title: Micromechanical spectroscopy of cartilage proteoglycans: hydration.
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.
authors.affiliation: Laboratoire de Physique des Solides Associé au C.N.R.S., Université Paul Sabatier, Toulouse, France.
authors.forename: A
authors.initials: A
authors.lastname: Lamure
authors.forename: M F
authors.initials: MF
authors.lastname: Harmand
authors.forename: C
authors.initials: C
authors.lastname: Lacabanne
mesh_terms: D000818:Animals; D001672:Biocompatible Materials; D002152:Calorimetry, Differential Scanning; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D008968:Molecular Conformation; D015394:Molecular Structure; D011509:Proteoglycans / Q000032:analysis*; D013057:Spectrum Analysis; D013314:Stress, Mechanical; D014867:Water / Q000032:analysis
chemical_list: D001672:Biocompatible Materials; D011509:Proteoglycans; D014867:Water