Tenascin-C: Its functions as an integrin ligand

Richard P Tucker, Ruth Chiquet-Ehrismann

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


This review summarizes the experimental evidence of tenascin-C/integrin interactions, emphasizing the identification of integrin binding sites and the effects of specific interactions on cell behavior. At least four integrins appear to bind to the third fibronectin-type 3 domain of tenascin-C: α9β1, αVβ3, α8β1 and αVβ6. The α9β1 integrin recognizes a highly conserved IDG motif in this domain, while the others recognize an RGD motif. There is also significant evidence that the collagen receptor α2β1 can bind to tenascin-C, but the interacting site is unknown. Tenascin-C interactions with α9β1 and αVβ3 can promote cell proliferation and interactions with αVβ3 can also inhibit apoptosis. Interactions with α7β1 integrin, which may bind to the alternatively spliced domain of tenascin-C, and α9β1 integrin are able to influence the differentiation of mesenchymal stem cells into the neuronal lineage. This illustrates the potential for using our knowledge of tenascins and their integrin receptors in stem cell-based therapies.

Original languageEnglish (US)
Pages (from-to)165-168
Number of pages4
JournalInternational Journal of Biochemistry and Cell Biology
StatePublished - Jun 18 2015


  • Extracellular matrix
  • IDG
  • Integrin
  • RGD
  • Tenascin

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


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