Department of Biomedical Engineering, University of Utah, Salt Lake City, UT, USA; Scientific Computing and Imaging Institute, University of Utah, Salt Lake City, UT, USA.
Department of Biomedical Engineering, University of Utah, Salt Lake City, UT, USA; Scientific Computing and Imaging Institute, University of Utah, Salt Lake City, UT, USA; Department of Orthopaedics, University of Utah, Salt Lake City, UT, USA; School of Computing, University of Utah, Salt Lake City, UT, USA.
Acta Biomater. 2021 Oct 15;134:435-442. doi: 10.1016/j.actbio.2021.07.045. Epub 2021 Jul 24.
Musculoskeletal soft connective tissues are commonly injured due to repetitive use, but the evolution of mechanical damage to the tissue structure during repeated loading is poorly understood. We investigated the strain-rate dependence of mechanical denaturation of collagen as a form of structural microdamage accumulation during creep fatigue loading of rat tail tendon fascicles. We cycled tendons at three strain rates to the same maximum stress relative to their rate-dependent tensile strength. Collagen denaturation at distinct points during the fatigue process was measured by fluorescence quantification of collagen hybridizing peptide binding. The amount of collagen denaturation was significantly correlated with fascicle creep strain, independent of the cyclic strain rate, supporting our hypothesis that tissue level creep is caused by collagen triple-helix unfolding. Samples that were loaded faster experienced more creep strain and denaturation as a function of the number of loading cycles relative to failure. Although this increased damage capacity at faster rates may serve as a protective measure during high-rate loading events, it may also predispose these tissues to subsequent injury and indicate a mechanism of overuse injury development. These results build on evidence that molecular-level collagen denaturation is the fundamental mechanism of structural damage to tendons during tensile loading. STATEMENT OF SIGNIFICANCE: This study is the first to investigate the accumulation of denatured collagen in tendons throughout fatigue loading when the maximum stress is scaled with the applied strain rate. The amount of denatured collagen was correlated with creep strain, independent of strain rate, but samples that were cycled faster withstood greater amounts of denaturation before failure. Differential accumulation of collagen damage between fast and slow repetitive loading has relevance toward understanding the prevalence of overuse musculoskeletal injuries following sudden changes in activity level. Since collagen is a ubiquitous biological structural component, the basic patterns and mechanisms of loading-induced collagen damage in connective tissues are relevant for understanding injury and disease in other tissues, including those from the cardiovascular and pulmonary systems.
肌肉骨骼的软连接组织通常会因重复使用而受伤,但对组织结构在重复加载下机械损伤的演变知之甚少。我们研究了胶原蛋白机械变性在大鼠尾腱束蠕变疲劳加载过程中的结构微损伤积累中的应变率依赖性。我们以相对于其应变率依赖性拉伸强度相同的最大应力在三种应变速率下循环肌腱。通过荧光定量胶原蛋白杂交肽结合来测量疲劳过程中不同时间点的胶原蛋白变性。胶原蛋白变性的量与束状蠕变应变显着相关,与循环应变速率无关,支持我们的假设,即组织水平的蠕变是由胶原蛋白三螺旋展开引起的。与失效相比,与加载循环数相关的快速加载的样品具有更多的蠕变应变和变性。虽然这种在较快速率下增加的损伤能力可能在高速加载事件中作为一种保护措施,但它也可能使这些组织容易受到随后的损伤,并表明过度使用损伤发展的机制。这些结果建立在证据基础上,即分子水平的胶原蛋白变性是在拉伸加载过程中肌腱结构损伤的基本机制。
本研究首次在最大应力与施加应变率相匹配的情况下,研究了在疲劳加载过程中整个肌腱中变性胶原蛋白的积累。变性胶原蛋白的量与蠕变应变相关,与应变速率无关,但循环速度较快的样品在失效前承受了更大的变性量。快速和缓慢重复加载之间胶原蛋白损伤的差异积累与理解活动水平突然变化后过度使用肌肉骨骼损伤的普遍性有关。由于胶原蛋白是一种普遍存在的生物结构成分,因此在连接组织中,负载诱导的胶原蛋白损伤的基本模式和机制与理解包括心血管和肺部系统在内的其他组织的损伤和疾病有关。