The basic mechanism of reinforcement in tendons addresses the transfer of stress, generated by the deforming proteoglycan (PG)-rich matrix, to the collagen fibrils. Regulating this mechanism involves the interactions of PGs on the fibril with those in the surrounding matrix and between PGs on adjacent fibrils. This understanding is key to establishing new insights on the biomechanics of tendon in various research domains. However, the experimental designs in many studies often involved long sample preparation time. To minimise biological degradation the tendons are usually stored by freezing. Here, we have investigated the effects of commonly used frozen storage temperatures on the mechanical properties of tendons from the tail of a @entity19 model (C57BL6 @entity19 ). Fresh (unfrozen) and thawed samples, frozen at temperatures of -20  C and -80  C, respectively, were stretched to @entity397 . Freezing at -20  C revealed no effect on the maximum stress (  ), stiffness (E), the corresponding strain (  ) at    and strain energy densities up to    (u) and from    until complete @entity397 (up). On the other hand, freezing at -80  C led to higher   , E and u;    and up were unaffected. The results implicate changes in the long-range order of radially packed collagen molecules in fibrils, resulting in fibril @entity397 at higher stresses, and changes to the composition of extrafibrillar matrix, resulting in an increase in the interaction energy between fibrils via collagen-bound PGs.

Effects of frozen storage temperature on the elasticity of tendons from a small XXXX model.

@entity19 :: ('10090', 'Species') :: ['murine', 'mouse'] @entity397 :: ('MESH:D012421', 'Disease') :: ['rupture']
@entity19 :: (10090,Species) :: ['murine']
