Numerous gastrointestinal pathogens have demonstrated molecular mimicry with thyroid tissue. Enzyme-linked immunosorbent assay (ELISA) evaluations have also shown immunological cross-reactivity to play a role in Hashimoto's thyroiditis. Additionally, heat shock protein 60 (Hsp60), a mitochondrial chaperonin involved in stress responses, diabetes, and immunological disorder, has structural similarity to thyroglobulin and thyroid peroxidase molecules. Various antigens have been shown to specifically cross-react with thyroid tissue and trigger thyroid autoimmunity. Įxposure to antigens that share amino acid sequence homology with self-tissue proteins in susceptible hosts has been theorized as a trigger for tissue-specific autoimmune disease. Further study found that cross-reactivity with pollen could also occur to human tissue target proteins. Immunological cross-reactivity was first identified in 1942 when it was found that individuals sensitized to pollen allergens developed immune reactivity to specific fruits. Immunologic cross-reactivity occurs when adaptive immune response against one antigen also occurs to another antigen with amino acid structural similarity. Laboratory analysis of immunological cross-reactivity between thyroid target sites and dietary proteins is the initial step necessary in determining whether dietary proteins may play a potential immunoreactive role in autoimmune thyroid disease. However, specific antigen-antibody immune reactivity was identified with several purified food proteins with triiodothyronine, thyroxine, thyroglobulin, and 5′deiodinase. There were no dietary protein immune reactions with TSH receptor, thyroid peroxidase, and thyroxine-binding globulin. Dietary protein determinants included unmodified (raw) and modified (cooked and roasted) foods, herbs, spices, food gums, brewed beverages, and additives. We also measured immune reactivity of either target specific monoclonal or polyclonal antibodies for thyroid-stimulating hormone (TSH) receptor, 5′deiodinase, thyroid peroxidase, thyroglobulin, thyroxine-binding globulin, thyroxine, and triiodothyronine against 204 purified dietary proteins commonly consumed in cooked and raw forms. We identified immune reactivity between dietary proteins and target sites on the thyroid axis that includes thyroid hormones, thyroid receptors, enzymes, and transport proteins. Our study was designed to investigate the potential role of dietary protein immune reactivity with thyroid hormones and thyroid axis target sites. Additionally, food interactions may play a role in a subset of individuals who have difficulty finding a suitable thyroid hormone dosage. Many hypothyroid and autoimmune thyroid patients experience reactions with specific foods.
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