Specific interaction of food proteins with apical membranes of the human intestinal cell lines Caco-2 and T84.

A comparison between the intestinal epithelial cell lines Caco-2 and T84 was made to assess the influence of enterocytic differentiation on food protein binding capacities of the brush border membrane. Cell morphology and expression of brush border-associated enzymes were studied as differentiation markers. Food protein binding to isolated brush border membranes was measured with a dot blot chemiluminescence assay. Early at confluence, Caco-2 cells exhibited a more differentiated state compared to T84 cells. Brush border membranes of both cell lines bound gliadin peptides, beta-lactoglobulin and ovalbumin specifically. Binding capacities increased from gliadin peptides to ovalbumin to beta-lactoglobulin. There was correlation of membrane binding capacity with degree of cell differentiation. Due to their similarity to small intestinal epithelial cells, the colon carcinoma cell lines Caco-2 and T84 represent models for studying food protein-enterocytic brush border membrane interactions in relation to varying degrees of cell differentiation.