Literature DB >> 20089348

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

Yoran Margaron1, Luciana Bostan, Jean-Yves Exposito, Maryline Malbouyres, Ana-Maria Trunfio-Sfarghiu, Yves Berthier, Claire Lethias.   

Abstract

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. Copyright 2009 Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20089348     DOI: 10.1016/j.bpc.2009.12.011

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


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