Influence of Decorin and Biglycan on Mechanical Properties of Multiple Tendons in Knockout Mice
- 1 February 2005
- journal article
- research article
- Published by ASME International in Journal of Biomechanical Engineering
- Vol. 127 (1) , 181-185
- https://doi.org/10.1115/1.1835363
Abstract
Evaluations of tendon mechanical behavior based on biochemical and structural arrangement have implications for designing tendon specific treatment modalities or replacement strategies. In addition to the well studied type I collagen, other important constituents of tendon are the small proteoglycans (PGs). PGs have been shown to vary in concentration within differently loaded areas of tendon, implicating them in specific tendon function. This study measured the mechanical properties of multiple tendon tissues from normal mice and from mice with knock-outs of the PGs decorin or biglycan. Tail tendon fascicles, patellar tendons (PT), and flexor digitorum longus tendons (FDL), three tissues representing different in vivo loading environments, were characterized from the three groups of mice. It was hypothesized that the absence of decorin or biglycan would have individual effects on each type of tendon tissue. Surprisingly, no change in mechanical properties was observed for the tail tendon fascicles due to the PG knockouts. The loss of decorin affected the PT, causing an increase in modulus and stress relaxation, but had little effect on the FDL. Conversely, the loss of biglycan did not significantly affect the PT, but caused a reduction in both the maximum stress and modulus of the FDL. These results give mechanical support to previous biochemical data that tendons likely are uniquely tailored to their specific location and function. Variances such as those presented here need to be further characterized and taken into account when designing therapies or replacements for any one particular tendon.Keywords
This publication has 51 references indexed in Scilit:
- A Syndrome of Joint Laxity and Impaired Tendon Integrity in Lumican- and Fibromodulin-deficient MiceJournal of Biological Chemistry, 2002
- Phenotypic Effects of Biglycan Deficiency Are Linked to Collagen Fibril Abnormalities, Are Synergized by Decorin Deficiency, and Mimic Ehlers-Danlos-Like Changes in Bone and Other Connective TissuesJournal of Bone and Mineral Research, 2002
- The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissueJournal of Orthopaedic Research, 2000
- Human Cells Unable to Express Decoron Produced Disorganized Extracellular Matrix Lacking “Shape Modules” (Interfibrillar Proteoglycan Bridges)Experimental Cell Research, 1998
- Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical propertiesBiophysical Journal, 1997
- Direct Visualization of Collagen-Bound Proteoglycans by Tapping-Mode Atomic Force MicroscopyJournal of Structural Biology, 1997
- Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin FragilityThe Journal of cell biology, 1997
- Role of decorin on in vitro fibrillogenesis of type I collagen.Glycoconjugate Journal, 1997
- Increased Diameters of Collagen Fibrils Precipitatedin vitroin the Presence of Decorin from Various Connective TissuesConnective Tissue Research, 1997
- Interaction of Biglycan with Type I CollagenJournal of Biological Chemistry, 1995