Relation of mineralization defects in collagen matrices to noncollagenous protein components. Identification of a molecular defect in dentinogenesis imperfecta.
Hydroxyapatite crystal deposition and stabilization within the collagen matrix of bone and dentin have been linked to the presence of noncollagenous proteins (NCP). Dentinogenesis imperfecta (DI), a genetic disorder of dentin mineralization, is being studied as a model for the analysis of mineralization mechanisms. A comparative study of the NCP in normal human dentin and dentinogenesis imperfecta Type II (hereditary opalescent dentin) dentin has been performed. The proteins of each tissue were extracted and separated using a variety of techniques. The calcium-binding, highly phosphorylated protein phosphophoryn was one of the principal NCP in normal human teeth dentin, whereas there was no evidence for the presence of such a component in the DI teeth. These data imply that dentin phosphophoryn may be related in function to the mineralization process. A similar calcium-binding protein defect should be sought in the various types of osteogenesis imperfecta.
D000328:Adult; D001857:Bone Matrix / Q000032:analysis*; D002848:Chromatography, DEAE-Cellulose; D003094:Collagen / Q000032:analysis; D003811:Dentinogenesis Imperfecta / Q000378:metabolism*; D004586:Electrophoresis; D005260:Female; D006801:Humans; D008903:Minerals / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis*
D008903:Minerals; D010750:Phosphoproteins; C017630:phosphophoryn; D003094:Collagen