Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19-20
pubmed:dateCreated
2007-11-5
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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...
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1421-30
pubmed:dateRevised
2009-11-19
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
pubmed:year
2007
pubmed:articleTitle
Modulation of Ca2+ transients in cultured endothelial cells in response to fluid flow through alphav integrin.
pubmed:affiliation
Department of Pharmacology, School of Pharmaceutical Sciences, Showa University, Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan. taku@pharm.showa-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't