A transmission electron microscope study using vitrified ice sections of predentin: structural changes in the dentin collagenous matrix prior to mineralization.
The assembly of the collagenous organic matrix prior to mineralization is a key step in the formation of bones and teeth. This process was studied in the predentin of continuously forming rat incisors, using unstained vitrified ice sections examined in the transmission electron microscope. Progressing from the odontoblast surface to the mineralization front, the collagen fibrils thicken to ultimately form a dense network, and their repeat D-spacings and banding patterns vary. Using immunolocalization, the most abundant noncollagenous protein in dentin, phosphophoryn, was mapped to the boundaries between the gap and overlap zones along the fibrils nearest the mineralization front. It thus appears that the premineralized collagen matrix undergoes dynamic changes in its structure. These may be mediated by the addition and interaction with the highly anionic noncollagenous proteins associated with collagen. These changes presumably create a collagenous framework that is able to mineralize.
Department of Structural Biology, Weizmann Institute of Science, Rehovot, 76100, Israel
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Beniash
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Traub
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Veis
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Weiner
D000818:Animals; D003094:Collagen / Q000648:ultrastructure; D015925:Cryopreservation / Q000379:methods*; D003804:Dentin / Q000737:chemistry / Q000648:ultrastructure*; D003810:Dentinogenesis; D005109:Extracellular Matrix / Q000648:ultrastructure; D005629:Frozen Sections; D007180:Incisor / Q000166:cytology; D008854:Microscopy, Electron / Q000379:methods; D008903:Minerals / Q000378:metabolism; D009804:Odontoblasts / Q000648:ultrastructure; D010750:Phosphoproteins / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar
D008903:Minerals; D010750:Phosphoproteins; C017630:phosphophoryn; D003094:Collagen