Linked Life Data

19182206

Source:http://linkedlifedata.com/resource/pubmed/id/19182206

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2009-5-29
pubmed:abstractText
Cell surface-associated proteolysis plays a crucial role in the migration of mononuclear phagocytes to sites of inflammation. The glycolytic enzyme enolase-1 (ENO-1) binds plasminogen at the cell surface, enhancing local plasmin production. This study addressed the role played by ENO-1 in lipopolysaccharide (LPS)-driven chemokine-directed monocyte migration and matrix invasion in vitro, as well as recruitment of monocytes to the alveolar compartment in vivo. LPS rapidly up-regulated ENO-1 cell-surface expression on human blood monocytes and U937 cells due to protein translocation from cytosolic pools, which increased plasmin generation, enhanced monocyte migration through epithelial monolayers, and promoted matrix degradation. These effects were abrogated by antibodies directed against the plasminogen binding site of ENO-1. Overexpression of ENO-1 in U937 cells increased their migratory and matrix-penetrating capacity, which was suppressed by overexpression of a truncated ENO-1 variant lacking the plasminogen binding site (ENO-1DeltaPLG). In vivo, intratracheal LPS application in mice promoted alveolar recruitment of monocytic cells that overexpressed ENO-1, but not of cells overexpressing ENO-1DeltaPLG. Consistent with these data, pneumonia-patients exhibited increased ENO-1 cell-surface expression on blood monocytes and intense ENO-1 staining of mononuclear cells in the alveolar space. These data suggest an important mechanism of inflammatory cell invasion mediated by increased cell-surface expression of ENO-1.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1528-0020
pubmed:author
pubmed:issnType
Electronic
pubmed:day
28
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5588-98
pubmed:meshHeading
pubmed-meshheading:19182206-Acute Disease, pubmed-meshheading:19182206-Animals, pubmed-meshheading:19182206-Antibodies, pubmed-meshheading:19182206-Antigens, Surface, pubmed-meshheading:19182206-Cell Adhesion, pubmed-meshheading:19182206-Cells, Cultured, pubmed-meshheading:19182206-Chemotaxis, Leukocyte, pubmed-meshheading:19182206-DNA-Binding Proteins, pubmed-meshheading:19182206-Humans, pubmed-meshheading:19182206-Lipopolysaccharides, pubmed-meshheading:19182206-Mice, pubmed-meshheading:19182206-Mice, Inbred BALB C, pubmed-meshheading:19182206-Monocytes, pubmed-meshheading:19182206-Phosphopyruvate Hydratase, pubmed-meshheading:19182206-Plasminogen, pubmed-meshheading:19182206-Pneumonia, pubmed-meshheading:19182206-Protein Processing, Post-Translational, pubmed-meshheading:19182206-Protein Transport, pubmed-meshheading:19182206-Tumor Markers, Biological, pubmed-meshheading:19182206-Tumor Suppressor Proteins, pubmed-meshheading:19182206-U937 Cells
pubmed:year
2009
pubmed:articleTitle
Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung.
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Giessen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't