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.
Biophys Chem. 2010 Mar;147(1-2):87-91. doi: 10.1016/j.bpc.2009.12.011. Epub 2010 Jan 4.
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.
Tenascin-X 是一种细胞外基质蛋白，其缺失会导致人类出现埃勒斯-当洛斯综合征，主要表现为结缔组织缺陷，包括纤维网络的紊乱、胶原沉积减少以及致密组织力学性能的改变。在这里，我们测试了 tenascin-X 对体外胶原蛋白纤维形成的影响。我们观察到纤维发生的主要参数没有变化，并且当 tenascin-X 存在时形成的纤维直径没有显著差异。有趣的是，对含有 tenascin-X 的胶原蛋白凝胶的力学分析表明其抗压阻力增加，表明该蛋白可能直接参与体内富含胶原蛋白组织力学性能的决定。
