| http://purl.uniprot.org/citations/20708079 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20708079 | http://www.w3.org/2000/01/rdf-schema#comment | "The sequence encoding the N-propeptide of collagen I is characterized by significant conservation of amino acids across species; however, the function of the N-propeptide remains poorly defined. Studies in vitro have suggested that one activity of this propeptide might be to act as a feedback inhibitor of collagen I synthesis. To determine whether the N-propeptide contributed to decreased collagen content in SPARC-null mice, mice carrying a deletion of exon 2, which encodes the globular domain of the N-propeptide of collagen I, were crossed to SPARC-null animals. Mice lacking SPARC and expressing collagen I without the globular domain of the N-propeptide were viable and fertile. However, a significant number of animals developed abdominal hernias within the first 2 months of life with an approximate 20% penetrance (~35% of males). The dermis of SPARC-null/exon 2-deleted mice was thinner and contained fewer large collagen fibers in comparison with wild-type or in either single transgenic animal. The average collagen fibril diameter of exon 2-deleted mice did not significantly differ from wild-type mice (WT: 87.9 nm versus exon 2-deleted: 88.2 nm), whereas SPARC-null/exon 2-deleted fibrils were smaller than that of SPARC-null dermis (SPARC-null: 60.2 nm, SPARC-null/exon 2-deleted: 40.8 nm). As measured by hydroxyproline analysis, double transgenic skin biopsies contained significantly less collagen than those of wild-type, those of exon 2-deleted, and those of SPARC-null biopsies. Acetic acid extraction of collagen from skin biopsies revealed an increase in the proportion of soluble collagen in the SPARC-null/exon 2-deleted mice. These results support a function of the N-propeptide of collagen I in facilitating incorporation and stabilization of collagen I into the insoluble ECM and argue against a primary function of the N-propeptide as a negative regulator of collagen synthesis."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.matbio.2010.08.002"xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/author | "Zhang Y."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/author | "Henderson N."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/author | "Bornstein P."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/author | "Bradshaw A.D."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/author | "Card L."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/name | "Matrix Biol"xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/pages | "559-564"xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/title | "Expression in SPARC-null mice of collagen type I lacking the globular domain of the alpha1(I) N-propeptide results in abdominal hernias and loss of dermal collagen."xsd:string |
| http://purl.uniprot.org/citations/20708079 | http://purl.uniprot.org/core/volume | "29"xsd:string |
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