Scanning electron microscope observations on collagen fibers in human dentin and pulp

Human permanent teeth were examined in the scanning electron microscope after demineralization and exposure to preparative procedures based on hydrogen peroxide, trypsin, and EDTA. These substances removed the inorganic material, the cellular structures, the homogeneous connective tissue ground substance, and interfibrillar matrix. The remaining tissue components comprised a network of distinct collagen fibers whose organization was related to the type of tissue in which these were incorporated. A similar or identical method has not been developed or applied to teeth previously. Dentin and predentin comprised a compact mass of fibers which basically were parallel to the continuously growing interior surface of the predentin, or arranged at an acute angle to this plane. Collagen fibers in the pulp were numerous, but lacked any particular orientation in most areas. Interodontoblastic fibers crossed the odontoblastic zone at a right angle to the pulp chamber wall and mingled with collagen fibers in predentin. When previously published findings of ours are taken into account, it is possible to conclude that other factors than the organization of the collagen fibers are responsible for the stainability of these fibers in predentin and in interglobular dentin with silver methenamine, and that aldehyde groups on collagen fibers in predentin may be actively and directly involved in the mineralization of the dentin.