJ, Thiry M, Herens C, et al. Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene. J Invest Dermatol 2004; 123: 656-63.
82. Smith LT, Wertelecki W, Milstone LM, Petty EM, Seashore MR, Braverman IM, et al. Human dermatosparaxis: A form of Ehlers-Danlos syndrome that results from failure to remove the amino-terminal propeptide of type I procollagen. Am J Hum Genet 1992; 51: 235-44.
83. Wertelecki W, Smith LT, Byers P. Initial observations of human dermatosparaxis: Ehlers-Danlos syndrome type VIIC. J Pediatr 1992; 121(4): 558-64.
84. Petty EM, Seashore MR, Braverman IM, Spiesel SZ, Smith LT, Milstone LM. Dermatosparaxis in children. A case report and review of the newly recognized phenotype. Arch Dermatol 1993; 129: 1310-5.
85. Reardon W, Winter RM, Smith LT, Lake BD, Rossiter M, Baraitser M. The natural history of human dermatosparaxis (Ehlers-Danlos syndrome type VIIC). Clin Dysmorphol 1995; 4: 1-11.
86. Fujimoto A, Wilcox WR, Cohn DH. Clinical, morphological, and biochemical phenotype of a new case of Ehlers-Danlos syndrome type VIIC. Am J Med Genet 1997; 68: 25-8.
87. Pasch MC, Sillevis Smitt JH, Veenhuizen L, Kuiters GR, van Essen AJ. [Boy with dermatosparaxis (Ehlers-Danlos type VIIC)]. Ned Tijdschr Geneesk 2000; 144: 2435-6.
88. Hanset R, Ansay M. Dermatosparaxie (peau déchirée) chez le veau: Un défaut général du tissue conjonctif, de nature héréditaire. Ann Med Vet 1967;7: 451-70.
89. Malfait F, De Coster P, Hausser I, van Essen AJ, Franck P, Colige A, et al. The natural history, including orofacial features of three patients with Ehlers-Danlos syndrome, dermatosparaxis type (EDS type VIIC). Am J Med Genet 2004;131: 18-28.
90. Li S, Arita M, Fertala A, Bao Y, Kopen G, Langsjo T, et al. Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility. Biochem J 2001; 355: 271-8.
91. Kesteloot F, Desmoulière A, Leclercq I, Thiry M, Arrese J, Prockop D, et al. ADAM metallopeptidase with thrombospondin type 1 motif 2 inactivation reduces the extent and stability of carbon tetrachloride-induced hepatic fibrosis in mice. Hepatology 2007; 46: 1620-31.
92. Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, et al. Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase. J Biol Chem 2003; 278: 19549-57.
93. Colige A, Ruggiero F, Vandenberghe I, Dubail J, Kesteloot F, Van Beeumen J, et al. Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V. J Biol Chem 2005; 280: 34397-408.
94. Tuderman L, Prockop DJ. Procollagen N-proteinase. Properties of the enzyme purified from chick embryo tendons. Eur J Biochem/FEBS 1982; 125: 545-9.
95. Peltonen L, Halila R, Ryhanen L. Enzymes converting procollagens to collagens. J Cell Biochemy 1985; 28: 15-21.
96. Halila R, Peltonen L. Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum. Biochem J 1986; 239: 47-52.
97. Halila R, Steinmann B, Peltonen L. Processing of types I and III procollagen in Ehlers-Danlos syndrome type VII. Am J Hum Genet 1986; 39: 222-31.
98. Le Goff C, Somerville RP, Kesteloot F, Powell K, Birk DE, Colige AC, et al. Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases: Insights on collagen biosynthesis and dermatosparaxis. Development 2006; 133: 1587-96.
99. Lapiere CM, Nusgens BV. Ehlers-Danlos type VII-C, or human dermatosparaxis. The offspring of a union between basic and clinical research. Arch Dermatol 1993;129: 1316-9.
100. Fernandes RJ, Hirohata S, Engle JM, Colige A, Cohn DH, Eyre DR, et al. Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. J Biol Chem 2001;276: 31502-9.
101. Colige A, Vandenberghe I, Thiry M, Lambert CA, Van Beeumen J, Li SW, et al. Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. J Biol Chem 2002; 277: 5756-66.
102. Imamura Y, Steiglitz BM, Greenspan DS. Bone morphogenetic protein-1 processes the NH2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-alpha1(V) collagen. J Biol Chem 1998;273: 27511-7.
103. Gopalakrishnan B, Wang WM, Greenspan DS. Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) pro-collagen heterotrimer. J Biol Chem 2004; 279: 30904-12.
104. Unsold C, Pappano WN, Imamura Y, Steiglitz BM, Greenspan DS. Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases. J Biol Chem 2002; 277: 5596-602.
105. Liu CJ, Kong W, Ilalov K, Yu S, Xu K, Prazak L, et al. ADAMTS-7: A metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein. FASEB J 2006; 20: 988-90.
106. Liu CJ, Kong W, Xu K, Luan Y, Ilalov K, Sehgal B, et al. ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein. J Biol Chem 2006; 281: 15800-8.
107. Luan Y, Kong L, Howell DR, Ilalov K, Fajardo M, Bai XH, et al. Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin. Osteoarthritis Cartilage 2008; 11: 1413-20.
108. Ruggeri ZM. Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost 2003; 1: 1335-42.
109. 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: 1662-6.
110. Soejima K, Mimura N, Hirashima M, Maeda H, Hamamoto T, Nakagaki T, et al. A novel human metalloprotease synthesized in the liver and secreted into the blood: Possibly, the von Willebrand factor-cleaving protease? J Biochem 2001; 130: 475-80.
111. Levy G, Nichols W, Uan E, Foroud T, McClintick J, McGee B, et al. Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature 2001; 413: 488-94.
112. Schneppenheim R, Kremer Hovinga J, Becker T, Budde U, Karpman D, Brockhaus W, et al. A common origin of the 4143insA ADAMTS13 mutation. Thromb Haemost 2006; 96: 3-6.
113. Plaimauer B, Fuhrmann J, Mohr G, Wernhart W, Bruno K, Ferrari S, et al. Modulation of ADAMTS13 secretion and specific activity by a combination of common amino acid polymorphisms and a missense mutation. Blood 2006; 107: 118-25.
114. Furlan M, Robles R, Galbusera M, Remuzzi G, Kyrle PA, Brenner B, et al. von Willebrand factor-cleaving protease in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome. N Engl J Med 1998; 339: 1578-84.
115. Soejima K, Matsumoto M, Kokame K, Yagi H, Ishizashi H, Maeda H, et al. ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage. Blood 2003; 102: 3232-7.
116. Klaus C, Plaimauer B, Studt JD, Dorner F, Lammle B, Mannucci PM, et al. Epitope mapping of ADAMTS13 autoantibodies in acquired thrombotic thrombocytopenic purpura. Blood 2004; 103: 4514-9.
117. Porter S, Scott SD, Sassoon EM, Williams MR, Jones JL, Girling AC, et al. Dysregulated expression of adamalysin-thrombospondin genes in human breast carcinoma. Clin Cancer Res 2004; 10: 2429-40.
118. Johnston P, Chojnowski A, Davidson R, Riley G, Donell S, Clark I. A complete expression profile of matrix-degrading metalloproteinases in Dupuytren's disease. J Hand Surg Am 2007;32: 343-51.
119. Johnston P, Larson D, Clark I, Chojnowski A. Metalloproteinase gene expression correlates with clinical outcome in Dupuytren's disease. J Hand Surg Am 2008; 33: 1160-7.
120. Gao S, De Geyter C, Kossowska K, Zhang H. FSH stimulates the expression of the ADAMTS-16 protease in mature human ovarian follicles. Mol Hum Reprod 2007; 13: 465-71.
121. Faivre L, Dollfus H, Lyonnet S, Alembik Y, Megarbane A, Samples J, et al. Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome. Am J Med Genet 2003; 123A(2): 204-7.
122. Dagoneau N, Benoist-Lasselin C, Huber C, Faivre L, Megarbane A, Alswaid A, et al. ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome. Am J Hum Genet 2004; 75: 801-6.
123. Kutz WE, Wang LW, Dagoneau N, Odrcic KJ, Cormier-Daire V, Traboulsi EI, et al. Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme. Hum Mutat 2008; 29: 1425-34.
124. Wirtz MK, Samples JR, Kramer PL, Rust K, Yount J, Acott TS, et al. Weill-Marchesani syndrome--possible linkage of the autosomal dominant form to 15q21.1. Am J Med Genet 1996; 65: 68-75.
125. Faivre L, Gorlin RJ, Wirtz MK, Godfrey M, Dagoneau N, Samples JR, et al. In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome. J Med Genet 2003; 40: 34-6.
126. Yao W, Chao M, Wasserman ZR, Liu RQ, Covington MB, Newton R, et al. Potent P1' biphenylmethyl substituted aggrecanase inhibitors. Bioorg Med Chem Lett 2002; 12: 101-4.
127. Zeng W, Corcoran C, L.A. C-R, Lavallie ER, Morris EA, Flannery CR. Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: Comparative analysis with ADAMTS-5, -9, -6 and -18. Biochem Biophys Acta 2006;1760: 517-24.
128. Troeberg L, Fushimi K, Khokha R, Emonard H, Ghosh P, Nagase H. Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases. FASEB J 2008; 10: 3515-24.
129. Wittwer AJ, Hills RL, Keith RH, Munie GE, Arner EC, Anglin CP, et al. Substrate-dependent inhibition kinetics of an active site-directed inhibitor of ADAMTS-4 (Aggrecanase 1). Biochemistry, 2007;46: 6393-401.
130. Yokoyama H, Wada T, Kobayashi K, Kuno K, Kurihara H, Shindo T, et al. 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.
131. Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, et al. ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 2005; 434: 648-52.
132. Chen J, Boyd L, Allen K, Tsuboyama M, Jing L, Malfait A, et al. Evaluation of intervertebral disc and vertebral endplate degeneration in ADAMTS-5 (aggrecanase-2) knock-out mice Osteoarthritis Research Society International World Congress on Osteoarthritis, December 6 - 9, Ft Lauderdale, Florida (abstract) 2007.
133. Motto DG, Chauhan AK, Zhu G, Homeister J, Lamb CB, Desch KC, et al. Shigatoxin triggers thrombotic thrombocytopenic purpura in genetically susceptible ADAMTS13-deficient mice. J Clin Invest 2005; 115: 2752-61.
134. Goertsches R, Comabella M, Navarro A, Perkal H, Montalban X. Genetic association between polymorphisms in the ADAMTS14 gene and multiple sclerosis. J Neuroimmunol 2005; 164: 140-7.
135. Kokame K, Matsumoto M, Soejima K, Yagi H, Ishizashi H, Funato M, et al. Mutations and common polymorphisms in ADAMTS13 gene responsible for von Willebrand factor-cleaving protease activity. Proc Natl Acad Sci USA 2002; 99: 11902-7.
136. Jang MJ, Kim NK, Chong SY, Kim HJ, Lee SJ, Kang MS, et al. Frequency of Pro475Ser polymorphism of ADAMTS13 gene and its association with ADAMTS-13 activity in the Korean population. Yonsei Med J 2008; 49: 405-8.
137. Bongers TN, De Maat MP, Dippel DW, Uitterlinden AG, Leebeek FW. Absence of Pro475Ser polymorphism in ADAMTS-13 in Caucasians. J Thromb Haemost 2005; 3: 805.
138. Masui T, Hosotani R, Tsuji S, Miyamoto Y, Yasuda S, Ida J, et al. Expression of METH-1 and METH-2 in pancreatic cancer. Clin Cancer Res 2001;7: 3437-43.
139. Lind G, Kleivi K, Meling G, Teixeira M, Thiis-Evensen E, Rognum T, et al. ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis. Cell Oncol 2006;28: 259-72.
140. Rocks N, Paulissen G, Quesada C, Polette M, Gueders M, Munaut C, et al. Expression of a disintegrin and metalloprotease (ADAM and ADAMTS) enzymes in human non-small-cell lung carcinomas (NSCLC). Br J Cancer 2006; 94: 724-30.
141. Jonsson-Rylander AC, Nilsson T, Fritsche-Danielson R, Hammarstrom A, Behrendt M, Andersson JO, et al. Role of ADAMTS-1 in atherosclerosis: Remodeling of carotid artery, immunohistochemistry, and proteolysis of versican. Arterioscler, Thromb Vasc Biol 2005;25: 180-5.
142. Le Maitre C, Freemont A, Hoyland J. Localization of degradative enzymes and their inhibitors in the degenerate human intervertebral disc. J Pathol 2004; 1(204): 47-54.
143. Held-Feindt J, Paredes EB, Blomer U, Seidenbecher C, Stark AM, Mehdorn HM, et al. Matrix-degrading proteases ADAMTS4 and ADAMTS5 (disintegrins and metalloproteinases with thrombospondin motifs 4 and 5) are expressed in human glioblastomas. Int J Cancer 2006;118: 55-61.
144. Corps A, Jones G, Harrall R, Curry V, Hazleman B, Riley G. The regulation of aggrecanase ADAMTS-4 expression in human Achilles tendon and tendon-derived cells. Matrix Biol 2008; 27: 393-401.
145. Dunn J, Reed J, du Plessis D, Shaw E, Reeves P, Gee A, et al. Expression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumours. Br J Cancer 2006; 94: 1186-93.
146. Porter S, Span P, Sweep F, Tjan-Heijnen V, Pennington C, Pedersen T, et al. ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma. Int J Cancer 2006; 118: 1241-7.
147. Roy R, Louis G, Loughlin KR, Wiederschain D, Kilroy SM, Lamb CC, et al. Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clin Cancer Res 2008; 14: 6610-7.