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Transmission electron microscopy on sound demineralized guinea pig dentin
Author(s) -
JOHANNESSEN JAN VINCENTS,
BANG GISLE
Publication year - 1972
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1972.tb00284.x
Subject(s) - dentin , demineralization , guinea pig , chemistry , transmission electron microscopy , collagen fibril , ultrastructure , electron microscope , biophysics , fibril , anatomy , dentinal tubule , materials science , composite material , nanotechnology , enamel paint , biochemistry , biology , optics , physics , endocrinology
– An investigation of the ultrastructure of sound demineralized guinea pig dentin was carried out by means of the electron microscope. ERL‐4206® (vinyl cyclohexene dioxide), a new low viscosity epoxy resin medium was found superior to Epon‐812® for the embedding of demineralized dentin for electron microscopic studies. The demineralization by means of 0.2 N HCl resulted in a poor preservation of the odontoblastic processes. No evidence for the existence of a hypermineralized peritubular zone was found. In contrast to human dentin the area adjacent to the tubules in guinea pig dentin was composed of dense bundles of collagen fibrils. In the vicinity of the predentin these bundles formed a 1 μm wide zone and were arranged parallel to the tubular axis. In the outer part of the dentin no marked differences were observed between the collagenous framework of the peritubular and the intertubular zones. Here too the preferred direction of the collagen fibrils was parallel to the tubules. The structure of guinea pig dentin differed markedly from that of human dentin but resembled the structure observed in rat dentin. It is possible that cross‐striated collagen fibrils are essential for the induction of heterotopic bone formation. The bone‐inducing capacity of guinea pig and rat dentin might depend on their high content of stable cross‐striated collagen.