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Tenascin-C: Its functions as an integrin ligand.
Journal article

Tenascin-C: Its functions as an integrin ligand.

  • Tucker RP Department of Cell Biology and Human Anatomy, University of California at Davis, 1 Shields Avenue, Davis, CA 95616, USA. Electronic address: rptucker@ucdavis.edu.
  • Chiquet-Ehrismann R Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland; Faculty of Science, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland.
  • 2015-06-10
Published in:
  • The international journal of biochemistry & cell biology. - 2015
Extracellular matrix
IDG
Integrin
RGD
Tenascin
Animals
Extracellular Matrix
Humans
Integrins
Ligands
Tenascin
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/202354
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