Lapiere C.M., Lenaers A., Kohn L.D. Procollagen peptidase: an enzyme excising the coordination peptides of procollagen. Proc Natl Acad Sci U S A 1971, 68:3054-3058.
Lenaers A., Ansay M., Nusgens B.V., Lapiere C.M. Collagen made of extended-chains, procollagen, in genetically-defective dermatosparaxic calves. Eur J Biochem 1971, 23:533-543.
Tuderman L., Kivirikko K.I., Prockop D.J. Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen. Biochemistry 1978, 17:2948-2954.
Hojima Y., Morgelin M.M., Engel J., Boutillon M.M., van der Rest M., McKenzie J., et al. Characterization of type I procollagen N-proteinase from fetal bovine tendon and skin. Purification of the 500-kilodalton form of the enzyme from bovine tendon. J Biol Chem 1994, 269:11381-11390.
Colige A., Beschin A., Samyn B., Goebels Y., Van Beeumen J., Nusgens B.V., et al. Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen. J Biol Chem 1995, 270:16724-16730.
Colige A., Li S.W., Sieron A.L., Nusgens B.V., Prockop D.J., Lapiere C.M. 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 U S A 1997, 94:2374-2379.
Colige A., Sieron A.L., Li S.W., 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, 65:308-317.
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.
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., et al. Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res 1997, 4:141-150.
Fernandes R.J., Hirohata S., Engle J.M., Colige A., Cohn D.H., Eyre D.R., et al. Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. J Biol Chem 2001, 276:31502-31509.
Le Goff C., Apte S.S. ADAMTS3 and ADAMTS14: procollagen peptidases that provide insight into the clinical presentation of dermatosparaxis 2005, c2005. Springer, Dordecht, The Netherlands, [Dordecht].
Bolz H., Ramirez A., von Brederlow B., Kubisch C. Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family. Biochim Biophys Acta 2001, 1522:221-225.
Cal S., Obaya A.J., 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.
Colige A., Vandenberghe I., Thiry M., Lambert C.A., Van Beeumen J., Li S.W., et al. Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3. J Biol Chem 2002, 277:5756-5766.
Jones G.C., Riley G.P. ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Res Ther 2005, 7:160-169.
Wang W.M., Lee S., Steiglitz B.M., Scott I.C., Lebares C.C., Allen M.L., et al. Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase. J Biol Chem 2003, 278:19549-19557.
Kesteloot F., Desmouliere A., Leclercq I., Thiry M., Arrese J.E., Prockop D.J., 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, 46:1620-1631.
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, 280:34397-34408.
Porter S., Clark I.M., Kevorkian L., Edwards D.R. The ADAMTS metalloproteinases. Biochem J 2005, 386:15-27.
Wang W.M., Ge G., Lim N.H., Nagase H., Greenspan D.S. TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2. Biochem J 2006, 398:515-519.
Lim N.H., Kashiwagi M., Visse R., Jones J., Enghild J.J., Brew K., et al. Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications. Biochem J 2010, 431:113-122.
Kramerova I.A., Kawaguchi N., Fessler L.I., Nelson R.E., Chen Y., Kramerov A.A., et al. Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases. Development 2000, 127:5475-5485.
Dubail J., Kesteloot F., Deroanne C., Motte P., Lambert V., Rakic J.M., et al. ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity. Cell Mol Life Sci 2010, 67:4213-4232.
Le Goff C., Somerville R.P., Kesteloot F., Powell K., Birk D.E., Colige A.C., 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, 133:1587-1596.
Cabral W.A., Makareeva E., Colige A., Letocha A.D., Ty J.M., Yeowell H.N., et al. Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing. J Biol Chem 2005, 280:19259-19269.
Halila R., Peltonen L. Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum. Biochem J 1986, 239:47-52.
Nusgens B.V., Goebels Y., Shinkai H., Lapiere C.M. Procollagen type III N-terminal endopeptidase in fibroblast culture. Biochem J 1980, 191:699-706.
Imamura Y., Steiglitz B.M., Greenspan D.S. 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, 273:27511-27517.
Gopalakrishnan B., Wang W.M., Greenspan D.S. Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer. J Biol Chem 2004, 279:30904-30912.
Jeltsch M., Jha S.K., Tvorogov D., Anisimov A., Leppanen V.M., Holopainen T., et al. CCBE1 enhances lymphangiogenesis via a disintegrin and metalloprotease with thrombospondin motifs-3-mediated vascular endothelial growth factor-C activation. Circulation 2014, 129:1962-1971.
Shi H., Huang Y., Zhou H., Song X., Yuan S., Fu Y., et al. Nucleolin is a receptor that mediates antiangiogenic and antitumor activity of endostatin. Blood 2007, 110:2899-2906.
Hofer T.P., Frankenberger M., Mages J., Lang R., Meyer P., Hoffmann R., et al. Tissue-specific induction of ADAMTS2 in monocytes and macrophages by glucocorticoids. J Mol Med (Berl) 2008, 86:323-332.
Li S.W., Arita M., Fertala A., Bao Y., Kopen G.C., Langsjo T.K., et al. Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility. Biochem J 2001, 355:271-278.
Beighton P., De Paepe A., Steinmann B., Tsipouras P., Wenstrup R.J. Ehlers-Danlos syndromes: revised nosology, Villefranche, 1997. Ehlers-Danlos National Foundation (USA) and Ehlers-Danlos Support Group (UK). Am J Med Genet 1998, 77:31-37.
Malfait F., De Paepe A. The Ehlers-Danlos syndrome. Adv Exp Med Biol 2014, 802:129-143.
Colige A., Nuytinck L., Hausser I., van Essen A.J., 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, 123:656-663.
Malfait F., De Coster P., Hausser I., van Essen A.J., 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 A 2004, 131:18-28.
Arning A., Hiersche M., Witten A., Kurlemann G., Kurnik K., Manner D., et al. A genome-wide association study identifies a gene network of ADAMTS genes in the predisposition to pediatric stroke. Blood 2012, 120:5231-5236.
Lee C.W., Hwang I., Park C.S., Lee H., Park D.W., Kang S.J., et al. Expression of ADAMTS-2, -3, -13, and -14 in culprit coronary lesions in patients with acute myocardial infarction or stable angina. J Thromb Thrombolysis 2012, 33:362-370.
Goertsches R., Comabella M., Navarro A., Perkal H., Montalban X. Genetic association between polymorphisms in the ADAMTS14 gene and multiple sclerosis. J Neuroimmunol 2005, 164:140-147.
Poonpet T., Honsawek S., Tammachote N., Kanitnate S., Tammachote R. ADAMTS14 gene polymorphism associated with knee osteoarthritis in Thai women. Genet Mol Res 2013, 12:5301-5309.
Rodriguez-Lopez J., Pombo-Suarez M., Loughlin J., Tsezou A., Blanco F.J., Meulenbelt I., et al. Association of a nsSNP in ADAMTS14 to some osteoarthritis phenotypes. Osteoarthr Cartil 2009, 17:321-327.