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Calcium‐ and hydroxyapatite‐binding properties of glucuronic acid‐rich and iduronic acid‐rich glycosaminoglycans and proteoglycans
Author(s) -
Embery Graham,
Rees Sarah,
Hall Rachel,
Rose Keith,
Waddington Rachel,
Shellis Peter
Publication year - 1998
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1998.tb02186.x
Subject(s) - iduronic acid , chemistry , glucuronic acid , chondroitin , glycosaminoglycan , proteoglycan , biochemistry , calcium , chondroitin sulphate , polysaccharide , organic chemistry , extracellular matrix
This study describes the interaction of a small chondroitin sulphate proteoglycan and the glycosaminoglycans chondroitin 4‐sulphate, dermatan sulphate and heparan sulphate with hydroxyapatite. All macromolecules possessed a high affinity, with the iduronic acid‐rich dermatan sulphate and heparan sulphate displaying higher adsorption maxima than the glucuronic acid‐rich chondroitin 4‐sulphate. At similar concentrations, dermatan sulphate produced a 30% inhibition of hydroxyapatite‐induced crystal growth, whilst chondroitin 4‐sulphate yielded 50% inhibition. Estimation of the calcium binding capacity of these glycosaminoglycans using equilibrium dialysis indicated that chondroitin 4‐sulphate bound five times more calcium than dermatan sulphate at a calcium concentration similar to that of serum. The data indicate a possible important role for chondroitin 4‐sulphate in dentinogenesis where it is the dominant glycosaminoglycan, since it could act as a capture point for calcium ions during mineralisation, with the leucine‐rich domain of its parent proteoglycan acting as anchor points to type I collagen.