| http://purl.uniprot.org/citations/15136578 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15136578 | http://www.w3.org/2000/01/rdf-schema#comment | "Type V collagen is a quantitatively minor fibrillar collagen comprised of different chain compositions in different tissues. The most widely distributed form, an alpha1(V)2alpha2(V) heterotrimer, regulates the physical properties of type I/V heterotypic collagen fibrils via partially processed NH2-terminal globular sequences. A less characterized alpha1(V)alpha2(V)alpha3(V) heterotrimer has a much more limited distribution of expression and unknown function(s). We characterized the biosynthetic processing of pro-alpha1(V)2pro-alpha2(V) procollagen previously and showed it to differ in important ways from biosynthetic processing of the major fibrillar procollagens I-III. Here we have successfully produced recombinant pro-alpha1(V)pro-alpha2(V)pro-alpha3(V) heterotrimers. We use these, and mouse embryo fibroblasts doubly homozygous null for the Bmp1 gene, which encodes the metalloproteinase bone morphogenetic protein-1 (BMP-1), and for a gene encoding the closely related metalloproteinase mammalian Tolloid-like 1, to characterize biosynthetic processing of pro-alpha1(V)pro-alpha2(V)pro-alpha3(V) heterotrimers, thus completing characterization of type V collagen biosynthetic processing. Whereas pro-alpha1(V) and pro-alpha2(V) processing in pro-alpha1(V)pro-alpha2(V)pro-alpha3(V) heterotrimers is similar to that which occurs in pro-alpha1(V)2pro-alpha2(V) heterotrimers, the processing of pro-alpha3(V) by BMP-1 occurs at an unexpected site within NH2-terminal globular sequences. We also demonstrate that, despite similarities in NH2-terminal domain structures, pro-alpha2(V) NH2-terminal globular sequences are not cleaved by ADAMTS-2, the metalloproteinase that cleaves the N-propeptides of the major fibrillar procollagen chains."xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m402252200"xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/author | "Greenspan D.S."xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/author | "Wang W.M."xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/author | "Gopalakrishnan B."xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/pages | "30904-30912"xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/title | "Biosynthetic processing of the Pro-alpha1(V)Pro-alpha2(V)Pro-alpha3(V) procollagen heterotrimer."xsd:string |
| http://purl.uniprot.org/citations/15136578 | http://purl.uniprot.org/core/volume | "279"xsd:string |
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