Signaling triggered by Thy-1 interaction with ? 3 integrin on astrocytes is an essential step towards unraveling neuronal Thy-1 function

Avalos A.M.; Labra C.V.; Leyton, L; Quest, A.F.G.

Keywords: proteins, growth, neurons, localization, adhesion, mouse, fiber, animals, phosphorylation, antigen, protein, cell, structure, ligand, surface, humans, transduction, receptor, astrocytes, astrocyte, interaction, nerve, signal, cytoskeleton, integrin, article, factor, molecule, actin, mammalia, guanosine, function, rho, thy-1, vitronectin, controlled, animal, study, 1, nonhuman, Receptors,, Animalia, triphosphatase, potential, Antigens,, GTP-Binding, beta3, spreading, Thy

Abstract

Thy-1 is an abundant neuronal glycoprotein in mammals. Despite such prevalence, Thy-1 function remains largely obscure in the absence of a defined ligand. Recently described evidence that Thy-1 interacts with ?3 integrin on astrocytes will be discussed. Thy-1 binding to ?3 integrin triggers tyrosine phosphorylation of focal adhesion proteins in astrocytes, thereby promoting focal adhesion formation, cell attachment and spreading. Thy-1 has been reported to modulate neurite outgrowth by triggering a cellular response in neurons. However, our data indicate that Thy-1 can also initiate signaling events that promote adhesion of adjacent astrocytes to the underlying surface. Preliminary results suggest that morphological changes observed in the actin cytoskeleton of astrocytes as a consequence of Thy-1 binding is mediated by small GTPases from the Rho family. Our findings argue that Thy-1 functions in a bimodal fashion, as a receptor on neuronal cells and as a ligand for ?3 integrin receptor on astrocytes. Since Thy-1 is implicated in the inhibition of neurite outgrowth, signaling events in astrocytes are likely to play an important role in this process.

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Título según SCOPUS: Signaling triggered by Thy-1 interaction with ?3 integrin on astrocytes is an essential step towards unraveling neuronal Thy-1 function
Título de la Revista: BIOLOGICAL RESEARCH
Volumen: 35
Número: 2
Editorial: Springer Nature
Fecha de publicación: 2002
Página de inicio: 231
Página final: 238
Idioma: English
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036401071&partnerID=q2rCbXpz
Notas: SCOPUS