Linked Life Data

12584244

Source:http://linkedlifedata.com/resource/pubmed/id/12584244

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2003-2-13
pubmed:abstractText
In endothelial monolayers agonist-induced influx of Ca(2+) and activities of the actin cytoskeleton have been shown to be crucially involved in regulation of barrier properties. By laser tweezer application we demonstrated that the strength of adhesion of VE-cadherin-coated microspheres to the surface of cultured endothelial monolayers is significantly reduced by treatment with two well-established permeability-increasing compounds, cytochalasin D and the Ca(2+)-ionophore A23187, which shows that both compounds directly affect cadherin-mediated adhesion. Cytochalasin D and A23187 caused considerable decay of F-actin (30-60%). Stabilisation of F-actin by jasplakinolide completely blocked drug-induced weakening of bead adhesion showing that attenuation of cadherin-cadherin trans-interaction induced by cytochalasin D and A23187 depends largely on downregulation of F-actin. Single molecule fluorescence microscopy demonstrated that drug-induced weakening of adhesion is accompanied by an increase in lateral mobility of cadherins as well as by dispersal of cadherin-enriched plasmalemmal microdomains. However, the lifetime ( approximately 700 milliseconds, k(off) approximately 1.4 second(-1)) and apparent on-rate of cadherin trans-interaction (relative frequency of binding) remained unchanged in response to cytochalasin D and A23187 indicating that cadherin-mediated adhesion is not modulated by inside-out changes of the affinity but, rather, appears to be controlled by actin-dependent tethering and compartmentalization of cadherins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1001-11
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12584244-Actin Cytoskeleton, pubmed-meshheading:12584244-Actins, pubmed-meshheading:12584244-Animals, pubmed-meshheading:12584244-Antigens, CD, pubmed-meshheading:12584244-Biophysical Phenomena, pubmed-meshheading:12584244-Biophysics, pubmed-meshheading:12584244-Cadherins, pubmed-meshheading:12584244-Calcimycin, pubmed-meshheading:12584244-Cell Adhesion, pubmed-meshheading:12584244-Cell Line, Transformed, pubmed-meshheading:12584244-Cytochalasin D, pubmed-meshheading:12584244-Endothelium, Vascular, pubmed-meshheading:12584244-Immunoglobulin Fab Fragments, pubmed-meshheading:12584244-Ionophores, pubmed-meshheading:12584244-Lasers, pubmed-meshheading:12584244-Mice, pubmed-meshheading:12584244-Micromanipulation, pubmed-meshheading:12584244-Microscopy, Fluorescence, pubmed-meshheading:12584244-Microspheres, pubmed-meshheading:12584244-Myocardium, pubmed-meshheading:12584244-Nucleic Acid Synthesis Inhibitors
pubmed:year
2003
pubmed:articleTitle
Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells.
pubmed:affiliation
Institute of Anatomy and Cell Biology, University of Würzburg, Koellikerstr. 6, D-97070 Würzburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't