Linked Life Data

10669631

Source:http://linkedlifedata.com/resource/pubmed/id/10669631

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-3-3
pubmed:abstractText
CD9, a widely expressed membrane protein of the tetraspanin family, has been implicated in diverse functions, such as signal transduction, cell adhesion, and cell motility. We tested the effects of an anti-CD9 monoclonal antibody (ALMA.1) on the migration and proliferation of human vascular endothelial cells (ECs) during repair of an in vitro mechanical wound mimicking angiogenic processes. ALMA.1 induced dose-dependent inhibition of wound repair with a 35+/-1.5% decrease at 20 microg/mL. Only cell migration was affected, because the rate of proliferation of ECs at the lesion margin was not modified and because the inhibition of repair was also observed for nonproliferating irradiated ECs. Monoclonal antibodies against CD63 tetraspanin (H5C6) and control mouse IgG (MOPC-21) were inactive. CD9, one of the most abundant proteins at the surface of ECs, colocalized with beta(1) or beta(3) integrins on EC membranes in double-labeling immunofluorescence experiments with ALMA.1 and an anti-beta(1) (4B4) or anti-beta(3) (SDF.3) monoclonal antibody. Moreover, ALMA.1 and 4B4 had additive inhibitory effects on lesion repair, whereas 4B4 alone also inhibited EC proliferation. In transmembrane Boyden-type assays, ALMA.1 induced dose-dependent inhibition of EC migration toward fibronectin and vitronectin with 45+/-6% and 31+/-10% inhibition, respectively, at 100 microg/mL. 4B4 inhibited migration toward fibronectin at 10 microg/mL but had no effect in the case of vitronectin. Adhesion of ECs to immobilized anti-CD9 monoclonal antibodies induced tyrosine-phosphorylated protein levels similar to those observed during interactions with beta(1) or beta(3) integrins. These results point to the involvement of CD9 in EC adhesion and migration during lesion repair and angiogenesis, probably through cooperation with integrins. As such, CD9 is a potential target to inhibit angiogenesis in metastatic and atherosclerotic processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1079-5642
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
360-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10669631-Antibodies, pubmed-meshheading:10669631-Antigens, CD, pubmed-meshheading:10669631-Antigens, CD9, pubmed-meshheading:10669631-Cell Adhesion, pubmed-meshheading:10669631-Cell Division, pubmed-meshheading:10669631-Cell Movement, pubmed-meshheading:10669631-Cells, Cultured, pubmed-meshheading:10669631-Endothelium, Vascular, pubmed-meshheading:10669631-Fibronectins, pubmed-meshheading:10669631-Humans, pubmed-meshheading:10669631-Integrins, pubmed-meshheading:10669631-Membrane Glycoproteins, pubmed-meshheading:10669631-Phosphorylation, pubmed-meshheading:10669631-Receptors, IgG, pubmed-meshheading:10669631-Tissue Distribution, pubmed-meshheading:10669631-Tyrosine, pubmed-meshheading:10669631-Vitronectin, pubmed-meshheading:10669631-Wound Healing, pubmed-meshheading:10669631-Wounds and Injuries
pubmed:year
2000
pubmed:articleTitle
CD9 participates in endothelial cell migration during in vitro wound repair.
pubmed:affiliation
INSERM U. 311, Etablissement de Transfusion Sanguine de Strasbourg Strasbourg, France. claudine.soyer@etss.u-strasbg.fr
pubmed:publicationType
Journal Article, In Vitro