The composition of bovine peritubular dentin: matching TOF-SIMS, scanning electron microscopy and biochemical component distributions. New light on peritubular dentin function.

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.

Enhancement of reaction specificity at interfaces.

A realistic picture of a cell is that of a highly viscous, condensed gel-like substance, crowded with macromolecules that are mostly anchored to membranes and to intricate networks of cytoskeletal elements. Theoretical and experimental approaches to investigating crowding have not considered the role of diffusion through a crowded medium in affecting the selectivity and specificity of reactions. Such diffusion is especially important when one considers interfaces, where at least one reactant must move through the medium and reach the interface.

Peritubular dentin, a vertebrate apatitic mineralized tissue without collagen: role of a phospholipid-proteolipid complex.

Peritubular dentin (PTD), a highly mineralized annular ring surrounding each odontoblastic process within the dentin, is an enigmatic component in vertebrate teeth. To characterize its structure and composition, we have coupled in situ scanning electron microscopic (SEM) and time-of-flight secondary ion mass spectrometric (TOF-SIMS) analysis of the surface composition of intact bovine coronal dentin with the isolation of intact PTD from hypochlorite-treated dentin and its subsequent TOF-SIMS and direct chemical analysis. The isolated PTD is shown to be a mineralized but porous structure complexed with a high-molecular mass calcium-proteolipid-phospholipid-phosphate complex, which cannot be extracted from the dentin prior to demineralization.

The composition and structure of bovine peritubular dentin: mapping by time of flight secondary ion mass spectroscopy.

The dentin layer of the tooth is a complex mineralized tissue traversed by a closely packed system of tubules. Each tubule is surrounded by highly mineralized tissue referred to as peritubular dentin (PTD). The remaining mineralized collagen network between the tubules is the intertubular dentin (ITD).

Mollusk shell formation: mapping the distribution of organic matrix components underlying a single aragonitic tablet in nacre.

Control over mineral formation in mollusk shells is exerted by the macromolecules of the organic matrix. Using histochemical methods, we mapped the carboxylates and sulfates of proteins and polysaccharides on the surfaces of decalcified interlamellar matrices from the nacreous shell layer of the cephalopod Nautilus pompilius, expanding upon an earlier study by Crenshaw and Ristedt [Crenshaw, M.A.

Asprich: A novel aspartic acid-rich protein family from the prismatic shell matrix of the bivalve Atrina rigida.

Almost all mineralized tissues contain proteins that are unusually acidic. As they are also often intimately associated with the mineral phase, they are thought to fulfill important functions in controlling mineral formation. Relatively little is known about these important proteins, because their acidic nature causes technical difficulties during purification and characterization procedures.

Mollusk shell acidic proteins: in search of individual functions.

Acidic proteins play a major role in the biomineralization process. These proteins are generally thought to control mineral formation and growth. Thus, characterization of individual acidic proteins is important as a first step toward linking function to individual proteins, which is our ultimate goal.