Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Tooth Calcification”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 505 records · Page 28Linked to original sources
PubMedDate not supplied

Abnormal pulp calcification in primary molars after fluoride supplementation.

Forty-five caries-free primary molars from children with continuous fluoride supplementation (n = 28) after birth and from children without fluoride prophylaxis (n = 17) were investigated by light microscopy. The following results were obtained: The prophylaxis group evidenced a special form of calcification consisting of fibrodentin-like hard tissue developing intramurally in the dentin wall especially at the pulp floor and spreading irregularily into the pulp cavity by displacing the degenerating pulp tissue (n = 24). These teeth were ankylosed in the bi- and trifurcation area as well as inside the roots. This kind of hard tissue was not observed in the teeth from untreated children. Only 5 children had greater calcifications attached at the pulp wall. Nevertheless, this difference was statistically significant (p = 0.001) and indicates a relationship between fluoride prophylaxis, the special form of pulp calcification and tooth ankylosis.

Adolescent↗
PubMed1993

Mineral-matrix interactions in bone and dentin.

The bone, dentin, and cementum of the mature individual are comprised from a dense collagenous fiber network into which the carbonate-apatite mineral phase is deposited. It is hypothesized that a set of collagen-interactive acidic phosphoproteins are secreted by the osteoblasts, odontoblasts, and cementoblasts into the preformed collagenous matrix. These proteins then interact specifically with the collagen and nucleate apatite formation on and within the fibrils. These phosphoproteins may also regulate the morphology, rate of growth, and stability of the mineral phase crystals. The acidic matrix phosphoproteins may thus be considered as the crucial regulators of mineralization and tissue stability. In the dentin system, these regulatory proteins are synthesized, posttranslationally modified, and secreted in vesicles different from the collagen secretory vesicles. Mineralization occurs as the regulatory proteins are deposited on the preformed fibrils. This model requires testing in the bone system. In dentin, in the absence of tissue turnover, the resident phosphoproteins are degraded in situ over time, perhaps changing the properties of the tissue. Regulation of synthesis, secretory pathways and retention of integrity within the matrix are thus important areas for further investigation.

Amino Acid Sequence↗
PubMed1975

Mineralization of dentin, bone and tendon in vitro.

Bovin dentin, bone and tendon slices, and rat bone, readily mineralize to variable degrees after demineralization by (EDTA) at pH 7.4, but they fail to mineralize after dimeralzation with acetic acid (HAc) at pH3.0. The demineralized dentin, but neither bone nor tendon, contained organically bound phosphate. The EDTA-demineralized dentin contained less phosphate than HAc-demineralized dentin. HAc-demineralized rat dentin contained high levels of phosphate. Since the EDTA- and HAc-demineralized rat dentin contained widely different levels of phosphate, yet both mineralized, it was concluded that phosphoprotein had little effect on nucleation. The reason why HAc-demineralized tissue other than rat dentin failed to nucleate and mineralize was not clarified.

Acetates↗
PubMed1995

Ultrastructural organic-inorganic relationships in calcified tissues: cartilage and bone vs. enamel.

Close organic-inorganic relationships exist in all calcified tissues, the inorganic substance being linked to crystal ghosts (CGs). These are organic, crystal-like structures present in areas of initial calcification. In cartilage and bone, they form aggregates with the same morphology and distribution as the calcification nodules; in enamel, they consist of long filament- and ribbon-like structures, having the same arrangement as untreated crystals. CGs of cartilage and bone are acidic structures with histochemical properties of proteoglycans; CGs of enamel probably correspond to enamelins. The close morphologic similarity between CGs and crystals suggests that the former have a role in the formation of the latter.

Bone and Bones↗