title: Non-specific interaction of proteoglycans with surfaces and matrices.
abstract: Evidence is presented that reversible non-specific adsorption of proteoglycans (PGs) to surfaces and matrices is an inherent property of the PGs. This adsorption is dependent on the intact PG structure as the glycosaminoglycans (GAGs), which are isolated after papain digestion of the PG show no such non-specific adsorption. The interaction of the PG with surfaces and matrices is also highly dependent on the internal milieu and can be both inhibited and enhanced by such factors as the ionic composition and concentration, pH, detergents and chaotropic reagents such as guanidine hydrochloride (Gdn-HC1). It is suggested that this inherent stickiness of the PGs allows them to function like a reversible fluid adhesant in the connective tissues. This weak binding force thus not only aids in maintaining the integrity of the connective tissues, but its reversible nature may provide for easy movement of other materials through the connective tissue matrix.
authors.affiliation: Department of Medicine, Queen's University, Kingston, Ontario, Canada.
authors.forename: L J
authors.initials: LJ
authors.lastname: Hronowski
authors.forename: T P
authors.initials: TP
authors.lastname: Anastassiades
mesh_terms: D000818:Animals; D002356:Cartilage / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D006146:Guanidines; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011509:Proteoglycans / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D006146:Guanidines; D011509:Proteoglycans