Dentinal proteoglycans demonstrate an increasing order of affinity for hydroxyapatite crystals during the transition of predentine to dentine.

Abstract

The transition from an unmineralized predentine to a mineralized dentine involves a variety of molecular extracellular matrix interactions and protein degradation events. Previous studies have identified that different pools of proteoglycan (PG) species are present within the matrix of the predentine, the transitional phase at the predentine-dentine border, and the mineralized dentine. These PGs alter with respect to the chemical nature of the glycosaminoglycan (GAG) chain and as a result of extracellular processing of the macromolecule in the matrix. This study has examined the hydroxyapatite (HAP) binding affinity of the PGs isolated from these phases and the influence of the attached GAG chains upon their binding characteristics. PGs isolated from the three phases were characterized to contain a mixture of decorin and biglycan, substituted with chondroitin sulfate GAG chain(s). Maximal binding for dentine PGs onto HAP was achieved at 15.60 microg/ml protein and for predentine-dentine interface PGs at 0.125 mg/ml. A significantly increasing gradient of affinity was observed moving toward dentine, with dentine PGs exhibiting 19 times greater binding affinity for HAP than predentine PGs and 7.5 times greater affinity than predentine-dentine interface PGs. Removal of the GAG chains from dentine PGs significantly reduced binding affinity for HAP but did not influence the number of binding sites. The difference in binding ability observed for the different PG pools gives further support for the involvement of these macromolecules in regulating the transition from predentine to dentine and suggests key roles for the GAG chains in the mineralisation process.