Direct Thy-1/alphaVbeta3 integrin interaction mediates neuron to astrocyte communication.

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Serval ID
serval:BIB_D5D4D60F0594
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Direct Thy-1/alphaVbeta3 integrin interaction mediates neuron to astrocyte communication.
Journal
Biochimica et Biophysica Acta-Molecular Cell Research
Author(s)
Hermosilla T., Muñoz D., Herrera-Molina R., Valdivia A., Muñoz N., Nham S.U., Schneider P., Burridge K., Quest A.F., Leyton L.
ISSN
0167-4889
ISSN-L
1879-2596
Publication state
Published
Issued date
06/2008
Peer-reviewed
Oui
Volume
1783
Number
6
Pages
1111-1120
Language
english
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
Abstract
Thy-1 is an abundant neuronal glycoprotein of poorly defined function. We recently provided evidence indicating that Thy-1 clusters a beta3-containing integrin in astrocytes to induce tyrosine phosphorylation, RhoA activation and the formation of focal adhesions and stress fibers. To date, the alpha subunit partner of beta3 integrin in DI TNC1 astrocytes is unknown. Similarly, the ability of neuronal, membrane-bound Thy-1 to trigger astrocyte signaling via integrin engagement remains speculation. Here, evidence that alphav forms an alphavbeta3 heterodimer in DI TNC1 astrocytes was obtained. In neuron-astrocyte association assays, the presence of either anti-alphav or anti-beta3 integrin antibodies reduced cell-cell interaction demonstrating the requirement of both integrin subunits for this association. Moreover, anti-Thy-1 antibodies blocked stimulation of astrocytes by neurons but not the binding of these two cell types. Thus, neuron-astrocyte association involved binding between molecular components in addition to the Thy-1-integrin; however, the signaling events leading to focal adhesion formation in astrocytes depended exclusively on the latter interaction. Additionally, wild-type (RLD) but not mutated (RLE) Thy-1 was shown to directly interact with alphavbeta3 integrin by Surface Plasmon Resonance analysis. This interaction was promoted by divalent cations and was species-independent. Together, these results demonstrate that the alphavbeta3 integrin heterodimer interacts directly with Thy-1 present on neuronal cells to stimulate astrocytes.
Keywords
Animals, Antigens, Thy-1, Astrocytes, Blotting, Western, Cell Adhesion, Cell Communication, Cells, Cultured, Fluorescent Antibody Technique, Indirect, Humans, Immunoprecipitation, Integrin alphaVbeta3, Mice, Neurons, Rats, Recombinant Proteins, Surface Plasmon Resonance, rhoA GTP-Binding Protein
Pubmed
Web of science
Open Access
Yes
Create date
13/02/2009 18:55
Last modification date
20/08/2019 15:55
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