Loading…

Study of extracellular matrix in vocal fold biomechanics using a two-phase model

The extracellular matrix (ECM) of the vocal fold tissue consists primarily of fibrous and interstitial proteins. The purpose of this study was to investigate the effects of selective enzymatic digestion of two ECM proteins, namely elastin and versican, on the elasticity of rabbit vocal fold tissue....

Full description

Saved in:
Bibliographic Details
Published in:Biomechanics and modeling in mechanobiology 2015-01, Vol.14 (1), p.49-57
Main Authors: Miri, Amir K., Li, Nicole Y. K., Avazmohammadi, Reza, Thibeault, Susan L., Mongrain, Rosaire, Mongeau, Luc
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The extracellular matrix (ECM) of the vocal fold tissue consists primarily of fibrous and interstitial proteins. The purpose of this study was to investigate the effects of selective enzymatic digestion of two ECM proteins, namely elastin and versican, on the elasticity of rabbit vocal fold tissue. Quasi-static, sinusoidal, uniaxial tensile tests were performed. The data were analyzed within the framework of a model of the ECM as a two-phase composite material consisting of collagen fibrils as the reinforcing fibers and noncollagenous ECM proteins as the matrix. To validate the two-phase model, the regression parameters for the fibers’ volume fraction and shear modulus in a different animal model were compared with corresponding published data. The proposed model was then used to analyze rabbit vocal fold tissues. The mean value and the standard deviation of the fiber volume fraction were found to be 8.49 ± 3.75 % for the control samples ( n  = 4), 0.59 ± 1.13 % after elastin removal ( n  = 4), and 8.22 ± 1.06 % after versican removal ( n  = 4). The results suggest that elastin removal may lead to a reduction in tissue stiffness, through counteracting the reinforcement of collagen fibrils.
ISSN:1617-7959
1617-7940
DOI:10.1007/s10237-014-0585-5