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Articles in PresS, published online ahead of print December 13, 2002
J Appl Physiol, 10.1152/jap.00690.2002
Submitted on July 29, 2002
Accepted on October 24, 2002
1 Division of Pulmonary and Critical Care Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, USA
* To whom correspondence should be addressed. E-mail: drgarcia{at}jhmi.edu.
Sphingosine1-phosphate (S1P) enhances human pulmonary endothelial monolayer integrity via Rac GTPase-dependent formation of a cortical actin ring [Garcia et al., 2001]. The mechanisms underlying this response are not well understood but may involve rapid redistribution of focal adhesions (FA) as attachment sites for actin filaments. In this report, we evaluate the effects of S1P on the redistribution of paxillin, focal adhesion kinase (FAK) and the G-protein-coupled receptor kinase interacting proteins (GITs). S1P induced Rac GTPase activation and cortical actin ring formation at physiological concentrations (0.5 µM), whereas at 5 µM, S1P caused prominent stress fiber formation and activation of Rho and Rac GTPases. S1P (0.5 µM) stimulated the tyrosine phosphorylation of both FAK [Y576] and paxillin linked to FA disruption and redistribution to the cell periphery. Furthermore, SIP induced a transient association of GIT1 with paxillin, and redistribution of GIT2-paxillin complex to the cell cortical area without affecting GIT2-paxillin association. These results suggest a role of focal adhesion rearrangement in S1P-mediated barrier enhancement via Rac- and GIT-mediated processes.
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