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Archives of Dermatological Research

, Volume 298, Issue 8, pp 389–396 | Cite as

Interactions of human tenascin-X domains with dermal extracellular matrix molecules

  • David Egging
  • Franka van den Berkmortel
  • Glen Taylor
  • Jim Bristow
  • Joost Schalkwijk
Original Paper

Abstract

Tenascin-X (TNX) is a large 450 kDa extracellular matrix protein expressed in a variety of tissues including skin, joints and blood vessels. Deficiency of TNX causes a recessive form of Ehlers–Danlos syndrome characterized by joint hypermobility, skin fragility and hyperextensible skin. Skin of TNX deficient patients shows abnormal elastic fibers and reduced collagen deposition. The mechanism by which TNX deficiency leads to connective tissue alterations is unknown. Here we report that C-terminal domains of human TNX bind to major dermal fibrillar collagens and tropoelastin. We have mapped these interactions to the fibronectin type III repeat 29 (FNIII29) and the C-terminal fibrinogen domain (FbgX) of TNX. In addition we found that FNIII29 of TNX accelerates collagen fibrillogenesis in vitro. We hypothesize that TNX contributes to matrix stability and is possibly involved in collagen fibril formation.

Keywords

Tenascin-X Collagen Elastin Fibrillogenesis Ehlers–Danlos syndrome 

Notes

Acknowledgments

The authors are grateful to Dr P. Handford, Dr N. Grebenchtchikov and Dr R. Mecham for providing biological reagents used in this study.

Supplementary material

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Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • David Egging
    • 1
  • Franka van den Berkmortel
    • 1
  • Glen Taylor
    • 2
  • Jim Bristow
    • 2
    • 3
  • Joost Schalkwijk
    • 1
  1. 1.Department of Dermatology, Nijmegen Centre for Molecular Life SciencesRadboud University Nijmegen Medical CentreNijmegenThe Netherlands
  2. 2.Department of PediatricsUniversity of CaliforniaSan FranciscoUSA
  3. 3.Department of Genome SciencesLawrence Berkeley National LaboratoryBerkeleyUSA

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