Am J Physiol Cell Physiol AJP: Gastrointestinal and Liver Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 279: C1285-C1289, 2000;
0363-6143/00 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
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 Web of Science (29)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tinsley, J. H.
Right arrow Articles by Yuan, S. Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tinsley, J. H.
Right arrow Articles by Yuan, S. Y.
Vol. 279, Issue 4, C1285-C1289, October 2000

RAPID COMMUNICATION
Myosin light chain kinase transference induces myosin light chain activation and endothelial hyperpermeability

John H. Tinsley1, Primal De Lanerolle2, Emily Wilson1, Weiya Ma1, and Sarah Y. Yuan1

1 Departments of Surgery and Medical Physiology, Texas A&M University System Health Science Center, Temple, Texas 76504; and 2 Department of Physiology, University of Illinois at Chicago, Chicago, Illinois 60612

The actomyosin complex is the major cytoskeletal component that controls cell contraction. In this study, we investigated the effects of actomyosin interaction on endothelial barrier function and gap formation. Activated myosin light chain kinase (MLCK) protein was transferred into coronary venular endothelial cell (CVEC) monolayers. Uptake of the activated protein resulted in a significant shift in myosin light chain (MLC) from an unphosphorylated to a diphosphorylated form. In addition, MLCK induced a hyperpermeability response of the monolayer as measured by albumin transendothelial flux. Microscopic examination of MLCK-treated CVECs revealed widespread gap formation in the monolayer, loss of peripheral beta -catenin, and increases in actin stress fibers. Inhibition of all of the above responses by a specific MLCK inhibitor suggests they are the direct result of exogenously added MLCK. These data suggest that activation of MLCK in CVECs causes phosphorylation of MLC and contraction of CVECs, resulting in gap formation and concomitant increases in permeability. This study uses a novel technique to measure the effects of an activated kinase on both its substrate and cellular morphology and function through direct transference into endothelial cells.

endothelial permeability; actin cytoskeleton; phosphorylation


This article has been cited by other articles:


Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
C. Csortos, I. Kolosova, and A. D. Verin
Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family
Am J Physiol Lung Cell Mol Physiol, October 1, 2007; 293(4): L843 - L854.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
S. K. Quadri and J. Bhattacharya
Resealing of endothelial junctions by focal adhesion kinase
Am J Physiol Lung Cell Mol Physiol, January 1, 2007; 292(1): L334 - L342.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
D. Ye, I. Ma, and T. Y. Ma
Molecular mechanism of tumor necrosis factor-{alpha} modulation of intestinal epithelial tight junction barrier
Am J Physiol Gastrointest Liver Physiol, March 1, 2006; 290(3): G496 - G504.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Heart Circ. Physiol.Home page
J. W. Breslin, H. Sun, W. Xu, C. Rodarte, A. B. Moy, M. H. Wu, and S. Y. Yuan
Involvement of ROCK-mediated endothelial tension development in neutrophil-stimulated microvascular leakage
Am J Physiol Heart Circ Physiol, February 1, 2006; 290(2): H741 - H750.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
D. Mehta and A. B. Malik
Signaling Mechanisms Regulating Endothelial Permeability
Physiol Rev, January 1, 2006; 86(1): 279 - 367.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
S. S. An, C. M. Pennella, A. Gonnabathula, J. Chen, N. Wang, M. Gaestel, P. M. Hassoun, J. J. Fredberg, and U. S. Kayyali
Hypoxia alters biophysical properties of endothelial cells via p38 MAPK- and Rho kinase-dependent pathways
Am J Physiol Cell Physiol, September 1, 2005; 289(3): C521 - C530.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
J. H. Tinsley, N. R. Teasdale, and S. Y. Yuan
Myosin light chain phosphorylation and pulmonary endothelial cell hyperpermeability in burns
Am J Physiol Lung Cell Mol Physiol, April 1, 2004; 286(4): L841 - L847.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Heart Circ. Physiol.Home page
J. W. Breslin and S. Y. Yuan
Involvement of RhoA and Rho kinase in neutrophil-stimulated endothelial hyperpermeability
Am J Physiol Heart Circ Physiol, March 1, 2004; 286(3): H1057 - H1062.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
M. Guo, M. H. Wu, H. J. Granger, and S. Y. Yuan
Transference of recombinant VE-cadherin cytoplasmic domain alters endothelial junctional integrity and porcine microvascular permeability
J. Physiol., January 1, 2004; 554(1): 78 - 88.
[Abstract] [Full Text] [PDF]

Home page
 J. Appl. Physiol.Home page
S. M. Dudek and J. G. N. Garcia
Cytoskeletal regulation of pulmonary vascular permeability
J Appl Physiol, October 1, 2001; 91(4): 1487 - 1500.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online