Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis.
Tenascin-X is an extracellular matrix protein whose absence leads to an Ehlers-Danlos Syndrome in humans, mainly characterised by connective tissue defects including the disorganisation of fibrillar networks, a reduced collagen deposition, and modifications in the mechanical properties of dense tissues. Here we tested the effect of tenascin-X on in vitro collagen fibril formation. We observed that the main parameters of fibrillogenesis were unchanged, and that the diameter of fibrils was not significantly different when they were formed in the presence of tenascin-X. Interestingly, mechanical analysis of collagen gels showed an increased compressive resistance of the gels containing tenascin-X, indicating that this protein might be directly involved in determining the mechanical properties of collagen-rich tissues in vivo.
Margaron
Yoran
Y
Institut de Biologie et Chimie des Protéines, IFR 128 Biosciences Lyon-Gerland, CNRS UMR 5086, Université de Lyon, 7 passage du Vercors, F-69367 Lyon Cedex 07, France.
Bostan
Luciana
L
Exposito
Jean-Yves
JY
Malbouyres
Maryline
M
Trunfio-Sfarghiu
Ana-Maria
AM
Berthier
Yves
Y
Lethias
Claire
C
D000818:Animals; D055592:Biophysical Phenomena; D002417:Cattle; D003094:Collagen / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D008855:Microscopy, Electron, Scanning; D051381:Rats; D019063:Tenascin / Q000502:physiology*
D019063:Tenascin; C081865:tenascin X; D003094:Collagen