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Transforming growth factor-{beta} induces secretion of activated ADAMTS-2: a procollagen III N-proteinase.
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Wang, Wei-Man | - |
dc.contributor.author | Lee, Seungbok | - |
dc.contributor.author | Steiglitz, Barry M | - |
dc.contributor.author | Scott, Ian C | - |
dc.contributor.author | Lebares, Carter C | - |
dc.contributor.author | Leah Allen, M | - |
dc.contributor.author | Brenner, Mitchell C | - |
dc.contributor.author | Takahara, Kazuhiko | - |
dc.contributor.author | Greenspan, Daniel S | - |
dc.date.accessioned | 2010-09-03T01:12:43Z | - |
dc.date.available | 2010-09-03T01:12:43Z | - |
dc.date.issued | 2003-05 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY 278, 19549-19557 | en |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://hdl.handle.net/10371/69618 | - |
dc.description.abstract | The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mutations in the ADAMTS-2 gene in dermatosparaxis and Ehlers-Danlos syndrome VIIC show this enzyme to be responsible in vivo for most biosynthetic processing of procollagen I N-propeptides in skin. Yet despite its important role in the regulation of collagen deposition, information regarding regulation and substrate specificity of ADAMTS-2 has remained sparse. Here we demonstrate that ADAMTS-2 can, like the procollagen C-proteinases, be regulated by transforming growth factor-β1 (TGF-β1), with implications for mechanisms whereby this growth factor effects net increases in formation of extracellular matrix. TGF-β1 induced ADAMTS-2 mRNA ∼8-fold in MG-63 osteosarcoma cells in a dose- and time-dependent, cycloheximide-inhibitable manner, which appeared to operate at the transcriptional level. Secreted ADAMTS-2 protein induced by TGF-β1 was 132 kDa and was identical in size to the fully processed, active form of the protease. Biosynthetic processing of ADAMTS-2 to yield the 132-kDa form is shown to be a two-step process involving sequential cleavage by furin-like convertases at two sites. Surprisingly, purified recombinant ADAMTS-2 is shown to cleave procollagen III N-propeptides as effectively as those of procollagens I and II, whereas processing of procollagen III is shown to be decreased in Ehlers-Danlos VIIC. Thus, the dogma that procollagen I and procollagen III N-proteinase activities are provided by separate enzymes appears to be false, whereas the phenotypes of dermatosparaxis and Ehlers-Danlos VIIC may arise from defects in both type I and type III collagen biosynthesis. | en |
dc.language.iso | en | en |
dc.publisher | American Society for Biochemistry and Molecular Biology | en |
dc.title | Transforming growth factor-{beta} induces secretion of activated ADAMTS-2: a procollagen III N-proteinase. | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 이승복 | - |
dc.identifier.doi | 10.1074/jbc.M300767200 | - |
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