Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:2744270rdf:typepubmed:Citationlld:pubmed
pubmed-article:2744270lifeskim:mentionsumls-concept:C0017968lld:lifeskim
pubmed-article:2744270lifeskim:mentionsumls-concept:C0018270lld:lifeskim
pubmed-article:2744270lifeskim:mentionsumls-concept:C0597538lld:lifeskim
pubmed-article:2744270lifeskim:mentionsumls-concept:C0443199lld:lifeskim
pubmed-article:2744270lifeskim:mentionsumls-concept:C0851285lld:lifeskim
pubmed-article:2744270lifeskim:mentionsumls-concept:C0086149lld:lifeskim
pubmed-article:2744270pubmed:issue1lld:pubmed
pubmed-article:2744270pubmed:dateCreated1989-8-17lld:pubmed
pubmed-article:2744270pubmed:abstractTextDuring early starvation-induced development, amoebae of Dictyostelium discoideum have been previously shown to increase sulfation and fucosylation of glycoprotein-linked oligosaccharides to levels above those observed in axenically growing cells. We report here that the axenic broth culture itself induces generation of high levels of fucosylated glycoprotein-linked oligosaccharides at all stages in the growth curve. However, when grown on bacteria, amoebae of both the axenic strain and the wild type show dramatic depression in fucose incorporation during early exponential growth. In mid- and late-exponential stages of growth, fucosylation rises to the levels found at all stages of axenic culture. Sulfation also increases during early development, but, in contrast to fucosylation, oligosaccharide sulfation is not altered by growth in axenic medium and does not increase during growth on bacteria. Starvation of bacterially grown cells results in increased sulfation and a further rise in fucosylation, as is also characteristic of broth-grown cells. The ability of axenic culture to uncouple control of these two classes of glycan-modification steps suggests that the synchronous increases during early development actually reflect responses to different regulatory signals, even though they participate in the same metabolic process. The increase in in vivo fucosyltransferase activity, which can act on many substrate glycoproteins, may alter many characteristics of the cells.lld:pubmed
pubmed-article:2744270pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:languageenglld:pubmed
pubmed-article:2744270pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:citationSubsetIMlld:pubmed
pubmed-article:2744270pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:2744270pubmed:statusMEDLINElld:pubmed
pubmed-article:2744270pubmed:monthMarlld:pubmed
pubmed-article:2744270pubmed:issn0301-4681lld:pubmed
pubmed-article:2744270pubmed:authorpubmed-author:RileyG RGRlld:pubmed
pubmed-article:2744270pubmed:authorpubmed-author:HendersonE...lld:pubmed
pubmed-article:2744270pubmed:authorpubmed-author:TschursinEElld:pubmed
pubmed-article:2744270pubmed:issnTypePrintlld:pubmed
pubmed-article:2744270pubmed:volume40lld:pubmed
pubmed-article:2744270pubmed:ownerNLMlld:pubmed
pubmed-article:2744270pubmed:authorsCompleteYlld:pubmed
pubmed-article:2744270pubmed:pagination1-9lld:pubmed
pubmed-article:2744270pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:2744270pubmed:meshHeadingpubmed-meshheading:2744270-...lld:pubmed
pubmed-article:2744270pubmed:meshHeadingpubmed-meshheading:2744270-...lld:pubmed
pubmed-article:2744270pubmed:meshHeadingpubmed-meshheading:2744270-...lld:pubmed
pubmed-article:2744270pubmed:meshHeadingpubmed-meshheading:2744270-...lld:pubmed
pubmed-article:2744270pubmed:meshHeadingpubmed-meshheading:2744270-...lld:pubmed
pubmed-article:2744270pubmed:year1989lld:pubmed
pubmed-article:2744270pubmed:articleTitleDifferential regulation of glycoprotein sulfation and fucosylation during growth of Dictyostelium discoideum.lld:pubmed
pubmed-article:2744270pubmed:affiliationDepartment of Biology, Gerogetown University, Washington, D.C. 20057.lld:pubmed
pubmed-article:2744270pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2744270pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:2744270pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed