title: Elastin governs the mechanical response of medial collateral ligament under shear and transverse tensile loading.
abstract: Elastin is a highly extensible structural protein network that provides near-elastic resistance to deformation in biological tissues. In ligament, elastin is localized between and along the collagen fibers and fascicles. When ligament is stretched along the primary collagen axis, elastin supports a relatively high percentage of load. We hypothesized that elastin may also provide significant load support under elongation transverse to the primary collagen axis and shear along the collagen axis. Quasi-static transverse tensile and shear material tests were performed to quantify the mechanical contributions of elastin during deformation of porcine medial collateral ligament. Dose response studies were conducted to determine the level of elastase enzymatic degradation required to produce a maximal change in the mechanical response. Maximal changes in peak stress occurred after 3h of treatment with 2U/ml porcine pancreatic elastase. Elastin degradation resulted in a 60-70% reduction in peak stress and a 2-3× reduction in modulus for both test protocols. These results demonstrate that elastin provides significant resistance to elongation transverse to the collagen axis and shear along the collagen axis while only constituting 4% of the tissue dry weight. The magnitudes of the elastin contribution to peak transverse and shear stress were approximately 0.03 MPa, as compared to 2 MPa for axial tensile tests, suggesting that elastin provides a highly anisotropic contribution to the mechanical response of ligament and is the dominant structural protein resisting transverse and shear deformation of the tissue.
authors.affiliation: Department of Bioengineering, and Scientific Computing and Imaging Institute, University of Utah, United States; Department of Orthopaedics, University of Utah, United States.
authors.forename: Heath B
authors.initials: HB
authors.lastname: Henninger
authors.affiliation: Department of Bioengineering, and Scientific Computing and Imaging Institute, University of Utah, United States.
authors.forename: William R
authors.initials: WR
authors.lastname: Valdez
authors.affiliation: Department of Bioengineering, and Scientific Computing and Imaging Institute, University of Utah, United States.
authors.forename: Sara A
authors.initials: SA
authors.lastname: Scott
authors.affiliation: Department of Bioengineering, and Scientific Computing and Imaging Institute, University of Utah, United States; Department of Orthopaedics, University of Utah, United States. Electronic address: jeff.weiss@utah.edu.
authors.forename: Jeffrey A
authors.initials: JA
authors.lastname: Weiss
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena / Q000187:drug effects; D003094:Collagen / Q000378:metabolism; D004549:Elastin / Q000737:chemistry / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism; D017888:Medial Collateral Ligament, Knee / Q000187:drug effects / Q000502:physiology*; D010196:Pancreatic Elastase / Q000494:pharmacology; D034421:Sus scrofa; D013718:Tensile Strength / Q000187:drug effects; D016474:Weight-Bearing / Q000502:physiology
chemical_list: D006025:Glycosaminoglycans; D003094:Collagen; D004549:Elastin; D010196:Pancreatic Elastase
keywords: Elastase; Elastin; Ligament; Shear; Transverse tensile