| http://purl.uniprot.org/citations/17135260 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17135260 | http://www.w3.org/2000/01/rdf-schema#comment | "Collagen prolyl 4-hydroxylases (C-P4Hs) catalyze the formation of the 4-hydroxyproline residues that are essential for the generation of triple helical collagen molecules. The vertebrate C-P4Hs I, II, and III are [alpha(I)]2beta2, [alpha(II)]2beta2, and [alpha(III)]2beta2 tetramers with identical beta subunits. We generated mice with targeted inactivation of the P4ha1 gene encoding the catalytic alpha subunit of C-P4H I to analyze its specific functions. The null mice died after E10.5, showing an overall developmental delay and a dilated endoplasmic reticulum in their cells. The capillary walls were frequently ruptured, but the capillary density remained unchanged. The C-P4H activity level in the null embryos and fibroblasts cultured from them was 20% of that in the wild type, being evidently due to the other two isoenzymes. Collagen IV immunofluorescence was almost absent in the basement membranes of the null embryos, and electron microscopy revealed disrupted basement membranes, while immunoelectron microscopy showed a lack of collagen IV in them. The amount of soluble collagen IV was increased in the null embryos and cultured null fibroblasts, indicating a lack of assembly of collagen IV molecules into insoluble structures, probably due to their underhydroxylation and hence abnormal conformation. In contrast, the null embryos had collagen I and III fibrils with a typical cross-striation pattern but slightly increased diameters, and the null fibroblasts secreted fibril-forming collagens, although less efficiently than wild-type cells. The primary cause of death of the null embryos was thus most likely an abnormal assembly of collagen IV."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606608200"xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Myllyharju J."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Pakkanen O."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Kivirikko K.I."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Soininen R."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Sormunen R."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Nokelainen M."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/author | "Holster T."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/pages | "2512-2519"xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/title | "Loss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null mice."xsd:string |
| http://purl.uniprot.org/citations/17135260 | http://purl.uniprot.org/core/volume | "282"xsd:string |
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