AJP - Lung Add DOIs to your references at manuscript stage!
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Am J Physiol Lung Cell Mol Physiol (August 10, 2007). doi:10.1152/ajplung.00120.2007
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
293/4/L843    most recent
00120.2007v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Csortos, C.
Right arrow Articles by Verin, A. D
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Csortos, C.
Right arrow Articles by Verin, A. D
Submitted on March 27, 2007
Accepted on August 6, 2007

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

Csilla Csortos1, Irina Kolosova2, and Alexander D Verin3*

1 Department of, University of Debrecen, Debrecen, Hungary
2 Department of, Case Western Reserve University, Cleveland, Ohio, United States
3 Medicine, Medical College of Georgia, Augusta, Georgia, United States

* To whom correspondence should be addressed. E-mail: averin{at}mcg.edu.

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.




This article has been cited by other articles:


Home page
Am. J. Respir. Cell Mol. Bio.Home page
A. Antonov, C. Snead, B. Gorshkov, G. N. Antonova, A. D. Verin, and J. D. Catravas
Heat Shock Protein 90 Inhibitors Protect and Restore Pulmonary Endothelial Barrier Function
Am. J. Respir. Cell Mol. Biol., November 1, 2008; 39(5): 551 - 559.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
C. Csortos, I. Czikora, N. V. Bogatcheva, D. M. Adyshev, C. Poirier, G. Olah, and A. D. Verin
TIMAP is a positive regulator of pulmonary endothelial barrier function
Am J Physiol Lung Cell Mol Physiol, September 1, 2008; 295(3): L440 - L450.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 2007 by the American Physiological Society.