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Articles in PresS, published online ahead of print November 27, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00862.2002
Submitted on October 3, 2002
Accepted on November 21, 2002
1 The Benjamin W. Zweifach Microcirculation Laboratories, V.A. Medical Center, Tucson, AZ, USA
* To whom correspondence should be addressed. E-mail: rcschaeffer{at}earthlink.net.
Endothelial monolayer hyperpermeability is regulated by a myosin light chain phosphorylation (MLC-P)-dependent contractile mechanism. In this study, we tested the role of src-dependent tyrosine phosphorylation to modulate endothelial contraction and monolayer barrier function using the myosin phosphatase inhibitor, calyculin A (CalA), to directly elevate MLC-P in combination with the src-family tyrosine kinase inhibitor, herbimycin A (HA), in bovine pulmonary artery endothelial cells (EC). CalA stimulated an increase in MLC-P, src kinase activity, an increase in the tyrosine phosphorylation of paxillin and focal adhesion kinase (p125FAK), and monolayer hyperpermeability. Microscopic examination of CalA-treated EC revealed a contractile morphology characterized by peripheral contractile bands of actomyosin filaments and stress fibers linked to phosphotyrosine-containing focal adhesions (FA). These CalA-dependent events were HA-sensitive. HA alone stimulated an improvement in monolayer barrier formation by reducing the levels of MLC-P, PY-containing proteins, and the number of large paracellular holes. These data show that src kinase plays an important role to regulate monolayer hyperpermeability through adjustments in tyrosine phosphorylation, MLC-P, and EC contraction.
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