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A 30-yr-old woman with allergic rhinitis and multinodular goiter developed atopic manifestations on different desiccated thyroid extract treatment. Urticaria was observed when the patient was on L-T4 treatment; no atopy was experienced during L-T3 regimen. Serum total immunoglobulin E (IgE) concentration was 390 +/- 7kU/liter (mean +/- SD) prior to any treatment and rose to 850 +/- 7.5 kU/liter when the patient developed urticaria, but declined to baseline figures while she was on L-T3. Intracutaneous testing was positive for desiccated pork thyroid powder, L-T4 and D-T4, but negative for L-T3, DIT and L-tyrosine. Immunoradioligand analyses of mixtures of patient's serum or precipitated immunoglobulin fraction and of 125I-T4 or of 125I-T3 revealed binding of radiolabeled thyroxine to the patient's serum IgE, in turn bound to anti-human-IgE serum covalently coupled to paper discs. This binding was completely inhibited by the preincubation of immunoglobulin fraction with excess unlabeled L-T4 and D-T4, but not with excess nonradioactive L-T3, thus proving the specificity of the binding. Preadsorption experiments performed with desiccated pork thyroid powder solution mixed with the patient's immunoglobulin fraction suggested binding of some unknown component(s) of desiccated thyroid which was apparently not thyroglobulin. This study provides evidence of IgE antibodies to L-T4 cross reacting with D-T4 and capable of binding 125I-T4 in serum. It also suggests a model for the detection of circulating IgE antibodies to thyroid hormones.

Thyroxine-binding globulin (TBG) is the major thyroid hormone carrier protein. The molecule contains approximately 10 sialic acid residues which play a key role in the peripheral metabolism of TBG. Since the serum of patients with liver disease often contains large amounts of several desialylated glycoproteins, the aim of the present studies was to characterize circulating TBG and to examine the possible presence of desialylated TBG (dTBG) in 24 patients with a variety of hepatobiliary diseases and selected on the basis of elevated serum levels of desialylated glycoproteins. Using 4 immunochemical techniques applied for the measurement of TBG, for the detection of dTBG and for the characterization of TBG microheterogeneity, the results indicated: a) a wide scatter of serum TBG levels between 4 and 23 mg/l; b) the absence of detectable amounts of dTBG in any of the sera tested; and c) a close similarity between the microheterogeneity of TBG in patients with liver disease with that of control sera or of purified TBG. In conclusion, in patients with acute and chronic liver disease, TBG, although quantitatively modified, remains qualitatively unaltered, suggesting that diseased liver produces fully sialylated TBG and that its catabolism is not impaired.

Thyroid hormones (TH) elicit a wide variety of metabolic and physiological responses in several tissues of higher organisms. The majority of these effects require the interaction of TH with protein receptors located at the cell nucleus. However, exranuclear actions of TH have elicited growing interest during the last decade. Red blood cells have been shown to possess plasma membrane-binding sites for both T3 and T4. Using this as a cellular model, a direct stimulation of erythrocyte membrane Ca++-dependent ATPase (Ca++-ATPase) by physiological concentrations of TH has recently been demonstrated (1,2). Among TH analogues, T4 exerts the highest stimulatory effect on basal enzyme activity which is not dependent upon prior conversion to T3 (3). This effect of T4 requires the mediation of calmodulin (CaM), an ubiquitous cytosolic protein which plays a major role in the regulation of Ca++-ATPase (4).