Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments

Cell. 1989 Oct 20;59(2):325-34. doi: 10.1016/0092-8674(89)90294-8.


A structural and functional model of tenascin was elaborated using recombinant parts of three alternatively spliced tenascin variants and anti-tenascin monoclonal antibodies. The fusion proteins were compared with intact tenascin for their functions and by electron microscopy. A strong cell binding site was localized within 104 amino acids. This fragment also contains the epitope of the monoclonal antibody anti-Tn68, which inhibits cell attachment to tenascin and binds near the tips of the six arms of tenascin. In contrast, constructs containing the 13 1/2 EGF-like repeats of tenascin showed an antiadhesive effect. The coexistence of the two contrary signals on the same molecule might be responsible for the versatile features of tenascin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Adhesion
  • Cell Adhesion Molecules, Neuronal / genetics
  • Cell Adhesion Molecules, Neuronal / physiology*
  • Chick Embryo
  • DNA / genetics*
  • Gene Library
  • Information Systems
  • L Cells / cytology
  • Microscopy, Electron
  • Molecular Sequence Data
  • Nerve Tissue Proteins / physiology*
  • Peptide Fragments / metabolism
  • Protein Conformation
  • Recombinant Fusion Proteins / ultrastructure
  • Sequence Homology, Nucleic Acid
  • Skin / metabolism
  • Tenascin


  • Cell Adhesion Molecules, Neuronal
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Recombinant Fusion Proteins
  • Tenascin
  • DNA

Associated data

  • GENBANK/M23121