| http://purl.uniprot.org/citations/34875533 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34875533 | http://www.w3.org/2000/01/rdf-schema#comment | "Lysyl hydroxylase 2 (LH2) regulates intermolecular cross-linking of collagen molecules. Accumulation of LH2-modified collagen, which is highly stable and resistant to collagenase cleavage, is one cause of fibrosis. We previously demonstrated that conventional LH2 knockout mice showed embryonic lethality. Here we established LH2 conditional knockout mice using a tamoxifen-inducible Cre system. Morphological analysis of LH2-deficient fibroblasts by microscopy showed a dramatic increase in the number of filopodia, the finger-like cell surface projections that enable cell movement. The tips and leading edges of these filopodia exhibited up-regulated expression of Myosin-X (Myo10), a regulator of filopodial integrity. Wound healing assays demonstrated that migration of LH2-deficient cells was significantly faster than that of control cells. Gene expression profiling data also supported this phenotype. Together these findings indicate that LH2 deficiency may prevent fibrosis through decreased accumulation of LH2-cross-linked collagen, and that fibroblasts with faster migration contribute to enhanced wound healing activity. In conclusion, our cellular models provide evidence that LH2 deficiency plays a critical role in cell migration mediated through filopodia formation. Understanding the precise role of this phenotype in LH2-deficient cells may be helpful to define the pathogenesis of fibrosis. As such, detailed analyses of fibrosis and wound healing using LH2-deficient mouse models are needed."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2021.11.100"xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/author | "Moss J."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/author | "Kasamatsu A."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/author | "Uzawa K."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/author | "Nozaki R."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/date | "2022"xsd:gYear |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/pages | "146-152"xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/title | "Lysyl hydroxylase 2 deficiency promotes filopodia formation and fibroblast migration."xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://purl.uniprot.org/core/volume | "587"xsd:string |
| http://purl.uniprot.org/citations/34875533 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/34875533 |
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