Three dental hard tissues, i.e., cementum, dentin, and enamel, are resorbed by multinucleated cells referred to as "odontoclasts." These cells have morphological and functional characteristics similar to those of bone-resorbing osteoclasts. However, concerning enamel resorption, which is a process that may occur during tooth eruption, satisfactory ultrastructural data on odontoclastic resorption are still lacking. Ultrastructural and histochemical characteristics of odontoclasts resorbing enamel of human deciduous teeth prior to shedding were examined by means of light microscopy and transmission and scanning electron microscopy. Odontoclasts that that resorbed enamel were tartrate-resistant acid phosphatase (TRAP)-positive multinucleated giant cells that were essentially the same as those that resorbed dentin and cementum. Ultrastructurally, they had numerous mitochondria, lysosomes, and free polysomes in their cytoplasm. In addition, they were characteristically rich in large cytoplasmic vacuoles containing enamel crystals in the cytoplasm opposite the ruffled border. Although they extended a well-developed, ruffled border against enamel surface, a clear zone--an area typically devoid of organelles--was rarely seen in these cells. In many cases, the cells were in very close contact with the enamel surface by the peripheral part of their cytoplasm. The enamel prisms at the resorption surface contained more loosely packed and electron-lucent enamel crystals compared with those of unresorbed, intact enamel. Furthermore, numerous thin needle- or plate-like enamel crystals that were liberated from the enamel matrix were found in the extracellular channels of the ruffled border and in various-sized cytoplasmic vacuoles in their cytoplasm. The superficial layer of the enamel matrix undergoing odontoclastic resorption stained positively with toluidine blue and for TRAP activity. The results of the present study suggest that odontoclasts resorbing enamel secrete acids as well as organic components, including hydrolytic enzymes, into the resorption zone underlying their ruffled border and that they phagocytose crystals that have been liberated from the partially demineralized enamel matrix by acids, subsequently dissolving them intracellularly.
Biomembranes feature phospholipid bilayers and serve as the interface between cells or organelles and the extracellular and/or cellular environment. Lipids can move freely throughout the membrane; the lipid bilayer behaves like a fluid. Such fluidity is important in terms of the actions of membrane transport proteins, which often mediate biological functions; membrane protein motion has attracted a great deal of attention. Because the proteins are small, diffusion phenomena are often in play, but flow-induced transport has rarely been addressed. Here, we used a dissipative particle dynamics approach to investigate flowinduced membrane protein transport. We analyzed the drift of a membrane protein located within a vesicle. Under the influence of shear flow, the protein gradually migrated toward the vorticity axis via a random walk, and the probability of retention around the axis was high. To understand the mechanism of protein migration, we varied both shear strength and protein size. Protein migration was induced by the balance between the drag and thermodynamic diffusion forces and could be represented by the P eclet number. These results improve our understanding of flow-induced membrane protein transport.
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