Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:7691747rdf:typepubmed:Citationlld:pubmed
pubmed-article:7691747lifeskim:mentionsumls-concept:C0029235lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0024109lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0032276lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0010453lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C1314972lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0014597lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0055023lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0237497lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C1145667lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0086597lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C0185023lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C1947904lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C1999228lld:lifeskim
pubmed-article:7691747lifeskim:mentionsumls-concept:C2825781lld:lifeskim
pubmed-article:7691747pubmed:issue10lld:pubmed
pubmed-article:7691747pubmed:dateCreated1993-11-16lld:pubmed
pubmed-article:7691747pubmed:abstractTextPneumocystis carinii attaches to alveolar epithelial cells during the development of pneumonia. Adhesive proteins found within the alveolar space have been proposed to mediate P. carinii adherence to lung cells. Vitronectin (Vn), a 75-kDa glycoprotein present in the lower respiratory tract, has substantial cell-adhesive properties and might participate in the host-parasite interaction during P. carinii pneumonia. To address whether Vn binds to P. carinii, we studied the interaction of radiolabeled Vn with purified P. carinii organisms. Vn bound to P. carinii, occupying an estimated 5.47 x 10(5) binding sites per organism, with an affinity constant, Kd, of 4.24 x 10(-7) M. Interestingly, the interaction of Vn with P. carinii was not mediated through the Arg-Gly-Asp cell-adhesive domain of Vn. Addition of Arg-Gly-Asp-Ser (RGDS) peptides did not inhibit binding. In contrast, Vn binding to P. carinii was substantially inhibited by the addition of heparin or by digesting the organisms with heparitinase, suggesting that P. carinii may interact with the glycosaminoglycan-binding domain of Vn. To determine whether Vn might enhance P. carinii attachment to lung epithelial cells, we studied the binding of 51Cr-labeled P. carinii to cultured A549 lung cells. Addition of Vn resulted in significantly increased binding of P. carinii to A549 cells, whereas a neutralizing anti-Vn serum substantially reduced the binding of P. carinii to A549 cells. These data suggest that Vn binds to P. carinii and that Vn might provide an additional means by which P. carinii attaches to respiratory epithelial cells.lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:languageenglld:pubmed
pubmed-article:7691747pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:citationSubsetIMlld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7691747pubmed:statusMEDLINElld:pubmed
pubmed-article:7691747pubmed:monthOctlld:pubmed
pubmed-article:7691747pubmed:issn0019-9567lld:pubmed
pubmed-article:7691747pubmed:authorpubmed-author:CastroMMlld:pubmed
pubmed-article:7691747pubmed:authorpubmed-author:LimperA HAHlld:pubmed
pubmed-article:7691747pubmed:authorpubmed-author:StandingJ EJElld:pubmed
pubmed-article:7691747pubmed:authorpubmed-author:NeeseL WLWlld:pubmed
pubmed-article:7691747pubmed:authorpubmed-author:HoffmanO AOAlld:pubmed
pubmed-article:7691747pubmed:issnTypePrintlld:pubmed
pubmed-article:7691747pubmed:volume61lld:pubmed
pubmed-article:7691747pubmed:ownerNLMlld:pubmed
pubmed-article:7691747pubmed:authorsCompleteYlld:pubmed
pubmed-article:7691747pubmed:pagination4302-9lld:pubmed
pubmed-article:7691747pubmed:dateRevised2009-11-18lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:meshHeadingpubmed-meshheading:7691747-...lld:pubmed
pubmed-article:7691747pubmed:year1993lld:pubmed
pubmed-article:7691747pubmed:articleTitleVitronectin binds to Pneumocystis carinii and mediates organism attachment to cultured lung epithelial cells.lld:pubmed
pubmed-article:7691747pubmed:affiliationDepartment of Internal Medicine, Mayo Clinic and Foundation, Rochester, Minnesota 55905.lld:pubmed
pubmed-article:7691747pubmed:publicationTypeJournal Articlelld:pubmed
More...