Abstract
We have demonstrated by indirect immunofluorescence that wheat gliadin binds in vitro to reticulin-like fibrils present in cryostat sections of human skin, and rat liver, kidney and stomach. Gliadin was seen to bind to fibrils throughout the dermis of both normal and dermatitis herpetiformis skin, and this was particularly striking in the dermal papillae. Serum from 2 dermatitis herpetiformis patients who did not have antireticulin antibody gave reticulin staining when retested by immunofluorescence on cryostat sections of rat tissue pretreated with gliadin. Gliadin treated sections may prove useful in screening patients with gluten sensitive enteropathy for anti-gliadin antibody. Binding of gliadin to skin sites in dermatitis herpetiformis patients and subsequent deposition of antigliadin antibody at these sites may be involved in the development of skin lesions.
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