Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin

FEBS Lett. 1996 Jul 8;389(3):304-8. doi: 10.1016/0014-5793(96)00609-6.

Abstract

The structural basis for the interaction between tenascin-C and the neuronal cell adhesion molecule, contactin/F11, was investigated using plasmon surface resonance technology. The binding site on tenascin-C for contactin/F11 is shown to span the two fibronectin type III homology domains 5 and 6. Either domain alone is insufficient for binding. Heparin, heparan sulfate and dermatan sulfate inhibit this interaction through binding to a conserved heparin-binding site on domain 5. In contrast, chondroitin sulfates A and C have no such effect.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Binding Sites
  • Cell Adhesion Molecules, Neuronal*
  • Chick Embryo
  • Contactins
  • Dermatan Sulfate / pharmacology
  • Extracellular Matrix / metabolism
  • Fibronectins / chemistry
  • Fibronectins / metabolism*
  • Glycosaminoglycans / pharmacology
  • Heparin / pharmacology*
  • Heparitin Sulfate / pharmacology
  • Membrane Glycoproteins / metabolism
  • Nerve Tissue Proteins / metabolism*
  • Neural Cell Adhesion Molecules / metabolism*
  • Protein Binding / drug effects
  • Recombinant Fusion Proteins / metabolism
  • Tenascin / chemistry
  • Tenascin / metabolism*

Substances

  • Antibodies, Monoclonal
  • Cell Adhesion Molecules, Neuronal
  • Contactins
  • Fibronectins
  • Glycosaminoglycans
  • Membrane Glycoproteins
  • Nerve Tissue Proteins
  • Neural Cell Adhesion Molecules
  • Recombinant Fusion Proteins
  • Tenascin
  • Dermatan Sulfate
  • Heparin
  • Heparitin Sulfate