| http://purl.uniprot.org/citations/11706042 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11706042 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11706042 | http://www.w3.org/2000/01/rdf-schema#comment | "The lipopolysaccharide (LPS) receptor is a multi-protein complex that consists of at least three proteins, CD14, TLR4, and MD-2. Because each of these proteins is glycosylated, we have examined the functional role of N-linked carbohydrates of both MD-2 and TLR4. We demonstrate that MD-2 contains 2 N-glycosylated sites at positions Asn(26) and Asn(114), whereas the amino-terminal ectodomain of human TLR4 contains 9 N-linked glycosylation sites. Site-directed mutagenesis studies showed that cell surface expression of MD-2 did not depend on the presence of either N-linked site, whereas in contrast, TLR4 mutants carrying substitutions in Asn(526) or Asn(575) failed to be transported to the cell surface. Using a UV-activated derivative of Re595 LPS (ASD-Re595 LPS) in cross-linking assays, we demonstrated a critical role of MD-2 and TLR4 carbohydrates in LPS cross-linking to the LPS receptor. The ability of the various glycosylation mutants to support cell activation was also evaluated in transiently transfected HeLa cells. The double mutant of MD-2 failed to support LPS-induced activation of an interleukin-8 (IL-8) promoter-driven luciferase reporter to induce IL-8 secretion or to activate amino-terminal c-Jun kinase (JNK). Similar results were observed with TLR4 mutants lacking three or more N-linked glycosylation sites. Surprisingly, the reduction in activation resulting from expression of the Asn mutants of MD-2 and TLR4 can be partially reversed by co-expression with CD14. This suggests that the functional integrity of the LPS receptor depends both on the surface expression of at least three proteins, CD14, MD-2, and TLR4, and that N-linked sites of both MD-2 and TLR4 are essential in maintaining the functional integrity of this receptor."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109910200"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109910200"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/author | "da Silva Correia J."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/author | "da Silva Correia J."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/author | "Ulevitch R.J."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/author | "Ulevitch R.J."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/pages | "1845-1854"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/pages | "1845-1854"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/title | "MD-2 and TLR4 N-linked glycosylations are important for a functional lipopolysaccharide receptor."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/title | "MD-2 and TLR4 N-linked glycosylations are important for a functional lipopolysaccharide receptor."xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11706042 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11706042 |
| http://purl.uniprot.org/citations/11706042 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11706042 |
| http://purl.uniprot.org/citations/11706042 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11706042 |
| http://purl.uniprot.org/citations/11706042 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11706042 |
| http://purl.uniprot.org/uniprot/O00206 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11706042 |
| http://purl.uniprot.org/uniprot/O00206#attribution-0C7EFC4B4DCD5E7FCA7758F48543233C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/11706042 |