Linked Life Data

11225730

Source:http://linkedlifedata.com/resource/pubmed/id/11225730

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-2-27
pubmed:abstractText
The small GTPase rac1 controls actin redistribution to membrane ruffles in fibroblasts and other cell types, as well as the activation of the NADPH oxidase in phagocytes. We explored the possibility that these two processes could be related. We used a replication-deficient adenoviral vector to overexpress the constitutively active form of rac1, racV12, in human and mouse aortic endothelial cells. We show here that, in addition to membrane ruffle formation, racV12 induced an increase in the total amount of F-actin within endothelial cells. Concurrently, racV12-overexpressing cells produced significantly higher amounts of free radicals, as detected by the fluorescent probe 5-(and-6)-chloromethyl-2',7'-dichloro-dihydrofluorescein diacetate, than cells infected with a control virus encoding the bacterial beta-galactosidase (Ad-betaGal). To assess the specific role of superoxide in racV12-induced actin reorganization, we co-expressed the human enzyme Cu,Zn-superoxide dismutase (SOD), by means of another adenoviral vector construct. Overexpressed SOD reduced the concentration of superoxide detected in Ad-racV12-transfected cells and reversed the effects of Ad-racV12 on the content of filamentous actin. MnTMPyP, an SOD mimetic, as well as the antioxidant N-acetyl cysteine, had similar effects, in that they reduced not only the free radicals production, but also ruffle formation and the concentration of F-actin within racV12-overexpressing endothelial cells. Our data support the hypothesis that superoxide is one of the important mediators acting downstream of rac1 on the pathway of actin cytoskeleton remodeling in endothelial cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1523-0864
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11225730-Acetylcysteine, pubmed-meshheading:11225730-Actins, pubmed-meshheading:11225730-Animals, pubmed-meshheading:11225730-Aorta, pubmed-meshheading:11225730-Blotting, Western, pubmed-meshheading:11225730-Cell Surface Extensions, pubmed-meshheading:11225730-Cells, Cultured, pubmed-meshheading:11225730-Coronary Vessels, pubmed-meshheading:11225730-Culture Media, Serum-Free, pubmed-meshheading:11225730-Cytoskeleton, pubmed-meshheading:11225730-Endothelium, Vascular, pubmed-meshheading:11225730-Fluorescent Dyes, pubmed-meshheading:11225730-Free Radical Scavengers, pubmed-meshheading:11225730-Humans, pubmed-meshheading:11225730-Metalloporphyrins, pubmed-meshheading:11225730-Mice, pubmed-meshheading:11225730-Microscopy, Confocal, pubmed-meshheading:11225730-Microscopy, Fluorescence, pubmed-meshheading:11225730-Recombinant Proteins, pubmed-meshheading:11225730-Superoxide Dismutase, pubmed-meshheading:11225730-Superoxides, pubmed-meshheading:11225730-Transfection, pubmed-meshheading:11225730-rac1 GTP-Binding Protein
pubmed:year
1999
pubmed:articleTitle
The actin cytoskeleton reorganization induced by Rac1 requires the production of superoxide.
pubmed:affiliation
Heart and Lung Institute, Department of Internal Medicine, The Ohio State University, Columbus 43210, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't