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1 Biomolecular Transport Dynamics Laboratory, Department of Chemical Engineering, The Pennsylvania State University, University Park 16802; and Departments of 2 Cellular and Molecular Physiology and 3 Ophthalmology, College of Medicine, Hershey, Pennsylvania 17033
Previous studies determined that shear stress imposed on
bovine aortic endothelial cell (BAEC) monolayers increased the
hydraulic conductivity (LP); however, the
mechanism by which shear stress increases LP
remains unknown. This study tested the hypothesis that shear stress
regulates paracellular transport by altering the expression and
phosphorylation state of the tight junction protein occludin. The
effect of shear stress on occludin content was examined by Western blot
analysis. Ten dyn/cm2 significantly reduced occludin
content in a time-dependent manner such that after a 3 h exposure
to shear, occludin content decreased to 44% of control. Twenty
dyn/cm2 decreased occludin content to 50% of control and
increased LP by 4.7-fold after 3 h.
Occludin expression and LP depend on tyrosine kinase activity because erbstatin A (10 µM) attenuated both the shear-induced decrease in occludin content and increase in
LP. Shear stress increased occludin
phosphorylation after 5 min, 15 min, and 3 h exposures. The
shear-induced increase in occludin phosphorylation was attenuated with
dibutyryl (DB) cAMP (1 mM), a reagent previously shown to reverse the
shear-induced increase in LP. We conclude that
shear stress rapidly (
5 min) increases occludin phosphorylation and
significantly decreases the expression of occludin over 1-4 h.
Alterations in the occludin phosphorylation state and occludin total
content are potential mechanisms by which shear stress increases
LP.
erbstatin A; dibutyryl cAMP; permeability; tight junctions
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