Anatomical heterogeneity of tendon: Fascicular and interfascicular tendon compartments have distinct proteomic composition.
Anatomical heterogeneity of tendon: Fascicular and interfascicular tendon compartments have distinct proteomic composition.
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DOI：
10.1038/srep20455
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发表时间：
2016-02-04
影响因子：
4.6
通讯作者：
Clegg PD
中科院分区：
文献类型：
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作者：
Thorpe CT;Peffers MJ;Simpson D;Halliwell E;Screen HR;Clegg PD
肌腱是一种简单排列的纤维复合材料，由富含胶原蛋白的纤维束组成，周围是较软的纤维束间基质（IFM）。这些材料相之间的组成和相互作用是确保组织力学满足功能要求的基础。然而，IFM的定义很差，因此肌腱的结构-功能关系不完全了解。我们假设，IFM有一个更复杂的蛋白质组，与更快的营业额比束状矩阵（FM）。使用激光捕获显微切割和质谱分析，我们表明，IFM包含更多的蛋白质，许多蛋白质显示差异丰富的基质相之间。IFM含有更多的蛋白质片段（新肽），表明该隔室中的基质降解更大，这可能有助于保持健康的肌腱结构。蛋白质丰度并没有随着年龄的增长而改变，但新肽的数量在老年IFM下降，表明营业额下降，这可能有助于与年龄相关的肌腱损伤。这些数据提供了重要的见解，肌腱成分和营业额的差异如何有助于肌腱的结构-功能关系和老化的影响。
Tendon is a simple aligned fibre composite, consisting of collagen-rich fascicles surrounded by a softer interfascicular matrix (IFM). The composition and interactions between these material phases are fundamental in ensuring tissue mechanics meet functional requirements. However the IFM is poorly defined, therefore tendon structure-function relationships are incompletely understood. We hypothesised that the IFM has a more complex proteome, with faster turnover than the fascicular matrix (FM). Using laser-capture microdissection and mass spectrometry, we demonstrate that the IFM contains more proteins, and that many proteins show differential abundance between matrix phases. The IFM contained more protein fragments (neopeptides), indicating greater matrix degradation in this compartment, which may act to maintain healthy tendon structure. Protein abundance did not alter with ageing, but neopeptide numbers decreased in the aged IFM, indicating decreased turnover which may contribute to age-related tendon injury. These data provide important insights into how differences in tendon composition and turnover contribute to tendon structure-function relationships and the effects of ageing.