Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9862714rdf:typepubmed:Citationlld:pubmed
pubmed-article:9862714lifeskim:mentionsumls-concept:C0026473lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0205093lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0008018lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0078056lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0209606lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C1704675lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0600210lld:lifeskim
pubmed-article:9862714lifeskim:mentionsumls-concept:C0183683lld:lifeskim
pubmed-article:9862714pubmed:issue12lld:pubmed
pubmed-article:9862714pubmed:dateCreated1999-1-22lld:pubmed
pubmed-article:9862714pubmed:abstractTextThe transient regulation of very late antigen (VLA)-4 avidity by CC chemokines may promote chemotaxis of monocytes across VCAM-1-bearing barriers, whereas late and prolonged activation of VLA-5 may mediate subsequent localization in the extracellular matrix. We demonstrate that interactions of VLA-4 with VCAM-1, fibronectin, or a 40-kDa fragment but not a 120-kDa fragment of fibronectin supported the lateral random migration of isolated blood monocytes induced by CC chemokines, termed chemokinesis. This effect was optimal at intermediate substrate concentrations. Moreover, coimmobilization of VCAM-1 with ICAM-1 allowed better migration than ICAM-1 alone. Chemokinesis on VCAM-1 appeared to be associated with transient regulation of VLA-4 avidity by CC chemokines, given that locking VLA-4 in a high avidity state markedly inhibited migration and the locomotion rate was inversely correlated with the adhesive strength of VLA-4 to VCAM-1 following stimulation with monocyte chemoattractant protein-1. Induction of VCAM-1 expression by endothelial activation with IL-4 improved chemokinesis and lateral migration toward a monocyte chemoattractant protein-1 or a monocyte inflammatory protein-1alpha gradient on endothelium and increased transendothelial chemotaxis of monocytes by a VLA-4-dependent mechanism. In contrast, endothelial activation with IL-4 did not affect the time required for diapedesis of monocytes itself. Hence, VCAM-1 may facilitate transendothelial chemotaxis by supporting lateral migration of attached monocytes along endothelium.lld:pubmed
pubmed-article:9862714pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:languageenglld:pubmed
pubmed-article:9862714pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:citationSubsetAIMlld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9862714pubmed:statusMEDLINElld:pubmed
pubmed-article:9862714pubmed:monthDeclld:pubmed
pubmed-article:9862714pubmed:issn0022-1767lld:pubmed
pubmed-article:9862714pubmed:authorpubmed-author:SpringerT ATAlld:pubmed
pubmed-article:9862714pubmed:authorpubmed-author:WeberCClld:pubmed
pubmed-article:9862714pubmed:issnTypePrintlld:pubmed
pubmed-article:9862714pubmed:day15lld:pubmed
pubmed-article:9862714pubmed:volume161lld:pubmed
pubmed-article:9862714pubmed:ownerNLMlld:pubmed
pubmed-article:9862714pubmed:authorsCompleteYlld:pubmed
pubmed-article:9862714pubmed:pagination6825-34lld:pubmed
pubmed-article:9862714pubmed:dateRevised2007-11-15lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:meshHeadingpubmed-meshheading:9862714-...lld:pubmed
pubmed-article:9862714pubmed:year1998lld:pubmed
pubmed-article:9862714pubmed:articleTitleInteraction of very late antigen-4 with VCAM-1 supports transendothelial chemotaxis of monocytes by facilitating lateral migration.lld:pubmed
pubmed-article:9862714pubmed:affiliationCenter For Blood Research and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.lld:pubmed
pubmed-article:9862714pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9862714pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:9862714pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:9862714pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9862714lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9862714lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9862714lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9862714lld:pubmed