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Arthur Veis

Publications and source records attributed to Arthur Veis.

23 records · Page 2Linked to original sources

Bioactive molecules and the future of pulp therapy.

Direct capping of bioactive molecules or implantation of these molecules in the pulp may induce the formation of reparative dentin and coronal or radicular pulp mineralization. In this review, we summarize what is known and/or assumed on the biological mechanisms of these therapies. We report on the effects which were obtained experimentally in rat maxillary molars by implantation of Bone Sialoprotein (BSP)/collagen pellets and Specific Amelogenin Gene Splice Products [A+4] and [A-4]) adsorbed on agarose beads. The effects were compared with those of BMP-7 (OP-1) and Ca(OH)2. Depending on the molecule that was used, we obtained either the formation of a dentin bridge, or the filling of the pulp in the mesial part of the coronal pulp chamber, or the total mineralization of the root canal. These molecules may provide new therapeutic tools in the next future in dentistry.

Animals↗

Electrostatic interactions lead to the formation of asymmetric collagen-phosphophoryn aggregates.

In bone and dentin the formation and mineralization of the extra cellular matrix structure is a complex process highly dependent on intermolecular interactions. In dentin, the phosphophoryns (PP) and type I collagen (COL1) are the major constituents implicated in mineralization. Thus, as a first step in understanding the tissue organization, we have initiated a study of their interaction as a function of pH, ionic strength, and relative concentrations or mixing ratios. Complex formation has been analyzed by dynamic light scattering to detect aggregate formation and by rotary shadowing electron microscopy (EM) to determine aggregate shape. The EM data showed that at the pH values studied, the PP-COL1 interaction leads to the formation of large fibrillar aggregates in which the PP are present along the fibril surfaces. The quantitative phase distribution data showed a 1/1 molar equivalence at the maximum aggregation point, not at electrostatic PP-COL1 equivalence. As the ionic strength was raised, the PP-COL1 aggregates became smaller but the binding and asymmetric fibrillar aggregation persisted. In EM, the PP appear as dense spheres. Along the surfaces of the collagen aggregates, the PP are larger and more open or extended, suggesting that COL1-bound PP may undergo a conformational change, opening up so that a single PP molecule might interact with and electrostatically link several COL1 molecules. This might have important implications for dentin structure, stability, and mineralization.

Animals↗

Dentin matrix protein 1 initiates hydroxyapatite formation in vitro.

Bone and dentin formation are interesting examples of matrix-mediated mineralization. However, factors and mechanisms regulating this process are poorly understood. Dentin matrix protein 1 (DMP1) is an acidic extracellular matrix protein found in dentin and bone, and based on its amino acid composition it could be postulated to play an important role in mineralization. Our present study examines the ability of recombinant DMP1 to initiate apatite formation in vitro. A 45Ca-binding assay demonstrated that recombinant DMP1 (rDMP1) possesses calcium-binding ability under physiological conditions. The in vitro nucleation experiments when conducted with rDMP1-coated glass plates demonstrated hydroxyapatite nucleation, while amorphous mineral was deposited on blank or BSA-coated surface. This mineral deposition was found to be 10-fold higher on rDMP1-coated glass surface when compared with the control glass plates. These findings suggest that DMP1 could be considered as a nucleator for apatite deposition in vitro.

Calcification, Physiologic↗

Mineral-related proteins of sea urchin teeth: Lytechinus variegatus.

Sea urchins have a set of five continuously growing teeth, each of which has a very complex structure. The mineral phase is calcite of varying Mg content, depending on the location within a tooth. The calcium carbonate is present in amorphous, plate-like and rod-like forms. It has been hypothesized that the mineral deposition is a matrix-mediated process, similar to that in vertebrate bone and tooth, wherein certain macromolecules within the organic matrix of the mineralized tissue play an important role in nucleating and controlling the growth habit of the mineral crystals. It has also been hypothesized that the mineral-related macromolecules involved in urchin teeth might bear a direct evolutionary relationship to those of the vertebrate tooth. These hypotheses are explored here by examining the pattern and nature of the mineral distribution, using microCT of intact teeth, and the nature of the mineral-related matrix proteins. The mineral-related proteins were extracted and fractionated by anion exchange chromatography. The relationship of certain fractions to vertebrate matrix proteins was established by immunoblots using antibodies to vertebrate tooth proteins. The antibodies were then used to localize the proteins within the teeth, by immunocytochemistry and histology with specific staining. The microCT data on mineral density has been correlated with the patterns of cellular migration and mineral deposition within the tooth as it grows. It appears that the mineralization within the different tooth compartments might take place under the influence of different matrix proteins. Further studies are in progress to more completely describe the vertebrate-invertebrate immunologically cross-reactive proteins of the urchin teeth.

Animals↗

Polypeptides translated from alternatively spliced transcripts of the amelogenin gene, devoid of the exon 6a, b, c region, have specific effects on tooth germ development in culture.

Recombinant proteins have been produced from cDNAs corresponding to alternatively spliced transcripts comprised from exons 2,3,4,5,6d,7 and 2,3,5,6d,7 of the rat amelogenin gene. These peptides, designated as [A + 4] and [A - 4], respectively, induce embryonic muscle fibroblasts in culture in vitro to express proteins characteristic of the chondrogenic and osteogenic phenotypes, and in matrix-supported implants into rat muscle, in vivo, induce typical bone matrix proteins. The aim of the present work was to examine the potential role of these proteins on the development of odontogenic tissue. The lower first molars were collected from Charles River CD-1 mice at postnatal days 1 and 2 and were grown on semisolid, serum-free medium supplemented with ascorbic and retinoic acids and transferin. The peptides were added to the serum-free media at 10 ng/ml. As controls, the medium was either 20% fetal bovine serum or the supplemented serum-free medium without either amelogenin peptide. The tooth germs were cultured for 6 days, then fixed and paraffin embedded by standard procedures. The tissue blocks were serially sectioned and stained with hematoxylin-eosin (H&E), or antibodies to collagen 1 (Col1), phosphophoryn (DMP2), or cementum attachment protein (CAP). CAP, DMP2, and Col1 expression was enhanced by the addition of the amelogenin peptides, as compared to the 0% fetal bovine serum (FBS) controls, but the peptides showed different effects. Expression of DMP2, characteristic of dentin matrix, was upregulated by [A + 4], whereas CAP, characteristic of cementum, was upregulated by [A - 4]. Since the recombinant peptides are active, their corresponding tissue forms may be important in the stimulation of mesenchymal tissue differentiation. Thus, these specific amelogenin proteins may be involved in tooth morphogenesis.

Aging↗