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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-8-12
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pubmed:abstractText |
Although extravasation of neutrophils is a critical step in acute inflammation, the role of the endothelial cytoskeleton in neutrophil transmigration has not been fully investigated. We used an in vitro model of neutrophil transmigration across a monolayer of HUVEC cultured on amniotic membrane. Human neutrophils were allowed to migrate across the HUVEC monolayer in response to a gradient leukotriene B4 and then the number of migrated neutrophils were counted microscopically. We also followed endothelial F-actin and myosin filament formation using rhodamine-phalloidin and anti-myosin Ab staining. Myosin light chain (MLC) phosphorylation in endothelial cells was determined by immunoprecipitation of 32P-labeled HUVEC with anti-myosin polyclonal Ab. Normally, neutrophil migration induced F-actin formation, myosin filament formation, and MLC phosphorylation in HUVEC. When HUVEC was pretreated with the myosin light chain kinase (MLCK) inhibitor, ML-9, neutrophil migration was diminished and F-actin formation, myosin filament formation, and MLC phosphorylation were inhibited. Pretreatments of HUVEC with the intracellular calcium ion chelator, bis-(O-aminophenoxyl)ethane-N, N, N', N'-tetraacetic acid acetoxymethyl ester (BAPTA/AM), and the calmodulin antagonist, trifluoperazine, had similar effects. These results indicate that a calcium/ calmodulin-dependent MLCK in endothelial cells regulates neutrophil transendothelial migration.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Leukotriene B4,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Light Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
161
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1533-40
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9686621-Actins,
pubmed-meshheading:9686621-Cell Movement,
pubmed-meshheading:9686621-Cells, Cultured,
pubmed-meshheading:9686621-Endothelium, Vascular,
pubmed-meshheading:9686621-Humans,
pubmed-meshheading:9686621-Leukotriene B4,
pubmed-meshheading:9686621-Myosin Light Chains,
pubmed-meshheading:9686621-Myosin-Light-Chain Kinase,
pubmed-meshheading:9686621-Myosins,
pubmed-meshheading:9686621-Neutrophils,
pubmed-meshheading:9686621-Phosphorylation,
pubmed-meshheading:9686621-Umbilical Veins
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pubmed:year |
1998
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pubmed:articleTitle |
Endothelial myosin light chain kinase regulates neutrophil migration across human umbilical vein endothelial cell monolayer.
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pubmed:affiliation |
Second Department of Surgery, Akita University School of Medicine, Hondo Akita City, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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