Source:http://linkedlifedata.com/resource/pubmed/id/17931663
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19-20
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pubmed:dateCreated |
2007-11-5
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pubmed:abstractText |
In order to determine whether integrin dynamics is associated with intracellular Ca(2+) concentration ([Ca(2+)](i)) mobilization in ECs in response to hemodynamic forces, changes in [Ca(2+)](i) in fluo-4-loaded cultured bovine aortic endothelial cells (BAECs) under fluid flow conditions were visualized employing laser scanning confocal microscopy. Following the onset of flow stimulus, transient increases in [Ca(2+)](i) occurred several times in individual BAECs during the 30-min observation period. The frequency of these [Ca(2+)](i) transients was clearly reduced by the application of an integrin antagonist (GRGDSP peptide). Furthermore, treatment of cells with an integrin activator (Mn(2+)) resulted in reduction of peak [Ca(2+)](i) levels and elevated frequency, which was markedly rescued upon GRGDSP administration. In contrast, an actin de-polymerizing agent (cytochalasin D) exerted no inhibitory effects; rather, cytochalasin D more likely facilitated [Ca(2+)](i) transients. Moreover, [Ca(2+)](i) transients, which were suppressed by short interference RNA-induced silencing of alphav integrin, exhibited greater frequently in cells cultured on vitronectin substratum in comparison with those cultured on fibronectin or collagen substratum. Either removal of extracellular Ca(2+), application of an inhibitor of endoplasmic reticulum Ca(2+)-ATPase (thapsigargin) or non-selective cation channel blocker (La(3+)) inhibited the [Ca(2+)](i) transients. Additionally, [Ca(2+)](i) transients were attenuated by extracellular signal-regulated kinase (ERK) kinase inhibitor (U0126); in contrast, [Ca(2+)](i) transients were unaffected by tyrosine kinase inhibitor (genistein) or phosphatidylinositol 3-kinase (PI3K) inhibitor (LY294002). Therefore, our findings revealed that alphav integrin dynamics modulates the frequency of flow-induced [Ca(2+)](i) transients in BAECs in an ERK-dependent fashion.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Butadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type IV,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alphaV,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/Nitriles,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/U 0126,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/glycyl-arginyl-glycyl-aspartyl-seryl...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0024-3205
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1421-30
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17931663-Actins,
pubmed-meshheading:17931663-Animals,
pubmed-meshheading:17931663-Butadienes,
pubmed-meshheading:17931663-Calcium,
pubmed-meshheading:17931663-Cattle,
pubmed-meshheading:17931663-Cell Adhesion,
pubmed-meshheading:17931663-Cells, Cultured,
pubmed-meshheading:17931663-Collagen Type IV,
pubmed-meshheading:17931663-Cytoskeleton,
pubmed-meshheading:17931663-Dose-Response Relationship, Drug,
pubmed-meshheading:17931663-Endothelial Cells,
pubmed-meshheading:17931663-Enzyme Inhibitors,
pubmed-meshheading:17931663-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:17931663-Fibronectins,
pubmed-meshheading:17931663-Integrin alphaV,
pubmed-meshheading:17931663-Manganese,
pubmed-meshheading:17931663-Microscopy, Confocal,
pubmed-meshheading:17931663-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:17931663-Models, Biological,
pubmed-meshheading:17931663-Nitriles,
pubmed-meshheading:17931663-Oligopeptides,
pubmed-meshheading:17931663-RNA Interference,
pubmed-meshheading:17931663-Rheology,
pubmed-meshheading:17931663-Stress, Mechanical,
pubmed-meshheading:17931663-Vitronectin
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pubmed:year |
2007
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pubmed:articleTitle |
Modulation of Ca2+ transients in cultured endothelial cells in response to fluid flow through alphav integrin.
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pubmed:affiliation |
Department of Pharmacology, School of Pharmaceutical Sciences, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan. taku@pharm.showa-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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