Abstract

The effect of a proline analog, L-azetidine-2-carboxylic acid (LACA), on protein matrix secretion by odontoblasts and ameloblasts was compared by light and electron microscopic radioautography after injection of 3H-glycine in young mice. LACA inhibited the secretion of dentin matrix with consequent accumulation of 3H-glycine labeled procollagen in the cisternae of the rough endoplasmic reticulum. In contrast, LACA had no apparent effect on ameloblasts as enamel matrix continued to be packaged in the Golgi apparatus and secreted from Tomes' process within 30 min after injection of the radioprecursor. Electron microscopy revealed that LACA did not cause any change in ameloblast ultrastructure but produced a marked alteration of the odontoblast Golgi complex. All odontoblast Golgi saccules and collagen secretion granules disappeared within 2 h after LACA administration. Odontoblast Golgi cisternae, however, appeared not to be affected. These observations confirm previous studies conducted in this laboratory showing that Golgi saccules in collagen-secreting cells are the initial staging areas for the formation of secretory granules. These results also indicate that a close correlation exists between form and function in the Golgi apparatus of collagen-secreting cells.

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