No abstract

Tendinopathic tissue has long been characterized by changes to collagen microstructure. However, initial tendon damage from excessive mechanical loading-a hallmark of tendinopathy development-could occur at the nanoscale level of collagen fibrils. Indeed, it is on this scale that tenocytes interact directly with tendon matrix, and excessive collagen fibril damage not visible at the microscale could trigger a degenerative cascade. In this study, we explored whether initiation of tendon damage during cyclic loading occurs via a longitudinal compression-induced buckling mechanism of collagen fibrils leading to nanoscale kinkband development. Two groups of tendons were cyclically loaded to equivalent peak stresses. In each loading cycle, tendons in one group were unloaded to the zero displacement mark, while those in the other group were unloaded to a nominal level of tension, minimizing the potential for fibril buckling. Tendons that were unloaded to the zero displacement mark ruptured significantly sooner during cyclic loading (1,446 ± 737 vs. 4,069 ± 1,129 cycles), indicating that significant fatigue damage is accrued in the low stress, toe region of the load-deformation response. Ultrastructural analysis using scanning electron microscopy of tendons stopped after 1,000 cycles showed that maintaining a nominal tension slowed the accumulation of kinkbands, supporting a longitudinal compression-induced buckling mechanism as the basis for kinkband development. Based on our results, we present a new descriptive model for the initiation of tendon damage during cyclic loading. The so-called Compression of Unrecovered Elongation or CUE Model may provide useful insight into the development of tendinopathy. © 2017 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 36:467-476, 2018.

Previous research has shown that both the mechanics and elongation mechanisms of tendon and ligament vary with strain rate during tensile loading. In this study, we sought to determine if the ultrastructural damage created during tendon rupture also varies with strain rate. A bovine forelimb model was used, allowing two anatomically proximate but physiologically distinct tendons to be studies: the positional common digital extensor tendon, and the energy storing superficial digital flexor tendon. Samples from the two tendon types were ruptured at rates of either 1%/s or 10%/s. Relative to unruptured control samples, changes to collagen fibril structure were assessed using scanning electron microscopy (SEM), and changes to collagen molecule packing were studied using differential scanning calorimetry (DSC). Rupture at 1%/s caused discrete plasticity damage that extended along the length of collagen fibrils in both the extensor and flexor tendons. Consistent with this, DSC showed molecular packing disruption relative to control samples. Both SEM and DSC showed that extensor tendon fibrils sustained more severe damage than the more highly crosslinked flexor tendon fibrils. Increasing strain rate during rupture decreased the level of longitudinal disruption experienced by the collagen fibrils of both tendon types. Disruption to D-banding was no longer seen in the extensor tendon fibrils, and discrete plasticity damage was completely eliminated in the flexor tendon fibrils, indicating a transition to localized point failure. Ultrastructural damage resulting from tendon rupture depends on both strain rate and tendon type. © 2018 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res.

No abstract