Immunologic localization of filaggrin in human oral epithelia and correlation with keratinization.

Localization of filaggrin, a human epithelial structural protein, was investigated by indirect-immunofluorescence microscopy of oral mucosa. Thirty specimens were tested, 10 each of palate, gingiva, and buccal mucosa. Orthokeratinized and parakeratinized specimens displayed immunofluorescence within the stratum corneum, stratum granulosum, and upper stratum spinosum. Within the stratum corneum, the reaction was diffuse. Within the stratum granulosum and spinosum, the reaction was in a granular pattern, in a perinuclear position. Several of the nonkeratinized specimens had a negative reaction; however, most displayed a very weak, scattered reaction in a granular pattern within the most superficial cells. The presence of filaggrin in keratinized palate was confirmed by immunoblot studies with the same antibody. Profilaggrin was detectable in representative nonkeratinized and parakeratinized oral tissues, as well as in keratinized palatal epithelium. The localization of filaggrin is consistent with its possible function as the interfilamentous matrix protein within cells of the stratum corneum, and with its derivation from a cross-reactive precursor protein stored in keratohyaline granules. A strong positive correlation was found between the degree of keratinization and the amount of immunofluorescence; therefore, filaggrin and related antigens may be useful and sensitive marker proteins for epithelial keratinization.