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The structure of rat incisor enamel is established at the topographically complex interface between secretory ameloblasts and forming enamel. The aim of this study was to gain additional information on this interface by sectioning parallel with the rows and the long axis of Tomes' processes and prisms. Rats were sacrificed and fixed by glutaraldehyde/paraformaldehyde perfusion. After dissection, demineralization and embedding transverse jaw/incisor segments were cut, reembedded, and reoriented. Sections were prepared for and observed in the transmission electron microscopy (TEM). The intraenamel part of Tomes' process was about 18 microns long. The forming prism occupied a longitudinally grooved invagination on its apical aspect. The parts of Tomes' process forming the side walls of the groove were attenuated and showed variation in extent and outline. Prism growth occurred over the whole grooved area. An estimation of Tomes' process secretory area in rat compared with data from humans suggests that there may be a relationship between secretory area and rate of prism formation. Prism crystals were oriented obliquely or parallel to the secretory surface of Tomes' process. At interprism growth sites matrix deposition was irregular and required some redistribution to conform to the pattern of interprism sheets.

Earlier studies indicate the presence of an insulin-like immunoreactivity (ILI) in rat submandibular salivary glands (SSG). Previous observations also showed that streptozotocin (STZ)-induced diabetes was accompanied by an increase in SSG ILI concentrations. In the present work we studied the effect of SSG ILI from normal and STZ diabetic rats (ILI-N and ILI-D, respectively) on insulin receptor binding and function in LMH cell line. ILI-N and ILI-D inhibited 125I-insulin binding to intact cells and wheat germ agglutinin (WGA)-purified insulin receptors with a high affinity. Furthermore, ILI-N and ILI-D activated, although weakly, the beta-subunit autophosphorylation of solubilized and WGA-purified insulin receptors. An ATP hydrolytic activity was present in ILI-N and, to a greater extent, in ILI-D extracts, which can at least in part explain their low potency for activating autophosphorylation and kinase activity of insulin receptors in vitro. However, after ILI treatment of intact cells and immunoprecipitation of insulin receptors, ILI induced a dose-dependent tyrosine phosphorylation of the insulin receptor beta-subunit. Finally, ILI-N and ILI-D stimulated amino acid uptake and lipogenesis in LMH cells. These findings suggest that SSG ILI is biologically active and can participate in metabolic regulations.

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