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Results for “Dentin Solubility”

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PubMed2000

N-terminal sequence analysis of bovine dentin phosphophoryn after conversion of phosphoseryl to S-propylcysteinyl residues.

Bovine dentin phosphophoryn (BDP), a protein rich in aspartyl (Asp) and O-phosphoseryl (Ser[P]) residues, is synthesized by odontoblasts and is believed to be involved in matrix-mediated biomineralization of dentin. We have purified BDP, using selective precipitation and ion exchange chromatography, from an EDTA soluble dentin extract and converted the Ser(P) residues to S-propylcysteinyl residues that are stable to Edman degradation, facilitating the determination of the amino acid sequence of the N-terminal 38 residues. After the initial Asp-Ser(P)-Pro-Asn-Ser(P)-Ser(P)-Asp-Glu-Ser(P)-Asn-Gly-, the sequence contained the repeated motifs Asp-Ser(P) and Asp-Ser(P)-Ser(P). Purified BDP migrated as a single band on gradient SDS-PAGE with an apparent molecular weight of 156 kDa. This value was consistent with the molecular weight of the dephosphorylated protein of 105 kDa determined by means of MALDI mass spectrometry.

Amino Acid Motifs↗
PubMedDate not supplied

In vitro differentiation and mineralization of human dental pulp cells induced by dentin extract.

In this study, the progenitor cells isolated from the human dental pulp were used to study the effects of ethylenediaminetetraacetic acid-soluble dentin extract (DE) on their differentiation and mineralization to better understand tissue injury and repair in the tooth. Mineralization of the matrix was increasingly evident at 14, 21, and 28 d after treatment with a mineralization supplement (MS) (ascorbic acid [AA], beta-glycerophosphate [beta-GP]) and MS + DE. Real-time polymerase chain reaction results showed type I collagen upregulation after the addition of MS + DE at 7 d. Alkaline phosphatase was downregulated after the mineralization became obvious at 14 d. Bone sialoprotein was shown to be upregulated in the mineralized cell groups at all time points and dentin sialophosphoprotein after 7 d. Core binding factor a 1 was upregulated by the treatment of MS and DE at 7, 14, and 21 d. These results indicated that the MS of AA, beta-GP, and DE synergistically induced cell differentiation of pulp progenitor cells into odontoblast-like cells and induced in vitro mineralization.

Alkaline Phosphatase↗
PubMed2002

TGF-beta latency-associated peptides (LAPs) in human dentin matrix and pulp.

Transforming growth factor (TGF)-beta s in dentin matrix provide a pool of bioactive molecules, but association with latency-associated peptides (LAPs) may influence their activity. We investigated TGF-beta 1, -beta 2, and -beta 3 LAP expression in sound and carious human teeth. Teeth were fixed and processed immediately following extraction prior to staining with rabbit polyclonal antibodies to the TGF-beta LAPs. A soluble dentin matrix fraction was prepared from dissected human dentin and sequential extraction of pulpal ECM was performed prior to purification. Fractions were Western blotted and probed with the LAP antibodies. All three LAPs were present in odontoblasts, cells of the pulp, and predentin; however, no staining of mineralized dentin matrix was seen. Similar patterns of expression were seen in carious tissue. Expression of TGF-beta LAPs in cells and pulpal matrix of healthy and carious teeth will be important in regulation of TGF-beta activity and may modulate the tissue response to injury.

Dental Caries↗
PubMed1999

Hydroxyproline interference during the gas chromatographic analysis of D/L aspartic acid in human dentine.

The proportion of D- to L-enantiomers of aspartic acid in metabolically isolated proteins has been used by forensic scientists to estimate age at death. We have demonstrated the interference of a derivative of hydroxyproline (N-TFA isopropyl Hyp ester) with the N-TFA isopropyl L-Aspartic (Asp) acid ester during gas chromatography of amino acids. This has serious implications for the accurate quantification of the D- to L-Asp ratio extracted from collagenous proteins. Having demonstrated the potential for this co-elution in amino acid standards, acid-soluble dentine proteins and non-mineralised collagen, we argue that this problem can be overcome either by high resolution separation or by analysis of the (Hyp-poor) non-collagenous protein fraction.

Aspartic Acid↗
PubMed1997

The dentin substrate: structure and properties related to bonding.

OBJECTIVES: Dentin is a vital, hydrated composite material with structural components and properties that vary with location. These variations are reviewed along with alterations by physiological and pathological changes that allow classification into various forms of dentin. Structural characteristics and mechanical properties are reviewed and the limitations of our understanding of structure-property relationships for normal and modified forms of dentin are discussed with respect to their impact on dentin bonding. Recent progress in methods available to study dentin and its demineralization are emphasized with their promise to increase our understanding of dentin properties and structure. DATA SOURCES: Recent microstructural studies, focusing on scanning electron microscopy, atomic force microscopy and X-ray tomographic microscopy are included. A review of fundamental studies with emphasis on microstructurally sensitive methods, and prior reviews of basic mechanical properties are included with discussion of their correlation to composition and structure. STUDY SELECTION AND CONCLUSIONS: Emphasis in this work was placed on the major structural components of the tissue, including the collagen based organic matrix and its mineral reinforcement, the distribution of these components and their microstructural organization as related to mechanical properties and response to demineralization. Little information is included on biochemical and developmental studies or on non-collagenous proteins and other organic components for which limited understanding is available with respect to their role in structure-property relations and influence on bonding. In spite of the fact that the complexity of dentin precluded a comprehensive review, it is clear that local structural variations influence properties and impact nearly all preventive and restorative dental treatments. Much more work is needed in order to understand differences between vital and non-vital dentin, and dentin from extracted teeth. Although our knowledge is rudimentary in certain areas, increasingly sophisticated methods of studying dentin should provide the necessary information to model structure-property relations, optimize dentin bonding, and improve many aspects of preventive and restorative dentistry.

Apatites↗
PubMed1990

Release of organic matrix components from bovine incisor roots during in vitro lesion formation.

The solubilization of organic matrix components during demineralization of powdered and intact root sections from adult bovine incisors was investigated. Root powder was demineralized with 0.1 mol/L acetic acid, pH 4.0, at 4 degrees C and 37 degrees C. Surfaces of intact root sections were subjected to 0.1 mol/L acetic acid, pH 4.0 (for production of erosive lesions), or to 0.1 mol/L lactic acid, 0.2 mmol/L methane hydroxy diphosphonate, pH 5.0 (for production of subsurface lesions at 37 degrees C). The solubilized organic material was analyzed for collagen, total noncollagenous protein (NCP), organic phosphate (Po), and proteoglycans (PGs), which were measured as chondroitin 4-sulfate (C-4-S). For root powder, a maximal release of NCPs and PGs was found only after neutralization of the extraction mixture. For both temperatures tested, the average amounts of liberated noncollagenous components (NCCs) were the same, i.e., 0.68 micrograms [NCP - Po], 0.11 microns Po, and 0.10 micrograms C-4-S per mumols released calcium. The amino acid composition of the NCP fraction revealed relatively high amounts of aspartic acid and serine. These findings indicate that the NCCs were easily liberated from the tissue, and that the NCP fraction consisted mainly of phosphoprotein. Demineralization of intact root sections resulted in average amounts of solubilized NCCs of 0.21 micrograms [NCP - Po], less than 0.01 micrograms Po, and less than 0.01 micrograms C-4-S per mumols released calcium, independent of incubation time and lesion type. The amino acid composition of all NCP fractions was virtually the same, high in glutamic acid, but lower in aspartic acid and serine when compared with the neutralized powder extracts. For both demineralization solutions, the amounts of solubilized collagen were 0.07 and 0.16 micrograms per micromol released calcium after three and 28 days of incubation, respectively. Our experiments indicate that phosphoprotein and proteoglycans may be released from root surfaces during the periods of neutral pH that follow acid demineralization.

Amino Acids↗
PubMed2002

Preserving the vital pulp in operative dentistry: I. A biological approach.

This is the first in a series of four papers aimed at understanding human pulpal responses to tissue injury, cavity preparation and restorative events. This article provides an insight into the exquisite regenerative potential of the dentine-pulp complex which underpins the success of restorative dentistry.

Acid Etching, Dental↗
PubMed2005

Hardness and Young's modulus of transparent dentin associated with aging and carious disease.

This study investigated the changes in hardness and Young's modulus of the transparent layer of dentin associated with aging and the carious process. Eighteen extracted human molars with or without coronal caries were used in this study. The normal teeth were divided into two groups by age, and the carious teeth were divided into two groups of active or arrested caries. After polishing the specimens parallel to the long axis of the tooth, both hardness and Young's modulus were measured using a nanoindentation tester. The hardness and Young's modulus of the transparent layer in aged dentin were higher than the other portions of aged dentin. The transparent layer under carious lesions had a significantly lower hardness than the underlying normal dentin, whereas its Young's modulus was not significantly reduced. The hardness and Young's modulus of the transparent layer in active carious lesions were lower than those in arrested carious lesions.

Aging↗