Document Detail


Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate.
MedLine Citation:
PMID:  9632115     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The involvement of tyrosine protein phosphorylation in the regulation of endothelial cell (EC) contraction and barrier function is poorly understood. We have previously shown that myosin light chain (MLC) phosphorylation catalyzed by a novel 214 kDa EC myosin light chain kinase (MLCK) isoform is a key event in EC contraction and barrier dysfunction [Garcia et al. (1995): J Cell Physiol 163:510-522; Garcia et al. (1997): Am J Respir Cell Mol Biol 16:487-491]. In this study, we tested the hypothesis that tyrosine phosphatases participate in the regulation of EC contraction and barrier function via modulation of MLCK activity. The tyrosine phosphatase inhibitor, sodium orthovanadate (vanadate), significantly decreased electrical resistance across bovine EC monolayers and increased albumin permeability consistent with EC barrier impairment. Vanadate significantly increased EC MLC phosphorylation in a time-dependent manner (maximal increase observed at 10 min) and augmented both the MLC phosphorylation and permeability responses produced by thrombin, an agonist which rapidly increases tyrosine kinase activities. The vanadate-mediated increase in MLC phosphorylation was not associated with alterations in either phosphorylase A Ser/Thr phosphatase activities or in cytosolic [Ca2+] but was strongly associated with significant increases in EC MLCK phosphotyrosine content. These data suggest that tyrosine phosphatase activities may participate in EC contractile and barrier responses via the regulation of the tyrosine phosphorylation status of EC MLCK.
Authors:
L I Gilbert-McClain; A D Verin; S Shi; R P Irwin; J G Garcia
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cellular biochemistry     Volume:  70     ISSN:  0730-2312     ISO Abbreviation:  J. Cell. Biochem.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-08-12     Completed Date:  1998-08-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8205768     Medline TA:  J Cell Biochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  141-55     Citation Subset:  IM    
Affiliation:
Department of Medicine, Indiana University School of Medicine, Richard L. Roudebush Veterans Administration Medical Center, Indianapolis 46202, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium / metabolism
Cattle
Cell Membrane Permeability / drug effects
Cells, Cultured
Endothelium, Vascular / cytology,  drug effects*,  metabolism
Enzyme Activation
Myosin Light Chains / metabolism*
Myosin-Light-Chain Kinase / metabolism
Phosphoprotein Phosphatases / antagonists & inhibitors,  metabolism
Phosphorylation
Protein Tyrosine Phosphatases / metabolism
Thrombin / pharmacology
Vanadates / pharmacology*
Grant Support
ID/Acronym/Agency:
HL50533/HL/NHLBI NIH HHS; HL57362/HL/NHLBI NIH HHS; HL57402/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Myosin Light Chains; 0/Vanadates; 7440-70-2/Calcium; EC 2.7.11.18/Myosin-Light-Chain Kinase; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 3.1.3.48/Protein Tyrosine Phosphatases; EC 3.4.21.5/Thrombin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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