Document Detail

The role of the dynamics of focal adhesion kinase in the mechanotaxis of endothelial cells.
MedLine Citation:
PMID:  11891289     Owner:  NLM     Status:  MEDLINE    
The migration of vascular endothelial cells (ECs) is critical in vascular remodeling. We showed that fluid shear stress enhanced EC migration in flow direction and called this "mechanotaxis." To visualize the molecular dynamics of focal adhesion kinase (FAK) at focal adhesions (FAs), FAK tagged with green fluorescence protein (GFP) was expressed in ECs. Within 10 min of shear stress application, lamellipodial protrusion was induced at cell periphery in the flow direction, with the recruitment of FAK at FAs. ECs under flow migrated with polarized formation of new FAs in flow direction, and these newly formed FAs subsequently disassembled after the rear of the cell moved over them. The cells migrating under flow had a decreased number of FAs. In contrast to shear stress, serum did not significantly affect the speed of cell migration. Serum induced lamellipodia and FAK recruitment at FAs without directional preference. FAK(Y397) phosphorylation colocalized with GFP-FAK at FAs in both shear stress and serum experiments. The total level of FAK(Y397) phosphorylation after shear stress was lower than that after serum treatment, suggesting that the polarized change at cell periphery rather than the total level of FAK(Y397) phosphorylation is important for directional migration. Our results demonstrate the dynamics of FAK at FAs during the directional migration of EC in response to mechanical force, and suggest that mechanotaxis is an important mechanism controlling EC migration.
Song Li; Peter Butler; Yingxiao Wang; Yingli Hu; Dong Cho Han; Shunichi Usami; Jun-Lin Guan; Shu Chien
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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.     Date:  2002-03-12
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  99     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2002 Mar 
Date Detail:
Created Date:  2002-03-20     Completed Date:  2002-04-24     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3546-51     Citation Subset:  IM    
Department of Bioengineering and The Whitaker Institute of Biomedical Engineering, University of California at San Diego, La Jolla, CA 92093-0427, USA.
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MeSH Terms
Actins / metabolism
Biopolymers / metabolism
Cell Movement* / drug effects
Cell Polarity
Cytoskeleton / drug effects,  metabolism
Endothelium, Vascular / cytology*,  drug effects,  enzymology*
Focal Adhesion Protein-Tyrosine Kinases
Focal Adhesions / drug effects,  enzymology*,  metabolism
Protein Transport / drug effects
Protein-Tyrosine Kinases / metabolism*
Pseudopodia / drug effects,  enzymology,  metabolism
Serum Albumin / pharmacology
Reg. No./Substance:
0/Actins; 0/Biopolymers; 0/Serum Albumin; EC Kinases; EC Adhesion Protein-Tyrosine Kinases

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

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