Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11

Eur J Neurosci. 1996 Apr;8(4):766-82. doi: 10.1111/j.1460-9568.1996.tb01262.x.

Abstract

We have identified distinct domains of the rat extracellular matrix glycoprotein tenascin-R using recombinant fragments of the molecule that confer neuronal cell functions. In short-term adhesion assays (0.5 h), cerebellar neurons adhered best to the fragment representing the fibrinogen knob (FG), but also the fibronectin type III (FN) repeats 1-2 and 6-8. FG, FN1-2 and FN3-5 were the most repellent fragments for neuronal cell bodies. Neurites and growth cones were strongly repelled from areas coated with fragments containing the cysteine-rich stretch and the EGF-like domains (EGF-L), FN1-2, FN3-5 and FG. Polarization of morphology of hippocampal neurons was exclusively associated with FG, while EGF-L prevented neurite outgrowth altogether. The binding site of the neuronal receptor for tenascin-R, the immunoglobulin superfamily adhesion molecule F3/11, was localized to EGF-L. The combined observations show distinct, but also overlapping functions for the different tenascin-R domains. They further suggest the existence of multiple neuronal tenascin-R receptors which influence the response of neurons to their extracellular matrix environment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CHO Cells / drug effects
  • Cell Adhesion / drug effects
  • Cell Adhesion Molecules, Neuronal / physiology*
  • Cell Polarity
  • Contactins
  • Cricetinae
  • Epidermal Growth Factor / chemistry
  • Epidermal Growth Factor / metabolism
  • Glutathione Transferase / pharmacology
  • Mice
  • Mice, Inbred ICR
  • Neural Cell Adhesion Molecules / physiology*
  • Neurites / drug effects
  • Neurites / physiology
  • Neurons / drug effects*
  • Neurons / physiology*
  • Peptide Fragments / pharmacology*
  • Rats
  • Receptors, Cell Surface / physiology
  • Recombinant Fusion Proteins / pharmacology
  • Recombinant Proteins
  • Tenascin / chemistry
  • Tenascin / metabolism
  • Tenascin / pharmacology*
  • Transfection

Substances

  • Cell Adhesion Molecules, Neuronal
  • Contactins
  • Neural Cell Adhesion Molecules
  • Peptide Fragments
  • Receptors, Cell Surface
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Tenascin
  • tenascin R
  • Epidermal Growth Factor
  • Glutathione Transferase