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Published in: Archives of Dermatological Research 8/2007

01-01-2007 | Original Paper

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

Authors: David Egging, Franka van den Berkmortel, Glen Taylor, Jim Bristow, Joost Schalkwijk

Published in: Archives of Dermatological Research | Issue 8/2007

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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.
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Metadata
Title
Interactions of human tenascin-X domains with dermal extracellular matrix molecules
Authors
David Egging
Franka van den Berkmortel
Glen Taylor
Jim Bristow
Joost Schalkwijk
Publication date
01-01-2007
Publisher
Springer-Verlag
Published in
Archives of Dermatological Research / Issue 8/2007
Print ISSN: 0340-3696
Electronic ISSN: 1432-069X
DOI
https://doi.org/10.1007/s00403-006-0706-9

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