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

Biol Res. 2002;35(2):231-8. doi: 10.4067/s0716-97602002000200015.


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 beta 3 integrin on astrocytes will be discussed. Thy-1 binding to beta 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 beta 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Astrocytes / physiology*
  • Humans
  • Integrin beta3 / physiology*
  • Neurons / physiology*
  • Receptors, Vitronectin / physiology
  • Signal Transduction / physiology*
  • Thy-1 Antigens / physiology*
  • rho GTP-Binding Proteins / physiology


  • Integrin beta3
  • Receptors, Vitronectin
  • Thy-1 Antigens
  • rho GTP-Binding Proteins