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Am J Physiol Lung Cell Mol Physiol 293: L843-L854, 2007. First published August 10, 2007; doi:10.1152/ajplung.00120.2007
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INVITED REVIEW

Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family

Csilla Csortos,1,2 Irina Kolosova,1,3 and Alexander D. Verin1,4

1Department of Medicine, Division of Biological Sciences, The University of Chicago, Chicago, Illinois; 2Department of Medical Chemistry, Research Center for Molecular Medicine, University of Debrecen, Medical and Health Science Center, Debrecen, Hungary; 3Division of Pulmonary, Critical Care and Sleep Medicine, Department of Medicine, Case Western Reserve University, Cleveland, Ohio; and 4Medical College of Georgia, Vascular Biology Center, Augusta, Georgia

Reversible phosphorylation of cytoskeletal and cytoskeleton-associated proteins is a significant element of endothelial barrier function regulation. Therefore, understanding the mechanisms of phosphorylation/dephosphorylation of endothelial cell cytoskeletal proteins is vital to the treatment of severe lung disorders such as high permeability pulmonary edema. In vivo, there is a controlled balance between the activities of protein kinases and phosphatases. Due to various external or internal signals, this balance may be shifted. The actual balances at a given time alter the phosphorylation level of certain proteins with appropriate physiological consequences. The latest information about the structure and regulation of different types of Ser/Thr protein phosphatases participating in the regulation of endothelial cytoskeletal organization and barrier function will be reviewed here.

endothelial barrier function; Ser/Thr protein phosphatases


Address for reprint requests and other correspondence: Alexander D. Verin, Vascular Biology Center, CB-3210A, Medical College of Georgia, Augusta, GA 30912-2500 (e-mail: averin{at}mcg.edu)






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