| http://purl.uniprot.org/citations/7629088 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7629088 | http://www.w3.org/2000/01/rdf-schema#comment | "The C-propeptides of the pro alpha 1(I) and pro alpha 2(I) chains of type I collagen are each substituted with a single high-mannose N-linked oligosaccharide. Conservation of this motif among the fibrillar collagens has led to the proposal that the oligosaccharide has structural or functional importance, but a role in collagen biosynthesis has not been unambiguously defined. To examine directly the function of the pro alpha 1(I) C-propeptide N-linked oligosaccharide, the acceptor Asn residue was changed to Gln by site-directed mutagenesis. In transfected mouse Mov13 and 3T6 cells, unglycosylated mutant pro alpha 1(I) folded and assembled normally into trimeric molecules with pro alpha 2(I). In biosynthetic pulse-chase experiments mutant pro alpha 1(I) were secreted at the same rate as wild-type chains; however, following secretion, the chains were partitioned differently between the cell layer and medium, with a greater proportion of the mutant pro alpha 1(I) being released into the medium. This distribution difference was not eliminated by the inclusion of yeast mannan indicating that the high-mannose oligosaccharide itself was not binding to the matrix or the fibroblast surface after secretion. Subtle alterations in the tertiary structure of unglycosylated C-propeptides may have decreased their affinity for a cell-surface component. Further support for a small conformational change in the mutant C-propeptides came from experiments suggesting that unglycosylated pro alpha 1(I) chains were cleaved in vitro by the purified C-proteinase slightly less efficiently than wild-type chains. Mutant and normal pro alpha 1(I) were deposited with equal efficiency into the 3T6 cell accumulated matrix, thus the reduced cleavage by C-proteinase and altered distribution in the short pulse-chase experiments were not functionally significant in this in vitro extracellular matrix model system."xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.30.17858"xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/author | "Bateman J.F."xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/author | "Lamande S.R."xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/pages | "17858-17865"xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/title | "The type I collagen pro alpha 1(I) COOH-terminal propeptide N-linked oligosaccharide. Functional analysis by site-directed mutagenesis."xsd:string |
| http://purl.uniprot.org/citations/7629088 | http://purl.uniprot.org/core/volume | "270"xsd:string |
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