Tenascin-C induced stimulation of chondrogenesis is dependent on the presence of the C-terminal fibrinogen-like globular domain

FEBS Lett. 2000 Sep 1;480(2-3):189-92. doi: 10.1016/s0014-5793(00)01936-0.


The relationship between structure of tenascin-C (Tn-C), a multi-domain extracellular matrix protein, and its stimulation of chondrogenesis was examined using recombinant Tn-C isoforms (full length or with specific domains deleted) as substrata for undifferentiated chicken mesenchymal cells. Of the Tn-C variants tested, only Tn-C lacking the fibrinogen-like domain or Tn-C comprised solely of fibrinogen-like domains failed to stimulate chondrogenesis. The ability of variants to stimulate chondrogenesis was not dependent on their ability to support adhesion or stimulate proliferation. These results demonstrate that the fibrinogen-like domain of Tn-C is necessary but not sufficient for induction of chondrogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Division
  • Cells, Cultured
  • Chickens
  • Chondrogenesis / physiology*
  • Fibrinogen / genetics
  • Fibrinogen / physiology*
  • Humans
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / physiology
  • Tenascin / genetics
  • Tenascin / physiology*
  • Tumor Cells, Cultured


  • Recombinant Fusion Proteins
  • Tenascin
  • Fibrinogen