E-selectin is an adhesion molecule, expressed by cytokine-activated endothelial cells, that participates in the binding of neutrophils. Recent studies in our laboratory documented binding of the E-selectin-specific monoclonal antibody H4/18 to keratinocytes in inflamed human oral mucosa, particularly gingival epithelium. To determine whether this immunoreactivity was due to expression of authentic E-selectin, the presence of E-selectin mRNA in gingival epithelium was analysed using the polymerase chain reaction (PCR). Reverse transcription of epithelial RNA and amplification of cDNA with E-selectin-specific primers resulted in the formation of a 178 nucleotide PCR product identical to that obtained from cytokine-activated endothelial cells. Sequencing of the PCR product revealed 100% homology between epithelial and endothelial E-selectin fragments. Epithelial preparations did not contain mRNA for von Willebrand factor, excluding the possibility of contamination by endothelial cells. These results confirm immunohistochemical studies of E-selectin immunoreactivity in human oral mucosa and demonstrate that E-selectin expression is not confined to endothelium.