ADAMTS2 is responsible for processing several types of procollagenproteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off one end of the procollagen. This clipping step is necessary for collagen molecules to function normally and assemble into fibrils outside cells.
Ehlers-Danlos syndrome, dermatosparaxis type is caused by mutations in the ADAMTS2 gene. Several mutations in the ADAMTS2 gene have been identified in people with this syndrome. These mutations greatly reduce the production of the enzyme made by the ADAMTS2 gene. Procollagen cannot be processed correctly without this enzyme. As a result, collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue (the tissue that binds and supports the body's muscles, ligaments, organs, and skin), which causes the signs and symptoms of the disorder.
^ abColige A, Nuytinck L, Hausser I, van Essen AJ, Thiry M, Herens C, Adès LC, Malfait F, Paepe AD, Franck P, Wolff G, Oosterwijk JC, Smitt JH, Lapière CM, Nusgens BV (October 2004). "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.123 (4): 656–63. doi:10.1111/j.0022-202X.2004.23406.x. PMID15373769.
Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, Brenner MC, Takahara K, Greenspan DS (May 2003). "Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase". J. Biol. Chem.278 (21): 19549–57. doi:10.1074/jbc.M300767200. PMID12646579.
Colige A, Vandenberghe I, Thiry M, et al. (2002). "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3". J. Biol. Chem.277 (8): 5756–66. doi:10.1074/jbc.M105601200. PMID11741898.
Kevorkian L, Young DA, Darrah C, et al. (2004). "Expression profiling of metalloproteinases and their inhibitors in cartilage". Arthritis Rheum.50 (1): 131–41. doi:10.1002/art.11433. PMID14730609.
Hurskainen TL, Hirohata S, Seldin MF, Apte SS (1999). "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.274 (36): 25555–63. doi:10.1074/jbc.274.36.25555. PMID10464288.
Dubail J, Kesteloot F, Deroanne C, et al. (2010). "ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity". Cellular and molecular life sciences : CMLS67 (24): 4213–32. doi:10.1007/s00018-010-0431-6. PMID20574651.
Colige A, Ruggiero F, Vandenberghe I, et al. (2005). "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.280 (41): 34397–408. doi:10.1074/jbc.M506458200. PMID16046392.
Brandenberger R, Wei H, Zhang S, et al. (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol.22 (6): 707–16. doi:10.1038/nbt971. PMID15146197.
Tomii Y, Kamochi J, Yamazaki H, et al. (2002). "Human thrombospondin 2 inhibits proliferation of microvascular endothelial cells". Int. J. Oncol.20 (2): 339–42. doi:10.3892/ijo.20.2.339. PMID11788898.