Triiodothyronine--binding immunoglobulin in a euthyroid patient. 1981

M R Pudek, and H W McIntosh

We describe a clinically euthyroid 60-year old woman with a past history of 1311 therapy for treatment of possible toxic nodular goitre. She had an elevated thyroxine level of 188 microgram/L (normal range 50-125 microgram/L) following her therapy, and her TSH was within normal limits at 4.7 mU/L. However her T3 level, as determined by an RIA technique employing charcoal to separate bound and free T3, was not measurable. T3 added to the patient's serum could not be recovered, therefore the presence of an unusual protein capable of binding T3 was suspected. To avoid this interference, T3 analysis was performed on an ethanol extract of the patient's serum and was found to be 17 microgram/L (normal range 0.8-1.8 microgram/L). At this time her thyroid microsomal antibody titre was 1:100,000. A protein, capable of binding more than 70% of the patient's T3, was demonstrated in the gamma globulin fraction by agarose gel electrophoresis. This protein did not bind T4. Scatchard analysis for T3 binding revealed a protein, presumably IGG, with a binding affinity of 2 x 109 L/mole and binding capacity of 50 microgram/L. This case exemplifies the caution that must be taken in interpreting thyroid function tests. When thyroid hormone levels are inappropriate to the clinical status of the patient the presence of circulating antibodies which can bind the thyroid hormones should be considered.

UI MeSH Term Description Entries
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D011988 Receptors, Thyroid Hormone Specific high affinity binding proteins for THYROID HORMONES in target cells. They are usually found in the nucleus and regulate DNA transcription. These receptors are activated by hormones that leads to transcription, cell differentiation, and growth suppression. Thyroid hormone receptors are encoded by two genes (GENES, ERBA): erbA-alpha and erbA-beta for alpha and beta thyroid hormone receptors, respectively. Diiodotyrosine Receptors,Receptors, Diiodotyrosine,Receptors, Thyroxine,Receptors, Triiodothyronine,T3 Receptors,T4 Receptors,Thyroid Hormone Receptors,Thyroxine Receptors,Triiodothyronine Receptors,DIT Receptors,Diiodotyrosine Receptor,MIT Receptors,Monoiodotyrosine Receptors,Receptors, DIT,Receptors, MIT,Receptors, Monoiodotyrosine,Receptors, T3,Receptors, T4,T3 Receptor,T4 Receptor,Thyroid Hormone Receptor,Thyroxine Receptor
D005188 False Negative Reactions Negative test results in subjects who possess the attribute for which the test is conducted. The labeling of diseased persons as healthy when screening in the detection of disease. (Last, A Dictionary of Epidemiology, 2d ed) False Negative Reaction,Reaction, False Negative,Reactions, False Negative
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000510 Alpha-Globulins Serum proteins that have the most rapid migration during ELECTROPHORESIS. This subgroup of globulins is divided into faster and slower alpha(1)- and alpha(2)-globulins. Alpha-Globulin,Alpha Globulin,Alpha Globulins
D013959 Thyroid Diseases Pathological processes involving the THYROID GLAND. Disease, Thyroid,Diseases, Thyroid,Thyroid Disease
D013974 Thyroxine The major hormone derived from the thyroid gland. Thyroxine is synthesized via the iodination of tyrosines (MONOIODOTYROSINE) and the coupling of iodotyrosines (DIIODOTYROSINE) in the THYROGLOBULIN. Thyroxine is released from thyroglobulin by proteolysis and secreted into the blood. Thyroxine is peripherally deiodinated to form TRIIODOTHYRONINE which exerts a broad spectrum of stimulatory effects on cell metabolism. L-Thyroxine,Levothyroxine,T4 Thyroid Hormone,3,5,3',5'-Tetraiodothyronine,Berlthyrox,Dexnon,Eferox,Eltroxin,Eltroxine,Euthyrox,Eutirox,L-3,5,3',5'-Tetraiodothyronine,L-Thyrox,L-Thyroxin Henning,L-Thyroxin beta,L-Thyroxine Roche,Levo-T,Levothroid,Levothyroid,Levothyroxin Deladande,Levothyroxin Delalande,Levothyroxine Sodium,Levoxine,Levoxyl,Lévothyrox,Novothyral,Novothyrox,O-(4-Hydroxy-3,5-diiodophenyl) 3,5-diiodo-L-tyrosine,O-(4-Hydroxy-3,5-diiodophenyl)-3,5-diiodotyrosine,Oroxine,Sodium Levothyroxine,Synthroid,Synthrox,Thevier,Thyrax,Thyroxin,Tiroidine,Tiroxina Leo,Unithroid,L Thyrox,L Thyroxin Henning,L Thyroxin beta,L Thyroxine,L Thyroxine Roche,Levo T,Thyroid Hormone, T4

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