dc.creator | Avalos, Ana Maria | |
dc.creator | Labra, Cecilia V. | |
dc.creator | Quest, Andrew F. G. | |
dc.creator | Leyton Campos, Lisette | |
dc.date.accessioned | 2019-01-29T17:51:09Z | |
dc.date.available | 2019-01-29T17:51:09Z | |
dc.date.created | 2019-01-29T17:51:09Z | |
dc.date.issued | 2002 | |
dc.identifier | Biological Research, Volumen 35, Issue 2, 2018, Pages 231-238 | |
dc.identifier | 07169760 | |
dc.identifier | http://repositorio.uchile.cl/handle/2250/163518 | |
dc.description.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 β3 integrin on astrocytes will be discussed. Thy-1 binding to β3 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 β3 integrin recepto | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Biological Research | |
dc.subject | Astrocytes | |
dc.subject | Focal adhesion | |
dc.subject | GPI-anchored proteins | |
dc.subject | Integrins | |
dc.subject | Thy-1 ligand | |
dc.title | Signaling triggered by Thy-1 interaction with β3 integrin on astrocytes is an essential step towards unraveling neuronal Thy-1 function | |
dc.type | Artículos de revistas | |