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Micromechanical spectroscopy of cartilage proteoglycans: hydration
A Lamure1, M F Harmand, C Lacabanne
1Laboratoire de Physique des Solides Associé au C.N.R.S., Université Paul Sabatier, Toulouse, France.
Abstract:
Proteoglycan subunits extracted from calf cartilage have been studied with a high resolving power mechanical spectroscopy: the Thermostimulated Creep (TSC). The influence of hydration on TSC spectra shows the existence of two types of bound water: the weakly bound water increases the inertia of proteoglycan and stiffens their structure; the strongly bound water is responsible to a compensation law indicating the existence of a resonance phenomenon at the physiological temperature. Because of the looseness of bonds in weakly bound water, an increase of the local pressure may induce, in vivo, a release of water in tissues. This hypothesis explains perfectly the role of a water pump of proteoglycans in cartilage.