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Table of Contents - September 2010 - Volume 4, Issue 09  

Product quality, human health and well-being

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

K. L. Goha1 c1, Y. Chena2, S. M. Choua3, A. Listrata4, D. Becheta5 and T. J. Wessa6

a1 School of Engineering, Monash University, 46150, Selangor Darul Ehsan, Malaysia

a2 School of Chemical & Biomedical Engineering, Nanyang Technological University, 637459, Singapore

a3 School of Mechanical & Aerospace Engineering, Nanyang Technological University, 639798, Singapore

a4 Growth and Muscle Metabolism Laboratory, Institut National de la Recherche Agronomique, 63122 St Genes-Champanelle, France

a5 Human Nutrition Research Center, Institut National de la Recherche Agronomique, 63122 St Genes-Champanelle, France

a6 School of Optometry & Vision Sciences, Cardiff University, Cardiff, CF24 4LU, UK

Abstract

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 murine model (C57BL6 mouse). Fresh (unfrozen) and thawed samples, frozen at temperatures of −20°C and −80°C, respectively, were stretched to rupture. Freezing at −20°C revealed no effect on the maximum stress (σ), stiffness (E), the corresponding strain (ε) at σ and strain energy densities up to ε (u) and from ε until complete rupture (up). On the other hand, freezing at −80°C led to higher σ, E and u; ε and up were unaffected. The results implicate changes in the long-range order of radially packed collagen molecules in fibrils, resulting in fibril rupture 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.

(Received September 07 2009)

(Accepted February 25 2010)

(Online publication April 26 2010)

Keywords

Correspondence:

c1 E-mail: goh.kheng.lim@eng.monash.edu.my