Linked Life Data

8572171

Source:http://linkedlifedata.com/resource/pubmed/id/8572171

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8572171rdf:typepubmed:Citationlld:pubmed
pubmed-article:8572171lifeskim:mentionsumls-concept:C0042172lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0022646lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0027713lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0001473lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0051926lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0443199lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0060611lld:lifeskim
pubmed-article:8572171lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:8572171pubmed:issue6 Pt 1lld:pubmed
pubmed-article:8572171pubmed:dateCreated1996-3-7lld:pubmed
pubmed-article:8572171pubmed:abstractTextIonic homeostasis in vertebrates is maintained by epithelial cells that line kidney nephrons. Transport of ions and solutes is coupled to Na+ reabsorption from the ultrafiltrate and requires specific subcellular distribution and activity of Na(+)-K(+)-ATPase along the nephron. Studies using cell culture models of renal epithelia indicate that the subcellular distribution of Na(+)-K(+)-ATPase is regulated by interactions with the submembrane cytoskeleton and E-cadherin-mediated adherens junctions. We have now examined the relevance of these in vitro observations to the subcellular organization of these proteins in different nephron segments of the adult mouse kidney using immunofluorescence microscopy. Our results demonstrate that segmental and subcellular distributions of Na(+)-K(+)-ATPase and the membrane-cytoskeletal proteins, ankyrin and fodrin, vary in parallel along the nephron and do not parallel variations in expression of the tight junction protein ZO-1 or E-cadherin. These data indicate that a mechanism for restricting Na(+)-K(+)-ATPase subcellular distributions through interactions with the membrane cytoskeleton is likely to be relevant in vivo.lld:pubmed
pubmed-article:8572171pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:languageenglld:pubmed
pubmed-article:8572171pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:citationSubsetIMlld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8572171pubmed:statusMEDLINElld:pubmed
pubmed-article:8572171pubmed:monthDeclld:pubmed
pubmed-article:8572171pubmed:issn0002-9513lld:pubmed
pubmed-article:8572171pubmed:authorpubmed-author:LuxS ESElld:pubmed
pubmed-article:8572171pubmed:authorpubmed-author:NelsonW JWJlld:pubmed
pubmed-article:8572171pubmed:authorpubmed-author:PetersL LLLlld:pubmed
pubmed-article:8572171pubmed:authorpubmed-author:PiepenhagenP...lld:pubmed
pubmed-article:8572171pubmed:issnTypePrintlld:pubmed
pubmed-article:8572171pubmed:volume269lld:pubmed
pubmed-article:8572171pubmed:ownerNLMlld:pubmed
pubmed-article:8572171pubmed:authorsCompleteYlld:pubmed
pubmed-article:8572171pubmed:paginationC1417-32lld:pubmed
pubmed-article:8572171pubmed:dateRevised2007-11-15lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:meshHeadingpubmed-meshheading:8572171-...lld:pubmed
pubmed-article:8572171pubmed:year1995lld:pubmed
pubmed-article:8572171pubmed:articleTitleDifferential expression of Na(+)-K(+)-ATPase, ankyrin, fodrin, and E-cadherin along the kidney nephron.lld:pubmed
pubmed-article:8572171pubmed:affiliationDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5426, USA.lld:pubmed
pubmed-article:8572171pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8572171pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8572171lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8572171lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8572171lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8572171lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8572171lld:pubmed