The influence of link protein stabilization on the viscometric properties of proteoglycan aggregate solutions.
The dynamic, steady-shear and transient shear flow properties of precisely prepared link-stable (s0 136, 66% aggregate) and link-free (s0 93, 59% aggregate) proteoglycan aggregate solutions at concentrations ranging from 10 to 50 mg/ml were determined using a cone-on-plate viscometer in a mechanical spectrometer. All proteoglycan solutions tested possessed: (1) linear viscoelastic properties - as measured by the dynamic complex modulus under small amplitude steady oscillatory conditions (1 less than or equal to omega less than or equal to 100 rad/s) - and (2) nonlinear shear-rate dependent apparent viscosities and primary normal stress difference under steady shearing conditions (0.25 less than or equal to gamma less than or equal to 250 s-1). Our transient flow data show that all proteoglycan aggregate solutions exhibited transient stress overshoot effects in shear stress and normal stress. From these steady and transient flow data, we conclude that link protein stabilized aggregates have significant effects on their dynamic and steady-shear properties as well as transient flow properties. The transient stress overshoot data provide a measure of the energy per unit volume of fluid required to overcome the proteoglycan networks in solution from a resting state. Thus we found that link-stable aggregates form much stronger networks than link-free aggregates. This is corroborated by the fact that link-stable aggregates form more elastic (lower than delta) and stiffer (higher [G*]) networks than link-free aggregates. The complete spectrum of viscometric flow data is entirely compatible with the proposed role of link protein in adding structural stability to the proteoglycan-hyaluronate bond. In cartilage, the enhanced strength of the networks formed by link-stable aggregates may play an important role in determining the material properties of the tissue and thereby contribute to the functional capacity of cartilage in diarthrodial joints.
Mow
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Orthopaedic Research Laboratory, Columbia University, New York 10032.
Zhu
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W
Lai
W M
WM
Hardingham
T E
TE
Hughes
C
C
Muir
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H
D000818:Animals; D002358:Cartilage, Articular; D004548:Elasticity; D016326:Extracellular Matrix Proteins; D046911:Macromolecular Substances; D011506:Proteins / Q000378:metabolism / Q000502:physiology; D011509:Proteoglycans / Q000502:physiology; D012212:Rheology; D012996:Solutions; D013552:Swine; D014783:Viscosity; D000099249:Proteoglycan Link Protein
D016326:Extracellular Matrix Proteins; D046911:Macromolecular Substances; D011506:Proteins; D011509:Proteoglycans; D012996:Solutions; D000099249:Proteoglycan Link Protein