Document Detail


Regulation of VE-cadherin linkage to the cytoskeleton in endothelial cells exposed to fluid shear stress.
MedLine Citation:
PMID:  11822879     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Endothelial cells exposed to shear stress realigned and elongated in the direction of flow through the coordinated remodeling of their adherens junctions and actin cytoskeleton. The elaborate networks of VE-cadherin complexes in static cultures became more uniform and compact in response to shear. In contrast, the cortical actin present in static cultures was reorganized into numerous stress fiber bundles distributed parallel to the direction of flow. Exposure to shear did not significantly alter the expression of the junctional proteins VE-cadherin, beta-catenin, and alpha-catenin, but the composition of the junctional complexes did change. We detected a marked decrease in the alpha-catenin associated with VE-cadherin complexes in endothelial monolayers subjected to shear. This loss of alpha-catenin, the protein that links beta-catenin-bound cadherin to the actin cytoskeleton, was not due to decreased quantities of beta-catenin associated with VE-cadherin. Instead, the loss of alpha-catenin from the junctional complexes coincided with the increased tyrosine phosphorylation of beta-catenin associated with VE-cadherin. The change in beta-catenin phosphorylation closely correlated with the shear-induced loss of the protein tyrosine phosphatase SHP-2 from VE-cadherin complexes. Thus, the functional interaction of alpha-catenin with VE-cadherin-bound beta-catenin is regulated by the extent of tyrosine phosphorylation of beta-catenin. This, concomitantly, is regulated by SHP-2 associated with VE-cadherin complexes.
Authors:
Jon A Ukropec; M Katherine Hollinger; Marilyn J Woolkalis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Experimental cell research     Volume:  273     ISSN:  0014-4827     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-02-01     Completed Date:  2002-03-15     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  240-7     Citation Subset:  IM    
Copyright Information:
©2002 Elsevier Science (USA).
Affiliation:
Department of Physiology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
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MeSH Terms
Descriptor/Qualifier:
Antigens, CD
Cadherins / biosynthesis,  metabolism*
Cells, Cultured
Cytoskeletal Proteins / metabolism*
Cytoskeleton / metabolism
Endothelium, Vascular / cytology,  metabolism*
Humans
Intercellular Junctions / metabolism
Intracellular Signaling Peptides and Proteins
Phosphorylation
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatases / metabolism*
Stress, Mechanical
Trans-Activators*
Tyrosine / metabolism
Umbilical Veins / cytology,  metabolism
alpha Catenin
beta Catenin
Grant Support
ID/Acronym/Agency:
HL52132/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, CD; 0/CTNNA1 protein, human; 0/CTNNB1 protein, human; 0/Cadherins; 0/Cytoskeletal Proteins; 0/Intracellular Signaling Peptides and Proteins; 0/Trans-Activators; 0/alpha Catenin; 0/beta Catenin; 0/cadherin 5; 55520-40-6/Tyrosine; EC 3.1.3.48/PTPN11 protein, human; EC 3.1.3.48/PTPN6 protein, human; EC 3.1.3.48/Protein Tyrosine Phosphatase, Non-Receptor Type 11; EC 3.1.3.48/Protein Tyrosine Phosphatase, Non-Receptor Type 6; EC 3.1.3.48/Protein Tyrosine Phosphatases

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


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