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17. Heterotrimeric type I Collagen C-Telopeptide Conformation as docked to its helix receptor

Author

Malone, James P. and Veis, Arthur

Subjects
Collagen -- Research, Molecular dynamics -- Research, Biological sciences, Chemistry
Abstract

A suite of molecular modeling software, the more complex heterotrimeric C-telo of human type I collagen is built from the correct sequence and energy minimized and the energy minimum confirmed by molecular dynamics. The receptor triple helix is modeled on the basis of the Protein Data Bank coordinates of a collagen like sequence.

Published
2004

33. Short-term effects of amelogenin gene splice products A+4 and A-4 implanted in the exposed rat molar pulp

Author

Poliard Anne, Veis Arthur, Septier Dominique, Jegat Nadège, and Goldberg Michel

Subjects
Specialties of internal medicine, RC581-951
Abstract

Abstract In order to study the short-time effects of two bioactive low-molecular amelogenins A+4 and A-4, half-moon cavities were prepared in the mesial aspect of the first maxillary molars, and after pulp exposure, agarose beads alone (controls) or beads soaked in A+4 or A-4 (experimental) were implanted into the pulp. After 1, 3 or 7 days, the rats were killed and the teeth studied by immunohistochemistry. Cell proliferation was studied by PCNA labeling, positive at 3 days, but decreasing at day 7 for A+4, whilst constantly high between 3 and 7 days for A-4. The differentiation toward the osteo/odontoblast lineage shown by RP59 labeling was more apparent for A-4 compared with A+4. Osteopontin-positive cells were alike at days 3 and 7 for A-4. In contrast, for A+4, the weak labeling detected at day 3 became stronger at day 7. Dentin sialoprotein (DSP), an in vivo odontoblast marker, was not detectable until day 7 where a few cells became DSP positive after A-4 stimulation, but not for A+4. These results suggest that A +/- 4 promote the proliferation of some pulp cells. Some of them further differentiate into osteoblast-like progenitors, the effects being more precocious for A-4 (day 3) compared with A+4 (day 7). The present data suggest that A +/- 4 promote early recruitment of osteogenic progenitors, and evidence functional differences between A+4 and A-4.

Published
2007
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37. Structure and assembly of the heterotrimeric and homotrimeric C-propeptides of type I collagen: Significance of the alpha2(I) chain

Author

Malone, James P., Alvares, Keith, and Veis, Arthur

Subjects
Peptides -- Structure, Molecular structure -- Research, Collagen -- Structure, Collagen -- Research, Biological sciences, Chemistry
Abstract

The mechanism of the in vivo assembly of a three-chain procollagen molecule is one of the most interesting problems remaining with regard to collagen biosynthesis. Each of the alpha chains of the heterotrimeric type I procollagen molecule has five major domains, the N-propeptide, N-telopeptide, triple helix, C-telopeptide, and C-propeptide.

Published
2005

49. The Composition of Bovine Peritubular Dentin: Matching TOF-SIMS, Scanning Electron Microscopy and Biochemical Component Distributions: New Light on Peritubular Dentin Function

Author

Gotliv, Bat Ami and Veis, Arthur

Subjects
Paper, Tooth Fractures, stomatognathic system, Surface Properties, Dentin, Sodium, Microscopy, Electron, Scanning, Animals, Spectrometry, Mass, Secondary Ion, Calcium, Cattle, Amino Acids, Tooth
Abstract

Peritubular dentin (PTD) is a hypermineralized phase within the dentinal tubules in some vertebrate teeth as an interface between the intertubular dentin (ITD) and the cell processes. Our aim has been to understand the composition, structure and role of PTD as a mineralized tissue. We have utilized the technique of time of flight secondary ion mass spectrometry (TOF-SIMS) to map the distribution of positive and negative inorganic ions as well as organic components in the fully mineralized, intact PTD structure in bovine tooth cross-sections, and correlated these with scanning electron microscopy (SEM) in standard and backscatter modes. In recent work, we developed a procedure to freeze fracture the teeth and separate PTD from the less dense ITD by the use of aqueous sodium phosphotungstate step density gradients, after degrading the ITD collagen with NaOCl. Here, PTD-containing fragments were characterized by SEM and TOF-SIMS surface structure analysis. The TOF-SIMS data show that the isolated PTD does not contain collagen, but its surface is rich in glutamic acid-containing protein(s). The TOF-SIMS spectra also indicated that the intact PTD fragments contain phospholipids, and chemical analyses showed phosphatidylserine, phosphatidylinositol and phosphatidylcholine as the principal lipid components. In SEM sections, untreated PTD shows as a smooth collar around the tubule, but after digestion with ethylenediamine to remove all organic components, the porous nature of the mineral phase of small, thin platy apatite crystals becomes evident. Thus, the organic matrix of PTD appears to be a proteolipid-phospholipid complex.

Published
2008

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