| http://purl.uniprot.org/citations/16754682 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16754682 | http://www.w3.org/2000/01/rdf-schema#comment | "The purpose of the current study was to examine the binding of pulmonary surfactant protein A (SP-A) to TLR4 and MD-2, which are critical signaling receptors for lipopolysaccharides (LPSs). The direct binding of SP-A to the recombinant soluble form of extracellular TLR4 domain (sTLR4) and MD-2 was detected using solid-phase binding, immunoprecipitation, and BIAcore. SP-A bound to sTLR4 and MD-2 in a Ca2+-dependent manner, and an anti-SP-A monoclonal antibody whose epitope lies in the region Thr184-Gly194 blocked the SP-A binding to sTLR4 and MD-2, indicating the involvement of the carbohydrate recognition domain (CRD) in the binding. SP-A avidly bound to the deglycosylated forms of sTLR4 and MD-2, suggesting a protein/protein interaction. In addition, SP-A attenuated cell surface binding of smooth LPS and smooth LPS-induced NF-kappaB activation in TLR4/MD-2-expressing cells. To know the role of oligomerization in the interaction of SP-A with TLR4 and MD-2, the collagenase-resistant fragment (CRF), which consisted of CRD plus neck domain of SP-A, was isolated. CRF assembled as a trimer, whereas SP-A assembled as a higher order oligomer. Although CRD was suggested to be involved in the binding, CRF exhibited approximately 600- and 155-fold higher KD for the binding to TLR4 and MD-2, respectively, when compared with SP-A. Consistently significantly higher molar concentrations of CRF were required to inhibit smooth LPS-induced NF-kappaB activation and tumor necrosis factor-alpha secretion. These results demonstrate for the first time the direct interaction between SP-A and TLR4/MD-2 and suggest the importance of supratrimeric oligomerization in the immunomodulatory function of SP-A."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m513041200"xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Kuroki Y."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Shimizu T."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Yamada C."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Sano H."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Mitsuzawa H."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Nishitani C."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/author | "Himi T."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/pages | "21771-21780"xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/title | "Surfactant protein A directly interacts with TLR4 and MD-2 and regulates inflammatory cellular response. Importance of supratrimeric oligomerization."xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16754682 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16754682 |
| http://purl.uniprot.org/citations/16754682 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16754682 |
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| http://purl.uniprot.org/uniprot/#_O00206-mappedCitation-16754682 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16754682 |