| http://purl.uniprot.org/citations/34224569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34224569 | http://www.w3.org/2000/01/rdf-schema#comment | "Among the enzymes of the biosynthesis of sialoglycoconjugates, uridine diphosphate-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE), catalyzing the first essential step of the sialic acid (Sia) de novo biosynthesis, and cytidine monophosphate (CMP)-Sia synthase (CMAS), activating Sia to CMP-Sia, are particularly important. The knockout of either of these enzymes in mice is embryonically lethal. While the lethality of Cmas-/-mice has been attributed to a maternal complement attack against asialo fetal placental cells, the cause of lethality in Gne-deficient embryos has remained elusive. Here, we advanced the significance of sialylation for embryonic development through detailed histological analyses of Gne-/-embryos and placentae. We found that Gne-/-embryonic and extraembryonic tissues are hyposialylated rather than being completely deficient of sialoglycans, which holds true for Cmas-/-embryos. Residual sialylation of Gne-/-cells can be explained by scavenging free Sia from sialylated maternal serum glycoconjugates via the lysosomal salvage pathway. The placental architecture of Gne-/-mice was unaffected, but severe hemorrhages in the neuroepithelium with extensive bleeding into the cephalic ventricles were present at E12.5 in the mutants. At E13.5, the vast majority of Gne-/-embryos were asystolic. This phenotype persisted when Gne-/-mice were backcrossed to a complement component 3-deficient background, confirming distinct pathomechanisms of Cmas-/- and Gne-/-mice. We conclude that the low level of sialylation observed in Gne-/-mice is sufficient both for immune homeostasis at the fetal-maternal interface and for embryonic development until E12.5. However, formation of the neural microvasculature is the first critical process, depending on a higher degree of sialylation during development of the embryo proper."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.org/dc/terms/identifier | "doi:10.1093/glycob/cwab069"xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Neumann H."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Kispert A."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Horstkorte R."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Wedekind H."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Kats E."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Weinhold B."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Weiss A.C."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Klaus C."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Thiesler H."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Abeln M."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/author | "Munster-Kuhnel A."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/name | "Glycobiology"xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/pages | "1478-1489"xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/title | "Uridine diphosphate-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase deletion in mice leads to lethal intracerebral hemorrhage during embryonic development."xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/34224569 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/34224569 |
| http://purl.uniprot.org/citations/34224569 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/34224569 |
| http://purl.uniprot.org/uniprot/#_Q3TCI8-mappedCitation-34224569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/34224569 |
| http://purl.uniprot.org/uniprot/#_Q3UW64-mappedCitation-34224569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/34224569 |
| http://purl.uniprot.org/uniprot/#_Q91WG8-mappedCitation-34224569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/34224569 |
| http://purl.uniprot.org/uniprot/Q3UW64 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/34224569 |