Vitamin A affects epithelial differentiation and growth via at least 3 different binding proteins. The specific delivery of extracellular retinol to target cells is performed by plasma retinol-binding protein (RBP) while cellular retinol- and retinoic acid-binding proteins (CRBP and CRABP) are implicated in the cellular action of the 2 natural retinoids. We have studied the levels of these 3 binding proteins by gel filtration and polyacrylamide electrophoresis in human oral mucosa, epithelium and chorion and compared it to those found in keratinizing human epidermis. The levels of CRABP in oral epithelium were markedly higher (about 4 times) than that of epidermis whereas CRBP was in a similar amount in epithelium chorion, dermis and epidermis. RBP with preserved affinity for retinol, was present in the epithelium of oral mucosa whereas only degraded RBP was detected in epidermis. These results suggest (i) a higher specific retinol delivery and (ii) a distinct cellular metabolism of retinoic acid in the oral epithelium as compared with epidermis. Since cornification occurs when keratinocytes are deprived of retinol, it might be that our observations are linked to the absence of cornification in the human oral mucosa. Further, high levels of CRABP in mucosal epithelium might have therapeutical implications because the synthetic retinoids used in human therapy bind to CRABP.