4.5 Article

Contribution of glycosaminoglycans to viscoelastic tensile behavior of human ligament

期刊

JOURNAL OF APPLIED PHYSIOLOGY
卷 106, 期 2, 页码 423-431

出版社

AMER PHYSIOLOGICAL SOC
DOI: 10.1152/japplphysiol.90748.2008

关键词

decorin; dermatan sulfate; material properties; tendon; polyethylene glycol

资金

  1. National Institute of Arthritis and Musculoskeletal and Skin Diseases [AR-047369]

向作者/读者索取更多资源

Lujan TJ, Underwood CJ, Jacobs NT, Weiss JA. Contribution of glycosaminoglycans to viscoelastic tensile behavior of human ligament. J Appl Physiol 106: 423-431, 2009. First published December 12, 2008; doi: 10.1152/japplphysiol.90748.2008.-The viscoelastic properties of human ligament potentially guard against structural failure, yet the microstructural origins of these transient behaviors are unknown. Glycosaminoglycans (GAGs) are widely suspected to affect ligament viscoelasticity by forming molecular bridges between neighboring collagen fibrils. This study investigated whether GAGs directly affect viscoelastic material behavior in human medial collateral ligament (MCL) by using nondestructive tensile tests before and after degradation of GAGs with chondroitinase ABC (ChABC). Control and ChABC treatment (83% GAG removal) produced similar alterations to ligament viscoelasticity. This finding was consistent at different levels of collagen fiber stretch and tissue hydration. On average, stress relaxation increased after incubation by 2.2% (control) and 2.1% (ChABC), dynamic modulus increased after incubation by 3.6% (control) and 3.8% (ChABC), and phase shift increased after incubation by 8.5% (control) and 8.4% (ChABC). The changes in viscoelastic behavior after treatment were significantly more pronounced at lower clamp- to- clamp strain levels. A 10% difference in the water content of tested specimens had minor influence on ligament viscoelastic properties. The major finding of this study is that mechanical interactions between collagen fibrils and GAGs are unrelated to tissue- level viscoelastic mechanics in mature human MCL. These findings narrow the possible number of extracellular matrix molecules that have a direct contribution to ligament viscoelasticity.

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