Effect of dermatan sulfate glycosaminoglycans on the quasi‐static material properties of the human medial collateral ligament
Open Access
- 7 March 2007
- journal article
- research article
- Published by Wiley in Journal of Orthopaedic Research
- Vol. 25 (7) , 894-903
Abstract
The glycosaminoglycan of decorin, dermatan sulfate (DS), has been suggested to contribute to the mechanical properties of soft connective tissues such as ligaments and tendons. This study investigated the mechanical function of DS in human medial collateral ligaments (MCL) using nondestructive shear and tensile material tests performed before and after targeted removal of DS with chondroitinase B (ChB). The quasi‐static elastic material properties of human MCL were unchanged after DS removal. At peak deformation, tensile and shear stresses in ChB treated tissue were within 0.5% (p > 0.70) and 2.0% (p > 0.30) of pre‐treatment values, respectively. From pre‐ to post‐ChB treatment under tensile loading, the tensile tangent modulus went from 242 ± 64 to 233 ± 57 MPa (p = 0.44), and tissue strain at peak deformation went from 4.3 ± 0.3% to 4.4 ± 0.3% (p = 0.54). Tissue hysteresis was unaffected by DS removal for both tensile and shear loading. Biochemical analysis confirmed that 90% of DS was removed by ChB treatment when compared to control samples, and transmission electron microscopy (TEM) imaging further verified the degradation of DS by showing an 88% reduction (p < .001) of sulfated glycosaminoglycans in ChB treated tissue. These results demonstrate that DS in mature knee MCL tissue does not resist tensile or shear deformation under quasi‐static loading conditions, challenging the theory that decorin proteoglycans contribute to the elastic material behavior of ligament. © 2007 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 25:894–903, 2007Keywords
This publication has 55 references indexed in Scilit:
- Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon developmentJournal of Cellular Biochemistry, 2006
- Direct measurement of the rupture force of single pair of decorin interactionsBiochemical and Biophysical Research Communications, 2005
- Proteoglycans and catabolic products of proteoglycans present in ligamentBiochemical Journal, 2005
- Structural Aspects of the Extracellular Matrix of the Tendon: An Atomic Force and Scanning Electron Microscopy Study.Archives of Histology and Cytology, 2002
- The effect of NKISK on tendon in an in vivo modelJournal of Orthopaedic Research, 2001
- The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissueJournal of Orthopaedic Research, 2000
- Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon maturesDevelopmental Dynamics, 1997
- The Production and Purification of Functional Decorin in a Baculovirus SystemBiochemical and Biophysical Research Communications, 1997
- An Estimate of the Mean Length of Collagen Fibrils in Rat Tail-Tendon as a Function of ageConnective Tissue Research, 1989
- The Effect of a Lathyritic Diet on the Sensitivity of Tendon to Strain RateJournal of Biomechanical Engineering, 1985