Wb. Zhu et al., VISCOELASTIC SHEAR PROPERTIES OF ARTICULAR-CARTILAGE AND THE EFFECTS OF GLYCOSIDASE TREATMENTS, Journal of orthopaedic research, 11(6), 1993, pp. 771-781
The objectives of this study were to determine the viscoelastic shear
properties of articular cartilage and to investigate the effects of th
e alteration of proteoglycan structure on these shear properties. Glyc
osidase treatments (chondroitinase ABC and Streptomyces hyaluronidase)
were used to alter the proteoglycan structure and content of the tiss
ue. The dynamic viscoelastic shear properties of control and treated t
issues were measured and statistically compared. Specifically, cylindr
ical bovine cartilage specimens were subjected to oscillatory shear de
formation of small amplitude (gamma(o) = 0.001 radian) over a physiolo
gical range of frequencies (0.01-20 Hz) and at various compressive str
ains (5,9,12, and 16%). The dynamic complex shear modulus was calculat
ed from the measurements. The experimental results show that the solid
matrix of normal articular cartilage exhibits intrinsic viscoelastic
properties in shear over the range of frequencies tested. These viscoe
lastic shear properties were found to be dependent on compressive stra
ins. Our data also provide significant insights into the structure-fun
ction relationships for articular cartilage. Significant correlations
were found between the material properties (the magnitude of dynamic s
hear modulus, the phase shift angle, and the equilibrium compressive m
odulus), and the biochemical compositions of the cartilage (collagen,
proteoglycan, and water contents). The shear modulus was greatly reduc
ed when the proteoglycans were degraded by either chondroitinase ABC o
r Streptomyces hyaluronidase. The results suggest that the ability of
collagen to resist tension elastically provides the stiffness of the c
artilage matrix in shear and its elastic energy storage capability. Pr
oteoglycans enmeshed in the collagen matrix inflate the collagen netwo
rk and induce a tensile prestress in the collagen fibrils. This intera
ction of the collagen and proteoglycan within the cartilage matrix pro
vides the complex mechanism that allows the tissue to resist shear def
ormation.