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http://purl.uniprot.org/citations/30905411http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30905411http://www.w3.org/2000/01/rdf-schema#comment"Lysyl hydroxylase 2 (LH2) is an endoplasmic reticulum (ER)-resident enzyme that catalyzes the hydroxylation of lysine residues in the telopeptides of fibrillar collagens. This is a critical modification to determine the fate of collagen cross-linking pathway that contributes to the stability of collagen fibrils. Studies have demonstrated that the aberrant LH2 function causes various diseases including osteogenesis imperfecta, fibrosis, and cancer metastasis. However, surprisingly, a LH2-deficient animal model has not been reported. In the current study, to better understand the function of LH2, we generated LH2 gene knockout mice by CRISPR/Cas9 technology. LH2 deficiency was confirmed by genotyping polymerase chain reaction (PCR), reverse transcriptase-PCR, and immunohistochemical analyses. Homozygous LH2 knockout (LH2-/-) embryos failed to develop normally and died at early embryonic stage E10.5 with abnormal common ventricle in a heart, i.e., an insufficient wall, a thin ventricular wall, and loosely packed cells. In the LH2-/- mice, the ER stress-responsive genes, ATF4 and CHOP were significantly up-regulated leading to increased levels of Bax and cleaved caspase-3. These data indicate that LH2 plays an essential role in cardiac development through an ER stress-mediated apoptosis pathway."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2019.03.091"xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Miki T."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Saito T."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Oka N."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Hayashi F."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Kita A."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Okubo Y."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Ito C."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Kasamatsu A."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Yamauchi M."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Toshimori K."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Miyamoto I."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Uzawa K."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Shiiba M."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/author"Tanzawa H."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/pages"486-491"xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/title"Deficiency of lysyl hydroxylase 2 in mice causes systemic endoplasmic reticulum stress leading to early embryonic lethality."xsd:string
http://purl.uniprot.org/citations/30905411http://purl.uniprot.org/core/volume"512"xsd:string
http://purl.uniprot.org/citations/30905411http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30905411
http://purl.uniprot.org/citations/30905411http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30905411