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PubMed1997

Fluoride uptake in dentin with and without simulating dentinal fluid flow.

The aim of the present study was to compare fluoride uptake of dentin with and without simulating dentinal fluid flow. Eighty-five dentinal discs were prepared from retained human molars. Seventeen discs were used to assess baseline fluoride content (controls). Sixty-eight discs were evenly distributed among two experimental groups and were fixed for 24 h in a two-chamber device allowing for simulating dentinal fluid flow. Thirty-four samples were treated with dentifrice slurry containing a low fluoride concentration (Elmex, dilution 1:5); the remaining discs were treated with a solution of a high fluoride concentration (Elmex Fluid). For the perfused group, each of the 17 discs of the high and low concentration fluoride groups were constantly perfused during the experiment. The remaining fluoridated specimens were not perfused. All specimens were assayed for KOH-soluble fluoride and structurally bound fluoride. Structurally bound fluoride was determined in three successive layers of 20 microns each. Uptake of KOH-soluble fluoride was significantly higher in the specimens fluoridated with Elmex Fluid compared to the samples treated with the dentifrice slurry. The uptake of KOH-soluble fluoride was not influenced by perfusion of the dentinal discs. However, perfusion resulted in lower acquisition of structurally bound fluoride in the samples treated with the dentifrice slurry. After application of Elmex Fluid, no significant difference was found in the amount of structurally bound fluoride between the perfused specimens and non-perfused samples. It is suggested that further studies on fluoride uptake in dentin should use a model simulating outward dentinal fluid flow.

Analysis of Variance↗
PubMed1983

Stereochemically altered noncollagenous protein from human dentin.

Highly phosphorylated noncollagenous proteins (NCP) with molecular weights of approximately 70-100,000 daltons have been purified from rat and bovine dentin. Efforts to isolate phosphoprotein from human teeth have not yielded consistent results, and failures have been attributed to proteolysis due to preparative techniques. Diagenetic reactions affecting metabolically stable proteins in vivo also can interfere in protein purification. Racemization is one of the reactions known to take place in human dentin. EDTA extraction of dentin from an age-graded series of human teeth has yielded an EDTA-soluble NCP fraction having an aspartic acid racemization rate 3 X that in unfractionated dentin and 8 X the rate in EDTA-insoluble protein. D-Aspartic acid is accumulating in EDTA-S protein at a rate of 0.22% yr-1. For humans, more than 13% of the aspartyl residues in NCP will be the D-enantiomer by 60 years of age. While racemization presents no problem for shorter lived mammals, such as rats, it could be partly responsible for purification difficulties with human dentin.

Aging↗
PubMed1996

Root canal irrigation with citric acid solution.

The purpose of this study was to investigate various properties of citric acid and EDTA solution as decalcifying and cleansing agents in root canal irrigation, and antibacterial effects of citric acid and EDTA solution. Powdered dentin-resin mixtures were used for evaluating the decalcifying effect of citric acid and EDTA solution. Twelve bacterial strains isolated from infected root canals, were used to evaluate the antibacterial effects of citric acid and EDTA solution. Powdered dentin-resin mixture was found to be more soluble in a 0.5, 1, and 2 M citric acid solutions than in a 0.5 M EDTA solution. Citric acid solution showed antibacterial effects on all the bacteria used.

Anti-Infective Agents, Local↗
PubMed1993

[Response of odontoblastic and pulpal cells to carious lesions].

The odontoblast responds to caries by the formation of sclerotic as well as reparative dentin. Sclerotic dentin is deposited during the early stages of the dentinal injury. It is characterized by the amplification of the collagen synthesis and the increase in alkaline phosphatase activity in the odontoblastic cell layer. Reparative dentin will be deposited under the sclerotic zone after the destruction of odontoblasts. At this stage, specific components from damaged dentinal tissues and/or odontoblastic necrotic debris will trigger pulpal cells to elaborate a cartilage-like matrix layer (fibrodentin). The latter may induce pulpal odontoblast-like cells to give rise to the tubular reparative dentin. Thus, pulpal cell response seems to be similar to bone-cell response to injury. Molecular signals responsible for this tissular healing remain largely unknown, but dentin is a potential source of matrical or soluble organic molecules that may be released after demineralization. Some of these factors have been identified in the sound tissue (glycoproteins, proteoglycans, growth factors, ...), but their role in the stimulation of the elaboration of the cicatricial tissue remains to be elucidated.

Cell Differentiation↗
PubMed1978

Micromorphologic features of cervical erosion after acid conditioning and its relation with composite resin.

The dentin surface in cervical erosion appears relatively smooth with evidence of intratubular deposits. After acid conditioning, the tubules are made patent though some still contain relatively less soluble intratubular contents. Resin applied to acid-conditioned, eroded dentin penetrated approximately 30 micrometers compared to more than 100 micrometers into the tubules of similarly treated normal dentin.

Acid Etching, Dental↗
PubMed2001

ADAM8: a novel osteoclast stimulating factor.

We used polymerase chain reaction (PCR)-selective complementary DNA (cDNA) subtraction hybridization with an immortalized murine osteoclast (OCL) precursor cell line to identify genes that are highly expressed in OCLs compared with OCL precursors and which may be involved in the OCL differentiation process. ADAM8 was one of the 50 genes identified. ADAM (a disintegrin and metalloproteinase) peptides are membrane-bound proteins that can act as cell-to-cell and cell-to-matrix adhesion molecules, degrade the extracellular matrix, and play a role in tissue morphogenesis. Addition of antisense (AS) S-oligonucleotides for ADAM8 (1-10 nM) to mouse bone marrow cultures treated with 10(-9) M 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] significantly inhibited OCL formation compared with treatment with the control S-oligonucleotide. Furthermore, conditioned media from 293 cells transiently transfected with a secretable form of the ADAM8 cDNA increased OCL formation in a dose-dependent manner. In addition, treatment of OCLs with soluble ADAM8 conditioned media significantly increased pit formation per dentin slice compared with control OCLs. Time course studies indicated that ADAM8 increased OCL formation only when it was present during days 4-7 of the 7-day culture period. Structural analysis, using truncated constructs of ADAM8, showed that the cysteine-rich/disintegrin domain was responsible for its OCL stimulatory activity. Western blot analysis confirmed that the soluble form of ADAM8 is present in normal marrow cultures. These data suggest that ADAM8 plays an important role in OCL formation and acts primarily at the later stages of OCL differentiation.

ADAM Proteins↗
PubMed1984

Biosynthesis of tooth germ proteins in vitro: a fast quantitative extraction of amelogenins from intact hamster molar tooth germs.

A three step extraction procedure was carried out on intact hamster molar tooth germs in vitro labelled with 32PO4 and/or 3H-proline, in order to quantify separately the synthesis of dentine matrix (collagen) and the proline rich enamel matrix proteins. The extraction was based on the high solubility of the proline rich enamel matrix proteins compared with the relatively insoluble dentine matrix collagens. Pretreatment with 10% trichloroacetic acid (step 1) demineralized and removed the non-incorporated amino acids and/or small sized peptides. A consecutive water extraction (step 2) removed a large percentage of the phosphorylated amelogenins as assessed by SDS-urea-polyacrylamide-electrophoresis and amino acid analyses. Collagenase digestibility data showed that only small amounts of collagens were present in this extract. Further extraction with 10% formic acid (step 3) released only small amounts of amelogenins from the explants but also increased contamination with collagens and another predominantly low molecular components. Most of the 3H-activity remaining in the residues was found in the collagenase labile material and was considered to be an appropriate measure for production of dentine collagens. On the other hand, the residues also contained small amounts of 3H-labelled material with the same electrophoretic mobility as amelogenins but had much more 32P-activity than the amelogenins derived from the water and formic acid extracts. It is suggested that this material in the residues probably contains the crystal bound enamel matrix proteins.

Amelogenesis↗
PubMed1994

Effect of wettability of adhesive resins on bonding to dentin.

The purpose of this study was to investigate on human dentin the relationships between, on the one hand, the wettability of five adhesive compounds, characterized by different solubility parameters delta, and on the other, the thickness of the resin impregnated dentin layer (RIL) and the shear bond strength (SBS). Cut dentin surfaces were treated with conditioners of pH 1.25, 3.6 or 7.4. Shear bond strength was measured on 20 specimens each. RIL was determined by scanning electron microscope on specimens fractured perpendicularly to the bonding interface. When resins with delta 32, 30 or 39 (MJ1/2/m3/2) were used RILs were consistently 4 microns and 1 micron on dentin pretreated with the two acidic conditioners. No clearly measurable RIL was shown after application of the conditioner with pH 7.4, and when resins with delta-values of 20 and 25 were applied. For the same adhesive no difference in SBS was found, when applied on the differently conditioned dentin sites. Resins with delta > 30 produced significantly higher SBS than the two adhesives with smaller delta.

Analysis of Variance↗
PubMed1983

Noncollagenous proteins of rat compact bone.

In order to obtain a comprehensive overview of the noncollagenous proteins (NCPs) of bone matrix, the NCPs were extracted from rat compact bone and fractionated using methods aiming to prevent artifactual degradation and losses of protein. The NCP content of rat bone was found to be similar to that of rat dentin in several respects but different in others. The soluble NCPs of bone fell into four categories: acidic glycoproteins, gamma-carboxyglutamate-containing proteins, phosphoproteins, and proteoglycans. With the exception of the gamma-carboxyglutamate-containing proteins, the majority of NCPs had apparent molecular weights exceeding 50,000. As in rat dentin, several gamma-carboxyglutamate-containing proteins could be demonstrated in rat bone. Earlier studies have only taken one molecular species into consideration. No highly phosphorylated phosphoprotein could be demonstrated in bone. However, at least two phosphoproteins with a low degree of phosphorylation were found to be present. No plasma proteins could be demonstrated in any of the chromatographic fractions from the EDTA extracted NCPs by means of double diffusion. The NCPs, remaining firmly associated with the collagenous matrix after thorough demineralization and extraction, were analyzed after CNBr and collagenase degradation of the matrix. Much smaller amounts of phosphoprotein were recovered after CNBr digestion than reported earlier. Collagenase digestion released small amounts of acidic glycoprotein, phosphoprotein, and proteoglycan. The results give additional evidence that this small remainder might be explained, not by any covalent linkage to collagen, but by an inefficient extraction.

Amino Acids↗
PubMed1997

Controlling dentine penetration in computer microleakage tracer mapping.

OBJECTIVES: Microleakage tracer penetration tests in dentine with simple sectioning are often confounded by dentine tubule penetration into the interface, leaching of water soluble tracers on wet sectioning, lack of standardized cavity dimensions affecting stresses, inadequate sectioning missing important tracer regions and airlocks obstructing tracer entry. The present aim was to create high resolution maps of stained interfaces without these confounding factors. METHODS: Ten intact extracted permanent upper central incisors were horizontally sectioned through the upper root, one third of the root length from the mid-buccal enamel limit. A dentine-bonded resin composite (Scotchbond MP, Z100, 3M) restoration was placed in a cylindrical cavity milled centrally in the root face of the coronal portion of five teeth. Tubules were angled at a mean of 12.5 +/- 4.8 degrees to the root face, and travelled approximately radially from the interface, such that tubule penetration was directed sufficiently radially outward to be distinguished from vertical interface penetration. Waterfast silver nitrate staining was applied with initial vacuum at 30 mmHg. A precision grinding machine serially removed approximately 100 microns increments of the tooth until no tracer remained, and computer image analysis data for the 18 revealed surfaces were used to construct detailed interface tracer maps. RESULTS: Control specimen tubule penetration was directed sufficiently radially outward to permit tubule penetration to be isolated from vertical interface penetration in test specimens, and ignored. Interface penetration ranged from approximately 0.3 to 1.6 mm in depth, and 0.90 to 5.09 mm2 in area. CONCLUSIONS: This method provided quantitative standardized high resolution mapping of interface tracer penetration, unconfounded by dentine penetration. None of the interfaces was fully sealed.

Coloring Agents↗
PubMed1993

Molar efficiency study of chlorinated NPG substitutes in dentin bonding.

This study evaluated and compared the contributions to dentin adhesive bonding of three N-phenylglycine analogues with electron-withdrawing substituents on the aromatic ring. These electron-deficient "N-compounds" included: N-(4-chlorophenyl)-glycine (NCPG), N-methyl-N-(4-chlorophenyl)-glycine (NMNCPG), and N-(3,4-dichlorophenyl)-glycine (NDCPG). An experimental three-step dentin-bonding protocol that consisted of sequential application of acidic ferric oxalate solution, an N-compound in acetone, and a surface-active comonomer in acetone was used. The first and third steps were held constant throughout the study. Each N-compound (NCPG, NMNCPG, NDCPG) was used in step two at ten concentrations ranging from 0.0 mol/L (pure acetone) to 5 x 10(-1) mol/L, depending on solubility. After overnight storage in distilled water, the dentin-to-composite bonds were broken in tension. The data were analyzed with ANOVA, and multiple comparisons were performed with Duncan's Multiple Range test. All statistical tests were controlled at alpha = 0.05. At 5 x 10(-3) mol/L, the relative effectiveness of the three N-compounds (as measured by tensile bond strengths) was NMNCPG > NCPG > NDCPG. Of all concentrations studied, the mean bond strengths produced with NMNCPG were statistically as good as or better than those produced by the other two compounds, and NCPG was always as good as or better than NDCPG. Increased electron-withdrawing from the nitrogen of the amine group by the substituents narrowed the effective concentration range for dentin bonding and, in general, produced lower mean bond strengths between dentin and composite.

Amines↗
PubMed1983

Evaluation of glass ionomer luting cements.

In the present study the three glass ionomer luting cements available on the Scandinavian market in June, 1982 were evaluated by comparison with a zinc phosphate and a zinc carboxylate cement. The following properties were tested: effective maximum grain size, retention, strength, bond strength to dentin, disintegration in and absorption of water and solubility in 0.001 n lactic acid. The glass ionomer cements proved to be fully acceptable luting materials.

Absorption↗
PubMed1995

Biocompatibility of dental adhesives.

This article provides biological and technological information to support routine use of new cohesive bonding systems with definitive restorations. With these systems, clinicians may expect many advantages over the more traditional water soluble base and liner systems. Hybridization of vital dentin will prevent postoperative hypersensitivity under restorations and completely seal the tooth-restoration interface to prevent bacterial infection of the underlying substrate, ultimately reducing recurrent caries underneath the hybridized restoration.

Acid Etching, Dental↗
PubMedDate not supplied

Human osteosarcoma-derived soluble bone morphogenetic protein.

A bone morphogenetic protein (BMP) fraction obtained from the organic matrix of dentin is extractable from human osteosarcoma. A fresh en-bloc specimen excised from the femur of a 16-year-old boy was extracted with 4 M guanidine hydrochloride. The GuHCl-soluble, water-insoluble protein fraction induced new bone formation when implanted into the thigh muscles of athymic nude mice.

Animals↗
PubMed1986

On the problem of covalent linkages between phosphoproteins and collagen in bovine dentin and bone.

The majority of phosphoproteins in bovine bone and dentin are insoluble in EDTA and guanidine hydrochloride (Gu.HCl) at 2 degrees C. After removal of EDTA and Gu.HCl-soluble proteins at 2 degrees C, collagen alpha-chains and alpha-chain polymers were extracted from bovine bone and dentin in Gu.HCl at elevated temperatures and purified by several chromatographic techniques and SDS-PAGE. Small amounts of O-phosphoserine were found in all collagen components. In contrast, O-phosphoserine was not detected in the purified collagen components soluble in EDTA or Gu.HCl at 2 degrees C nor was hydroxyproline detected in the EDTA-soluble phosphoproteins. In contrast, although the vast majority of EDTA-insoluble collagen and phosphoprotein molecules can be readily dissociated by a variety of molecular sieving and ion-exchange chromatographic procedures, a small number are very strongly associated or covalently cross-linked. These results are consistent with the findings that both hydroxyproline and hydroxylysine are present in purified phosphoprotein components released from the EDTA-insoluble tissue by bacterial collagenase. The hydroxylysine/100 hydroxyproline ratios in the phosphoprotein-collagen complexes are much higher than those in dentin or bone collagens.

Animals↗