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Its primary function is to process collagen type I, II, III, and V precursors into mature molecules by excising the aminopropeptide. This process allows the correct assembly of collagen molecules into fibrils and fibers, which confers to connective tissues their architectural structure and mechanical resistance. To evaluate the impact of ADAMTS2 on the pathological accumulation of extracellular matrix proteins, mainly type I and III collagens, we evaluated carbon tetrachloride\u2013induced liver fibrosis in ADAMTS2-deficient (TS2\u2212\/\u2212) and wild-type (WT) mice. A single carbon tetrachloride injection caused a similar acute liver injury in deficient and WT mice. A chronic treatment induced collagen deposition in fibrous septa that were made of thinner and irregular fibers in TS2\u2212\/\u2212 mice. The rate of collagen deposition was slower in TS2\u2212\/\u2212 mice, and at an equivalent degree of fibrosis, the resorption of fibrous septa was slightly faster. Most of the genes involved in the development and reversion of the fibrosis were similarly regulated in TS2\u2212\/\u2212 and WT mice.<\/jats:bold>\n                              <\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion:<\/jats:title>\n            <jats:p>\n                                 <jats:bold>These data indicate that the extent of fibrosis is reduced in TS2\u2212\/\u2212 mice in comparison with their WT littermates. Inhibiting the maturation of fibrillar collagens may be a beneficial therapeutic approach to interfering with the development of fibrotic lesions.<\/jats:bold>\n                              <\/jats:p>\n          <\/jats:sec>","DOI":"10.1002\/hep.21868","type":"journal-article","created":{"date-parts":[[2007,10,10]],"date-time":"2007-10-10T21:16:25Z","timestamp":1192050985000},"page":"1620-1631","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":64,"title":["ADAM metallopeptidase with thrombospondin type 1 motif 2 inactivation reduces the extent and stability of carbon tetrachloride\u2013induced hepatic fibrosis in mice"],"prefix":"10.1097","volume":"46","author":[{"given":"Fr\u00e9d\u00e9ric","family":"Kesteloot","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexis","family":"Desmouli\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Leclercq","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc","family":"Thiry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge E.","family":"Arrese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darwin J.","family":"Prockop","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles M.","family":"Lapi\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Betty V.","family":"Nusgens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain","family":"Colige","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"R1-35-20241201","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1055\/s-2008-1040452","article-title":"Structure of the extracellular matrix in normal and fibrotic liver: collagens and glycoproteins.","volume":"10","author":"Schuppan","year":"1990","journal-title":"Semin Liver Dis"},{"key":"R2-35-20241201","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/j.jhep.2004.03.007","article-title":"Cirrhosis reversal: a duel between dogma and myth.","volume":"40","author":"Desmet","year":"2004","journal-title":"J Hepatol"},{"key":"R3-35-20241201","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/S0168-8278(98)80269-9","article-title":"Molecular regulation of hepatic fibrogenesis.","volume":"29","author":"Olaso","year":"1998","journal-title":"J Hepatol"},{"key":"R5-35-20241201","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1172\/JCI24282","article-title":"Liver fibrosis.","volume":"115","author":"Bataller","year":"2005","journal-title":"J Clin Invest"},{"key":"R6-35-20241201","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.cca.2005.06.014","article-title":"Mechanisms of liver fibrosis.","volume":"364","author":"Tsukada","year":"2006","journal-title":"Clin Chim Acta"},{"key":"R7-35-20241201","doi-asserted-by":"crossref","first-page":"5127","DOI":"10.1073\/pnas.93.10.5127","article-title":"The Cproteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein1.","volume":"93","author":"Li","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R8-35-20241201","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1126\/science.271.5247.360","article-title":"Bone morphogenetic protein1: the type I procollagen Cproteinase.","volume":"271","author":"Kessler","year":"1996","journal-title":"Science"},{"key":"R9-35-20241201","doi-asserted-by":"crossref","first-page":"3054","DOI":"10.1073\/pnas.68.12.3054","article-title":"Procollagen peptidase: an enzyme excising the coordination peptides of procollagen.","volume":"68","author":"Lapiere","year":"1971","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R10-35-20241201","doi-asserted-by":"crossref","first-page":"2374","DOI":"10.1073\/pnas.94.6.2374","article-title":"cDNA cloning and expression of bovine procollagen I Nproteinase: a new member of the superfamily of zincmetalloproteinases with binding sites for cells and other matrix components.","volume":"94","author":"Colige","year":"1997","journal-title":"Proc Natl Acad Sci U S A"},{"key":"R11-35-20241201","doi-asserted-by":"crossref","first-page":"31502","DOI":"10.1074\/jbc.M103466200","article-title":"Procollagen II amino propeptide processing by ADAMTS3. 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