4.5 Article

The dynamics of collagen uncrimping and lateral contraction in tendon and the effect of ionic concentration

Journal

JOURNAL OF BIOMECHANICS
Volume 46, Issue 13, Pages 2242-2249

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.jbiomech.2013.06.029

Keywords

Tendon; Crimp; Fluid flow; Ionic concentration; Viscoelasticity; Poroelasticity

Funding

  1. NIH [R01 AR055543S1]
  2. NSF
  3. University of Pennsylvania Center for Musculoskeletal Disorders [NIH P30 AR050950]

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Under tensile loading, tendon undergoes a number of unique structural changes that govern its mechanical response. For example, stretching a tendon is known to induce both the progressive uncrimping of wavy collagen fibrils and extensive lateral contraction mediated by fluid flow out of the tissue. However, it is not known whether these processes are interdependent. Moreover, the rate-dependence of collagen uncrimping and its contribution to tendon's viscoelastic mechanical properties are unknown. Therefore, the objective of this study was to (a) develop a methodology allowing for simultaneous measurement of crimp, stress, axial strain and lateral contraction in tendon under dynamic loading; (b) determine the interdependence of collagen uncrimping and lateral contraction by testing tendons in different swelling conditions; and (c) assess how the process of collagen uncrimping depends on loading rate. Murine flexor carpi ulnaris (FCU) tendons in varying ionic environments were dynamically stretched to a set strain level and imaged through a plane polariscope with the polarizer and analyzer at a fixed angle. Analysis of the resulting images allowed for direct measurement of the crimp frequency and indirect measurement of the tendon thickness. Our findings demonstrate that collagen uncrimping and lateral contraction can occur independently and interstitial fluid impacts tendon mechanics directly. Furthermore, tensile stress, transverse contraction and degree of collagen uncrimping were all rate-dependent, suggesting that collagen uncrimping plays a role in tendon's dynamic mechanical response. This study is the first to characterize the time-dependence of collagen uncrimping in tendon, and establishes structure-function relationships for healthy tendons that can be used to better understand and assess changes in tendon mechanics after disease or injury. (C) 2013 Elsevier Ltd. All rights reserved.

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