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http://purl.uniprot.org/citations/9065415http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9065415http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9065415http://www.w3.org/2000/01/rdf-schema#comment"Recombinant human procollagenase-3 and a C-terminal truncated form (Delta249-451 procollagenase-3) have been stably expressed in myeloma cells and purified. The truncated proenzyme could be processed by aminophenylmercuric acetate via a short-lived intermediate form (N-terminal Leu58) to the final active form (N-terminal Tyr85). The kinetics of activation were not affected by removal of the hemopexin-like C-terminal domain. The specific activities of both collagenase-3 and Delta249-451 collagenase-3 were found to be similar using two quenched fluorescent substrates, but Delta249-451 collagenase-3 failed to cleave native triple helical collagens (types I and II) into characteristic one- and three-quarter fragments. It was noted, however, that the beta1,2(I) chains of type I collagen were susceptible to Delta249-451 collagenase-3, which indicates that the catalytic domain displays telopeptidase activity, thereby generating alpha1,2(I) chains that are slightly shorter than those in native type I collagen. It can be concluded that the C-terminal domain is only essential for the triple helicase activity of collagenase-3. Binding of procollagenase-3 and active collagenase-3 to type I collagen is mediated by the C-terminal domain. Both collagenase-3 and Delta249-451 collagenase-3 hydrolyzed the large tenascin C isoform, fibronectin, recombinant fibronectin fragments, and type IV, IX, X, and XIV collagens; thus, these events were independent from C-terminal domain interactions. In contrast, the minor cartilage type XI collagen was resistant to cleavage. Kinetic analysis of the mechanism of inhibition of wild-type and Delta249-451 collagenase-3 by wild-type and mutant tissue inhibitors of metalloproteinase (TIMPs) revealed that the association rates for complex formation were influenced by both N- and C-terminal domain interactions. The C-terminal domain of wild-type collagenase-3 promoted increased association rates with the full-length inhibitors TIMP-1 and TIMP-3 and the hybrid N.TIMP-2/C.TIMP-1 by a factor of up to 33. In contrast, the association rates for complex formation with TIMP-2 and N.TIMP-1/C.TIMP-2 were only marginally affected by C-terminal domain interactions."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.12.7608"xsd:string
http://purl.uniprot.org/citations/9065415http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.12.7608"xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Lopez-Otin C."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Lopez-Otin C."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Murphy G."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Murphy G."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Smith B."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Smith B."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Morris H."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Morris H."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"O'Shea M."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"O'Shea M."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Zardi L."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Zardi L."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Cowell S."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Cowell S."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Knaeuper V."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/author"Knaeuper V."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9065415http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
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