Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10358066rdf:typepubmed:Citationlld:pubmed
pubmed-article:10358066lifeskim:mentionsumls-concept:C0009015lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0003316lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0016956lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0220781lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C1412716lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0679622lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C1314939lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0205314lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:10358066lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:10358066pubmed:issue24lld:pubmed
pubmed-article:10358066pubmed:dateCreated1999-7-6lld:pubmed
pubmed-article:10358066pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:abstractTextWe isolated a cDNA encoding a novel glucuronyltransferase, designated GlcAT-D, involved in the biosynthesis of the HNK-1 carbohydrate epitope from rat embryo cDNA by the degenerate polymerase chain reaction method. The new cDNA sequence revealed an open reading frame coding for a protein of 324 amino acids with type II transmembrane protein topology. The amino acid sequence of GlcAT-D displayed 50.0% identity to rat GlcAT-P, which is involved in the biosynthesis of the HNK-1 epitope on glycoproteins. Expression of GlcAT-D in COS-7 cells resulted in the formation of the HNK-1 epitope on the cell surface. The enzyme expressed in COS-7 cells transferred a glucuronic acid (GlcA) not only to asialo-orosomucoid, a glycoprotein bearing terminal N-acetyllactosamine structure, but also to paragloboside (lacto-N-neotetraosylceramide), a precursor of the HNK-1 epitope on glycolipids. Furthermore, substrate specificity analysis using a soluble chimeric form of GlcAT-D revealed that GlcAT-D transfers a GlcA not only to Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine++ + but also to Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine++ +. Enzymatic hydrolysis and Smith degradation of the reaction product indicated that GlcAT-D transfers a GlcA through a beta1,3-linkage to a terminal galactose. The GlcAT-D transcripts were detected in embryonic, postnatal, and adult rat brain. In situ hybridization analysis revealed that the expression pattern of GlcAT-D transcript in embryo is similar to that of GlcAT-P, but distinct expression of GlcAT-D was observed in the embryonic pallidum and retina. Regions that expressed GlcAT-D and/or GlcAT-P were always HNK-1-positive, indicating that both GlcATs are involved in the synthesis of the HNK-1 epitope in vivo.lld:pubmed
pubmed-article:10358066pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:languageenglld:pubmed
pubmed-article:10358066pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:citationSubsetIMlld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358066pubmed:statusMEDLINElld:pubmed
pubmed-article:10358066pubmed:monthJunlld:pubmed
pubmed-article:10358066pubmed:issn0021-9258lld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:ShimodaYYlld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:SanaiYYlld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:HarioMMlld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:TajimaYYlld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:NagaseTTlld:pubmed
pubmed-article:10358066pubmed:authorpubmed-author:OsumiNNlld:pubmed
pubmed-article:10358066pubmed:issnTypePrintlld:pubmed
pubmed-article:10358066pubmed:day11lld:pubmed
pubmed-article:10358066pubmed:volume274lld:pubmed
pubmed-article:10358066pubmed:ownerNLMlld:pubmed
pubmed-article:10358066pubmed:authorsCompleteYlld:pubmed
pubmed-article:10358066pubmed:pagination17115-22lld:pubmed
pubmed-article:10358066pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:meshHeadingpubmed-meshheading:10358066...lld:pubmed
pubmed-article:10358066pubmed:year1999lld:pubmed
pubmed-article:10358066pubmed:articleTitleCloning and expression of a novel galactoside beta1, 3-glucuronyltransferase involved in the biosynthesis of HNK-1 epitope.lld:pubmed
pubmed-article:10358066pubmed:affiliationDepartment of Biochemical Cell Research, Tokyo Metropolitan Institute of Medical Science (RINSHOKEN), Tokyo 113-8613, Japan.lld:pubmed
pubmed-article:10358066pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10358066pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:10358066pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:64544entrezgene:pubmedpubmed-article:10358066lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10358066lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10358066lld:pubmed