Source:http://linkedlifedata.com/resource/pubmed/id/18310225
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2008-5-2
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pubmed:abstractText |
Angiopoietins are ligands for Tie-2 receptors and play important roles in angiogenesis and inflammation. While angiopoietin-1 (Ang-1) inhibits inflammatory responses, angiopoietin-2 (Ang-2) promotes cytokine production and vascular leakage. In this study, we evaluated in vivo and in vitro effects of Escherichia coli lipopolysaccharides (LPS) on angiopoietin expression. Wild-type C57/BL6 mice were injected with saline (control) or E. coli LPS (20 mg/ml ip) and killed 6, 12, and 24 h later. The diaphragm, lung, and liver were excised and assayed for mRNA and protein expression of Ang-1, Ang-2, and Tie-2 protein and tyrosine phosphorylation. LPS injection elicited a severalfold rise in Ang-2 mRNA and protein levels in the three organs. By comparison, both Ang-1 and Tie-2 levels in the diaphragm, liver, and lung were significantly attenuated by LPS administration. In addition, Tie-2 tyrosine phosphorylation in the lung was significantly reduced in response to LPS injection. In vitro exposure to E. coli LPS elicited cell-specific changes in Ang-1 expression, with significant induction in Ang-1 expression being observed in cultured human epithelial cells, whereas significant attenuation of Ang-1 expression was observed in response to E. coli LPS exposure in primary human skeletal myoblasts. In both cell types, E. coli LPS elicited substantial induction of Ang-2 mRNA, a response that was mediated in part through NF-kappaB. We conclude that in vivo endotoxemia triggers functional inhibition of the Ang-1/Tie-2 receptor pathway by reducing Ang-1 and Tie-2 expression and inducing Ang-2 levels and that this response may contribute to enhanced vascular leakage in sepsis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ANGPT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Angiopoietin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Angiopoietin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Angiopoietins,
http://linkedlifedata.com/resource/pubmed/chemical/Angpt1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Angpt4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, TIE-2
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1040-0605
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
L955-63
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pubmed:dateRevised |
2011-8-3
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pubmed:meshHeading |
pubmed-meshheading:18310225-Angiopoietin-1,
pubmed-meshheading:18310225-Angiopoietin-2,
pubmed-meshheading:18310225-Angiopoietins,
pubmed-meshheading:18310225-Animals,
pubmed-meshheading:18310225-Cells, Cultured,
pubmed-meshheading:18310225-Gene Expression,
pubmed-meshheading:18310225-Humans,
pubmed-meshheading:18310225-Lipopolysaccharides,
pubmed-meshheading:18310225-Male,
pubmed-meshheading:18310225-Mice,
pubmed-meshheading:18310225-Mice, Inbred C57BL,
pubmed-meshheading:18310225-Muscle, Skeletal,
pubmed-meshheading:18310225-Myoblasts,
pubmed-meshheading:18310225-NF-kappa B,
pubmed-meshheading:18310225-Pneumonia,
pubmed-meshheading:18310225-Receptor, TIE-2,
pubmed-meshheading:18310225-Respiratory Mucosa,
pubmed-meshheading:18310225-Sepsis
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pubmed:year |
2008
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pubmed:articleTitle |
Regulation of angiopoietin expression by bacterial lipopolysaccharide.
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pubmed:affiliation |
Critical Care Division, Royal Victoria Hospital, 687 Pine Ave West, Montréal, Québec, Canada H3A 1A1.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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