Related Experiment Videos
Tenascin-contactin/F11 interactions: a clue for a developmental role?
L Vaughan1, P Weber, L D'Alessandri
1Laboratorium für Biochemie I, ETH-Zentrum, Zürich, Switzerland.
Perspectives on Developmental Neurobiology
|January 1, 1994
Summary
Researchers identified two cell surface receptors for tenascin: contactin/F11 and glypican. These interactions are crucial for tenascin
Area of Science:
- Neuroscience
- Cell Biology
- Developmental Biology
Background:
- Extracellular matrix glycoprotein tenascin influences cell adhesion and neurite outgrowth.
- Understanding tenascin's cellular receptors is key to elucidating its developmental roles.
- Two distinct tenascin ligands have been previously identified.
Purpose of the Study:
- To isolate and characterize cellular receptors for tenascin.
- To investigate the binding sites and interaction mechanisms between tenascin and its receptors.
- To explore the role of tenascin-ligand interactions in neural development.
Main Methods:
- Affinity chromatography using tenascin-Sepharose.
- Solid-phase assays.
- Fusion protein analysis and site-directed mutagenesis.
- Immunohistochemistry and in situ hybridization for tenascin isoforms and contactin/F11 distribution.
Main Results:
- Identified neuronal cell adhesion molecule contactin/F11 (immunoglobulin superfamily) as a tenascin receptor.
- Identified heparan sulfate proteoglycan glypican as a second tenascin receptor.
- Localized a tenascin binding site to the fifth fibronectin type III homology domain.
- Observed coordinate upregulation of tenascin isoforms and contactin/F11 in embryonic chick retina development.
Conclusions:
- Contactin/F11 and glypican are key cellular receptors mediating tenascin's effects on cell adhesion and neurite outgrowth.
- Specific binding interactions involving tenascin's fibronectin type III domains are critical.
- Tenascin-receptor interactions likely contribute to pattern formation in the developing nervous system.