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PubMed1998

Pulpal injury: pathology, diagnosis and periodontal reactions.

Diagnosis of pulpal disease can be difficult due to the lack of diagnostic signs and symptoms available to the practitioner. An understanding of the possible underlying pathological processes, combined with an exact assessment of the pain history, and appropriate clinical tests, should aid the practitioner in determining the nature of pulpal inflammation, and differentiating it from dentine sensitivity and cracked teeth. The responses of the pulp to traumatic injury to the periodontal membrane (PDM) require special consideration, particularly with respect to the assessment of pulp vitality, and the determination of cases requiring pulp extirpation in order to avoid inflammatory root resorption. Although the pulp is relatively isolated from the rest of the dentoalveolar complex by a dentine/cementum barrier, it is important to remember that it can communicate with the PDM through apical and lateral foramina, and areas of damaged cementum. Hence, it is a priority to both preserve the integrity of the cemental layer in cases of traumatic injury and periodontal disease, and to prevent the inflammation and resorption associated with periapical lesions by accurate diagnosis of irreversible pulpitis and pulp necrosis, followed by appropriate endodontic debridement procedures.

Cracked Tooth Syndrome↗
PubMed1979

Correlative transmission and scanning electron microscopy of the initial mineralization of healing alveolar bone in rats.

Primary mineralization in healing sockets after extraction of molar teeth was studied in rats. The observations obtained by scanning electron microscopy were correlated by transmission electron microscopy. The process is characterized by abundance of extracellular matrix vesicles distributed between the forming cells and the calcifying fronts. The occurrence of osmiophilic material and solitary hydroxyapatitte crystals within the vesicles was followed by accumulation of hydroxyapatite crystals, disappearance of the vesicular membrane and formation of calcospherites that conglomerate into calcified fronts. The process described here in bone healing is essentially similar to primary mineralization in other normal and pathological calcified tissues.

Alveolar Process↗
PubMed1998

Pulpal response to intrusive orthodontic forces.

Many studies have examined the effect of orthodontic forces on supporting tissue. However, their effect on dental pulp has not been sufficiently studied. The aim of the present study was to evaluate, histologically, the pulpal response to the action of intrusive orthodontic forces. The study was performed on 40 first premolars which had to be extracted for orthodontic reasons from 11-17 year-old patients. The twenty teeth of the experimental group received, prior to extraction, an intrusive force with an initial load of 150 g over a period of 15 to 20 days. The control group comprised the 20 homologous teeth which were not submitted to intrusive forces prior to extraction. All the teeth were fixed in 10% buffered formalin, decalcified, embedded in paraffin, sectioned and stained with hematoxylin-eosin. Light microscopy observation revealed alterations in predentine, calcium deposition, fibrohyalinosis, congestion, inflammation and haemorrhage. The data were statistically analysed employing Fisher's exact probability test. Congestion, haemorrhage and fibrohyalinosis were significantly (p < 0.005) greater in the experimental group than in controls.

Adolescent↗
PubMed2004

Immunocytochemistry of keratan sulfate proteoglycan and dermatan sulfate proteoglycan in porcine tooth-germ dentin.

Keratan sulfate proteoglycan and dermatan sulfate proteoglycan have been reported to inhibit collagen fibrillogenesis. We investigated their distribution in order to evaluate the role of proteoglycan in dentinogenesis. Specimens of porcine tooth-germ dentin and erupted teeth were the materials on which antibodies to keratin sulfate and dermatan sulfate proteoglycan were used. Predentin was found to be positive for both antibodies and the reaction ceased in the calcification front. Uniformly thick collagen fibrils (30-70 nm in diameter) were distributed in the predentin matrix, which would become intertubular dentin in the future. Both antibodies reacted positively along these fibrils. In contrast, along the surface layer of dentin in the tooth germ and that in erupted teeth, collagen fibrils of 10-300 nm in diameter were noted occasionally in dentinal tubules whose odontoblastic processes had disappeared and these heterogeneous fibrils were negative for both antibodies. Our findings suggest that keratan sulfate proteoglycan and dermatan sulfate proteoglycan distributed in the predentin inhibit calcification of collagen fibrils in the uncalcified matrix and disappear in the calcification front. It is further suggested that keratan sulfate proteoglycan and dermatan sulfate proteoglycan distributed along collagen fibrils in the predentin matrix maintain uniform thickness, whereas collagen fibrils in dentinal tubules varied in thickness because of the absence of involvement of both proteoglycans. Therefore, keratan sulfate proteoglycan and dermatan sulfate proteoglycan were thought to be involved in both calcification and matrix formation.

Animals↗
PubMed1995

Purification of nonamelogenin proteins from bovine secretory enamel.

The developing enamel matrix is composed of two groups of proteins that can be generally classified as amelogenins and nonamelogenins. The hydrophobic amelogenins represent the majority of the developing enamel matrix proteins, whereas nonamelogenins include the more hydrophilic enamelins, proteinases, and other minor protein components, which represent a small proportion of the matrix. This report describes the purification and partial amino acid sequences of two previously unknown proteins isolated from developing bovine enamel. These proteins were prepared by extracting bovine secretory stage enamel with low ionic strength buffer, followed by ammonium sulfate fractionation. The proteins were purified by ion-exchange, affinity, and reversed-phase chromatography. We propose to designate the proteins BEgp (a glycoprotein) and BEpa. A partial sequence was also obtained from a third protein (BEpb) which was nearly identical to BEpa. Antibodies were prepared to a synthetic peptide based on the N-terminal sequence of BEpa and subsequent immunoblots of various bovine tissues showed a major component of approximately 25 kDa specifically in enamel and ameloblasts. Little or no cross-reactivity of the antibody was found to bovine proteins extracted from heart, lung, kidney, liver, dental pulp, or bone. Similar analyses of both rat secretory stage and maturation stage enamel showed two bands of 28 kDa and 29 kDa. Immunohistochemical localization in rat incisors, showed specific staining of the enamel, secretory granules, and Golgi apparatus in ameloblasts. No sequence homology with known proteins could be demonstrated for BEgp or BEpa, suggesting that these components of developing enamel are novel tooth-specific proteins.

Amino Acid Sequence↗