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

Détails

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Etat: Public
Version: de l'auteur⸱e
ID Serval
serval:BIB_D5D4D60F0594
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Direct Thy-1/alphaVbeta3 integrin interaction mediates neuron to astrocyte communication.
Périodique
Biochimica et Biophysica Acta-Molecular Cell Research
Auteur⸱e⸱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
Statut éditorial
Publié
Date de publication
06/2008
Peer-reviewed
Oui
Volume
1783
Numéro
6
Pages
1111-1120
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
Résumé
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.
Mots-clé
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
Oui
Création de la notice
13/02/2009 18:55
Dernière modification de la notice
20/08/2019 15:55
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