Abstract

A monospecific and high titer polyclonal antibody, designated as Fas D, raised against synthetic polypeptides selected from a part of the human Fas antigen (aa 104-114), was used to identify the Fas antigen in human oral epithelia in normal and pathological states. The human gingival proteins had been extracted and analysed by an ABC (avidin-biotin complex) immunoblotting technique. The antibody interacted with a single band in gingival proteins with an estimated molecular weight of 35,000, which is in good agreement with that calculated from amino acid sequences of the human Fas antigen. Using an indirect immunohistochemical method, the antibody localized on the stratum spinosum and the basal part of the stratum corneum of normal human gingiva. Specimens obtained from patients with odontogenic keratocysts, leukoplakia, lichen planus, and squamous cell carcinoma were also stained with the antibody. The pattern of the Fas antigen distribution in oral stratified squamous epithelia was, with some overlapping, characteristic for each disease.

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