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First published online 29 January 2003
doi: 10.1242/jcs.00322
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Research Article |
1 Institute of Anatomy and Cell Biology, University of Würzburg,
Koellikerstr. 6, D-97070 Würzburg, Germany
2 Institute of Biophysics, University of Linz, Altenbergerstr. 69, A-4040 Linz,
Austria
* Author for correspondence (e-mail: anat015{at}mail.uni-wuerzburg.de)
Accepted 13 December 2002
In endothelial monolayers agonist-induced influx of Ca2+ 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 Ca2+-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 (
700 milliseconds, koff1.4
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.
Key words: VE-cadherin, Biophysics, Permeability, Actin
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