Oral mucosal pellicle. Adsorption and transpeptidation of salivary components to buccal epithelial cells.

The present investigation was carried out to examine the mechanism(s) whereby salivary molecules interact with human buccal epithelial cells. By utilizing antiserum against human parotid saliva, selected salivary components were detected by electrophoretic-transfer analysis of 1.5% SDS extracts of epithelial cells. Incubation of the cells and their aqueous cell-free extracts with 125I-labelled parotid saliva resulted in the formation of an iodinated high-molecular-mass complex which was not present in 125I-labelled saline alone. Formation of this complex was time-dependent and was inhibited by treating the buccal epithelial cells or their cell-free extracts with EGTA, iodoacetamide, N-ethylmaleimide or by heating at 100 degrees C for 15 min. The epithelial cells also promoted incorporation of [14C]putrescine into high-molecular-mass complexes whose formation was inhibited by iodoacetamide, unlabelled putrescine and EGTA. Cell extracts mediated cross-linking of monodansylcadaverine into alpha-casein, and this interaction was inhibited by iodoacetamide. Significant amounts of radioactivity were recovered with the epithelial-cell envelopes after exhaustive extraction of 125I-saliva- or [14C]putrescine-treated epithelial cells with 4% (w/v) SDS/10% (v/v) beta-mercaptoethanol. The incorporation of radioactivity into epithelial-cell envelopes was inhibited by pretreatment of the cells with putrescine, EGTA, iodoacetamide, or heating at 100 degrees C for 15 min. These data suggest that: (1) oral mucosal pellicle is formed by the selective adsorption of saliva to the epithelial-cell plasma membrane and its associated cytoskeleton; and (2) the adsorbed salivary components may be cross-linked to each other or the epithelial cytoskeleton by epithelial transglutaminases.