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Proteoglycan degradation mimics static compression by altering the natural gradients in fibrillar organisation in cartilage

机译:通过改变软骨中的纤维状组织中的自然梯度来模拟蛋白质聚糖降解模拟静态压缩

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摘要

Structural and associated biomechanical gradients within biological tissues are important for tissue functionality and preventing damaging interfacial stress concentrations. Articular cartilage possesses an inhomogeneous structure throughout its thickness, driving the associated variation in the biomechanical strain profile within the tissue under physiological compressive loading. However, little is known experimentally about the nanostructural mechanical role of the collagen fibrils and how this varies with depth. Utilising a high-brilliance synchrotron X-ray source, we have measured the depth-wise nanostructural parameters of the collagen network in terms of the periodic fibrillar banding (D-period) and associated parameters. We show that there is a depth dependent variation in D-period reflecting the pre-strain and concurrent with changes in the level of intrafibrillar order. Further, prolonged static compression leads to fibrillar changes mirroring those caused by removal of extrafibrillar proteoglycans (as may occur in aging or disease). We suggest that fibrillar D-period is a sensitive indicator of localised changes to the mechanical environment at the nanoscale in soft connective tissues.
机译:生物组织内的结构和相关的生物力学梯度对于组织功能和预防损伤界面应激浓度很重要。关节软骨在其厚度中具有不均匀的结构,在生理压缩载荷下驱动组织内的生物力学应变型的相关变化。然而,很少是通过实验众所周知的胶原型原纤维的纳米结构机械作用以及深度变化的作用。利用高亮度同步旋流X射线源,我们在周期性纤维条带(D周)和相关参数方面测量了胶原网络的深度明智的纳米结构参数。我们表明,D周期的深度依赖性变化,反映了预突变和同时的D间隔,并随着富集程度的变化。此外,延长的静态压缩导致纤维化变化,镜像通过去除预先除去Extrafibrill蛋白多糖(如衰老或疾病可能发生)引起的那些。我们建议Fibrillar D-句点是软结缔组织中纳米级的机械环境的局部变化的敏感指标。

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