Linked Life Data

10362589

Source:http://linkedlifedata.com/resource/pubmed/id/10362589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6 Pt 1
pubmed:dateCreated
1999-7-29
pubmed:abstractText
A permissive role of nitric oxide (NO) in endothelial cell migration and angiogenesis promoted by vascular endothelial growth factor (VEGF), endothelin, and substance P has previously been established. The present studies were designed to examine the mechanism(s) involved in the NO effect on focal adhesions. Time-lapse videomicroscopy of human umbilical vein endothelial cells (HUVECs) plated on the silicone rubber substrate revealed that unstimulated cells were constantly remodeling the wrinkling pattern, indicative of changing tractional forces. Application of NO donors reversibly decreased the degree of wrinkling, consistent with the release of tractional forces exerted by focal adhesions and stress fibers. Morphometric and immunocytochemical analyses showed that NO inhibited adhesion and spreading of HUVECs and attenuated recruitment of paxillin to focal adhesions. NO also had a profound dose-dependent effect on the formation of stress fibers by HUVECs. De novo formation of focal adhesions in HUVECs was significantly diminished in the presence of NO donors. Migration of HUVECs showed an absolute requirement for the functional NO synthase. NO donors did not interfere with focal adhesion kinase recruitment to focal adhesions but affected the state of its tyrosine phosphorylation, as judged from the results of immunoprecipitation and immunoblotting experiments. Videomicroscopy of HUVECs presented with VEGF in a micropipette showed that the rate of cell migration was slowed down by NO synthase inhibition as well as by inhibition of tyrosine phosphorylation. Collectively, these data indicate that NO reversibly releases tractional forces exerted by spreading endothelial cells via interference with the de novo formation of focal adhesions, tyrosine phosphorylation of components of focal adhesion complexes, and assembly of stress fibers.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C1271-81
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10362589-Cell Adhesion, pubmed-meshheading:10362589-Cell Line, pubmed-meshheading:10362589-Cell Movement, pubmed-meshheading:10362589-Endothelial Growth Factors, pubmed-meshheading:10362589-Endothelium, Vascular, pubmed-meshheading:10362589-Humans, pubmed-meshheading:10362589-Lymphokines, pubmed-meshheading:10362589-Microscopy, Video, pubmed-meshheading:10362589-Nitric Oxide, pubmed-meshheading:10362589-Nitric Oxide Donors, pubmed-meshheading:10362589-Nitric Oxide Synthase, pubmed-meshheading:10362589-Phosphorylation, pubmed-meshheading:10362589-Protein-Tyrosine Kinases, pubmed-meshheading:10362589-Tissue Adhesions, pubmed-meshheading:10362589-Tyrosine, pubmed-meshheading:10362589-Vascular Diseases, pubmed-meshheading:10362589-Vascular Endothelial Growth Factor A, pubmed-meshheading:10362589-Vascular Endothelial Growth Factors
pubmed:year
1999
pubmed:articleTitle
Nitric oxide modulation of focal adhesions in endothelial cells.
pubmed:affiliation
Departments of Medicine and Physiology, State University of New York, Stony Brook, New York 11794-8152, USA. mgoligorsky@mail.som.sunysb.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't