SUMMARY Brush cells occur in the epithelium of the small intestine and in various other epithelia of endodermal origin. Ultrastructural and histochemical characteristics suggest that they represent sensory cells. Because the apical membrane of brush cells might be involved in and specialized for (chemo-)receptive functions, we investigated the composition of the glycocalyx and compared it with that of enterocytes. Ultrathin sections of murine small intestine were labeled with a panel of eight lectins. Their binding sites in the brush border and on vesicles of the apical cytoplasm were detected by colloidal gold and quantified using image analysis. The glycocalyx of brush cells contained significantly higher amounts of L -fucose residues than that of enterocytes, as detected by the lectins UEA-I and LTA. In contrast, most of the other lectins bound more avidly to the glycocalyx of enterocytes. The cytoplasmic vesicles closely resembled the apical membrane in their labeling pattern. Quantitation of the brush cells' distribution revealed that the epithelia of the Peyer's patches contained 10-fold higher numbers of brush cells than the small intestinal mucosa distant from lymphoid tissue. We conclude that brush cells possess a glycocalyx with a specialized composition and differ significantly from enterocytes. Because similar peculiarities of the apical membrane have previously been described for sensory cells of the olfactory and gustatory organs, this study provides further evidence in favor of a sensory function of brush cells.

Brush cells are specialised epithelial cells that are assumed to represent chemoreceptors of the digestive tract. They comprise a small population of the epithelial cells lining the intestine, possess a unique ultrastructure and, in many aspects, resemble the receptor cells of taste buds. To characterise glycoconjugates possibly involved in a sensory function, we investigated brush cells in the small intestine of three species using lectin histochemistry in confocal light and thin-section electron microscopy. Brush cells of rats were selectively labelled by the sialic acid-specific lectin Maackia amurensis agglutinin, those of guinea-pigs by the D-galactose-specific lectin Bandeiraea simplicifolia agglutinin, isolectin B 4 and those of mice by the L-fucose-specific lectin Ulex europaeus agglutinin lectin I. Lectin binding sites were consistently located in the glycocalyx of the apical membrane and in that of cytoplasmic vesicles. In vivo lectin labelling revealed that the glycoconjugates of the apical membrane are accessible under physiological conditions, that brush cells do not endocytose and that they probably possess a high membrane turnover rate. The results show that specialisations exist in the composition of glycoconjugates forming the glycocalyx of brush cells in all species investigated. The presence of brush cell-specific glycoconjugates would be in accordance with the current hypothesis of a receptive function of brush cells. Differences in the specific glycosylation patterns among rats, guinea-pigs and mice indicate that species-specific adaptations exist.

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