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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1985-3-13
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pubmed:abstractText |
We have measured the effect of activated neutrophils on endothelial monolayer integrity in vitro by assessing the capacity of endothelial monolayers on polycarbonate filters to exclude 125I-albumin. Although formylmethionyl-leucyl-phenylalanine (FMLP)-activated neutrophils failed to induce 51Cr-release or detachment after 4 hours of incubation with endothelial monolayers cultured in polystyrene wells, FMLP-activated neutrophils produced a marked increase in the passage of 125I-albumin across bovine aortic or pulmonary artery endothelial monolayers on polycarbonate filters. This effect was evident as early as 30 minutes following the addition of FMLP-activated neutrophils to the monolayer and reached 180% over control values at 2 hours (p = 0.001). Light and transmission electron microscopic examination of the polycarbonate filters exposed to FMLP-activated neutrophils revealed focal disruption of the endothelial monolayers. Chronic granulomatous disease neutrophils produced similar disruption of the endothelial monolayer at 2 hours. Moreover, catalase and superoxide dismutase failed to reduce significantly the neutrophil-mediated increase in 125I-albumin passage at 2 hours. Cell-free postsecretory supernatants of FMLP-activated neutrophils, leukotriene C4, and platelet activating factor did not induce a significant increase in 125I-albumin passage across the endothelial monolayers. Of note, FMLP-activated neutrophils from a patient with a congenital abnormality of neutrophil adhesion and chemotaxis did not induce disruption of the monolayer or increase 125I-albumin passage. We conclude that activated neutrophils mediate rapid, nonlytic disruption of endothelial monolayer integrity by an oxygen radical-independent mechanism that requires neutrophil-endothelial contact.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Albumins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromium Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0023-6837
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3968867-Albumins,
pubmed-meshheading:3968867-Animals,
pubmed-meshheading:3968867-Aorta,
pubmed-meshheading:3968867-Cattle,
pubmed-meshheading:3968867-Cell Adhesion,
pubmed-meshheading:3968867-Chromium Radioisotopes,
pubmed-meshheading:3968867-Endothelium,
pubmed-meshheading:3968867-Filtration,
pubmed-meshheading:3968867-Free Radicals,
pubmed-meshheading:3968867-Horseradish Peroxidase,
pubmed-meshheading:3968867-Humans,
pubmed-meshheading:3968867-L-Lactate Dehydrogenase,
pubmed-meshheading:3968867-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:3968867-Neutrophils,
pubmed-meshheading:3968867-Oxygen,
pubmed-meshheading:3968867-Permeability,
pubmed-meshheading:3968867-Pulmonary Artery
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pubmed:year |
1985
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pubmed:articleTitle |
Activated neutrophils disrupt endothelial monolayer integrity by an oxygen radical-independent mechanism.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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