Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis

Yoran Margaron , Luciana Bostan , Jean-Yves Exposito , Maryline Malbouyres , Ana-Maria Trunfio-Sfarghiu , Yves Berthier , Claire Lethias

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 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 determinating the mechanical properties of collagen-rich tissues .

Mots clés: extracellular matrix; Ehlers-Danlos Syndrome; tenascin-X; collagen; elastic modulus

Yoran Margaron, Luciana Bostan, Jean-Yves Exposito, Maryline Malbouyres, Ana-Maria Trunfio-Sfarghiu, et al.. Tenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis. Biophysical Chemistry, 2010, 147 (1-2), pp.87. ⟨10.1016/j.bpc.2009.12.011⟩. ⟨hal-00612709⟩