Volume 45, Issue 2 pp. 108-116

The role of collagen in the declining mechanical properties of aging human cortical bone

P. Zioupos

Corresponding Author

P. Zioupos

Department of Materials and Medical Sciences, Cranfield University, RMCS Shrivenham, SN6 8LA, United Kingdom

Department of Materials and Medical Sciences, Cranfield University, RMCS Shrivenham, SN6 8LA, United KingdomSearch for more papers by this author
J. D. Currey

J. D. Currey

Department of Biology, University of York, P.O. Box 373, York YO1 5YW, United Kingdom

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A. J. Hamer

A. J. Hamer

Northern General Hospital NHS Trust, Herries Rd., Sheffield S5 7AU, United Kingdom

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Parts of this work were presented at the 44th Annual Meeting of the Orthopaedic Research Society in New Orleans, Louisiana, March 16–19, 1998.

Abstract

The importance of the mechanical role of collagen in bone is becoming increasingly more clear as evidence mounts on the detrimental effects of altered collagen on the mechanical properties of bone. We previously examined a set of mechanical properties (material stiffness, strength, and toughness) of human femoral bone (ages 35–92) and found that a gradual deterioration in these properties occurs with age. The present study examines the collagen of the same specimens and relates the collagen properties to the mechanical ones. In the collagen we measured the concentration of stable mature crosslinks, the shrinkage temperature, and the rate of contraction during isometric heating. The changes in the concentration of mature (pyridinium and deoxypyridinium) crosslinks showed no clear relationship to age nor did they correlate with the mechanical properties. The shrinkage temperature declined with age and correlated with a bone's toughness. The maximum rate of contraction was strongly correlated with three different measures of tissue toughness, but much less to stiffness and strength. Our results reinforce speculation regarding the toughening role of collagen in bone mechanics and suggest that the fragility of aging bone may be related to collagen changes. © 1999 John Wiley & Sons, Inc. J Biomed Mater Res, 45, 108–116, 1999.

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