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Department of Internal Medicine III and Clinical Endocrinology, Medical Faculty, Erasmus University, Rotterdam, The Netherlands
(Received 19 November 1976)
Recently data have suggested that in man the contribution to the overall turnover of thyroxine (T4) of pathways along which this prohormone is converted either into metabolically active 3,3′,5-tri-iodothyronine (T3) or into inactive 3,3′,5′-tri-iodothyronine (reverse T3, rT3) is under physiological control. We describe here the synthesis of [125I]rT3 and the production and characterization of antisera raised against an rT 3-bovine serum albumin (rT3-BSA) conjugate.
3,3′,5′-Tri-iodo-l-thyronine-BSA, prepared essentially according to the method of Olivier, Parker, Brasfield & Parker (1968), l-rT3 and 3,3′-di-iodo-l-thyronine (3,3′-T2) were obtained by courtesy of Dr E. Scheiffele (Henning GmbH., Berlin); l-T4 and l-T3 were purchased from Sigma Chemical Co. (St Louis, Missouri, U.S.A.); 3-iodo-l-tyrosine (MIT) and 3,5-di-iodo-l-tyrosine (DIT) were obtained from Calbiochem AG (Lucerne, Switzerland); Na125I (sp.act. approximately 14 mCi/μg) from The Radiochemical Centre (Amersham) and goat anti-rabbit
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Transport of thyroxine (T(4)) into the liver is inhibited in fasting and by bilirubin, a compound often accumulating in the serum of critically ill patients. We tested the effects of chronic and acute energy deprivation, bilirubin and its precursor biliverdin on the 15-min uptake of [(125)I]tri-iodothyronine ([(125)I]T(3)) and [(125)I]T(4) and on TSH release in rat anterior pituitary cells maintained in primary culture for 3 days. When cells were cultured and incubated in medium without glucose and glutamine to induce chronic energy deprivation, the ATP content was reduced by 45% (P<0. 05) and [(125)I]T(3) uptake by 13% (NS), but TSH release was unaltered. Preincubation (30 min) and incubation (15 min) with 10 microM oligomycin reduced ATP content by 51% (P<0.05) and 53% (P<0. 05) under energy-rich and energy-poor culture conditions respectively; [(125)I]T(3) uptake was reduced by 66% (P<0.05) and 64% (P<0.05). Neither bilirubin nor biliverdin (both 1-200 microM) affected uptake of [(125)I]T(3) or [(125)I]T(4). Bilirubin (1-50 microM) did not alter basal or TRH-induced TSH release. In conclusion, the absence of inhibitory effects of chronic energy deprivation and bilirubin on thyroid hormone uptake by pituitary cells supports the view that the transport is regulated differently than that in the liver.
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The development of a highly sensitive and specific radioimmunoassay for 3,3′-di-iodothyronine (3,3′-T2) is described. The assay was applied to the measurement of 3,3′-T2 in unextracted human serum and used 8-anilino-l-naphthalene-sulphonic acid to inhibit the binding of 3,3′-T2 to serum transport proteins. The lower limit of detection of the assay was 2 fmol 3,3′-T2 per tube, which corresponded to 10 pmol 3,3′-T2/l serum. The mean concentration of 3,3′-T2 in normal serum was found to be 23 pmol/l, which is considerably lower than most values reported previously. Evidence is presented which suggests that the cross-reactivity of tri-iodothyronine with the antiserum to 3,3′-T2 is an important factor in the measurement of serum concentrations of 3,3′-T2 by radioimmunoassay.
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Cellular and nuclear uptake of [125I]tri-iodothyronine (T3) and [125I]triiodothyroacetic acid (Triac) were compared in cardiomyocytes of 2-3 day old rats, and the effect of thyroid hormone analogs on cellular T(3) uptake was measured. Cells (5-10 x 10(5) per well) were cultured in DMEM-M199 with 5% horse serum and 5% FCS. Incubations were performed for from 15 min to 24 h at 37 degrees C in the same medium, 0.5% BSA and [125I]T3 (100 pM), or [125I]Triac (240 pM). Expressed as % dose, T(3) uptake was five times Triac uptake, but expressed as fmol/pM free hormone, Triac uptake was at least 30% (P<0.001) greater than T3 uptake, whereas the relative nuclear binding of the two tracers was comparable. The 15 min uptake of [125I]T3 was competitively inhibited by 10 microM unlabeled T3 (45-52%; P<0.001) or 3,3'- diiodothyronine (T2) (52%; P<0.001), and to a smaller extent by thyroxine (T(4)) (27%; 0.05<0.1). In contrast, 10 microM 3,5-T2, Triac, or tetraiodothyroacetic acid (Tetrac) did not affect T3 uptake after 15 min or after 24 h. Diiodothyropropionic acid (DITPA) (10 microM) reduced 15-min T3 uptake by about 24% (P<0.05), but it had a greater effect after 4 h (56%; P<0.001). Exposure to 10 nM DITPA during culture reduced cellular T3 uptake, as did 10 nM T3, suggesting down-regulation of the plasma membrane T3 transporters. We conclude that i) Triac is taken up by cardiomyocytes; ii) 3,3'-T2 and, to a lesser extent, DITPA and T4 interfere with plasma membrane transport of T3, whereas 3,5-T2, Triac, or Tetrac do not; iii) the transport mechanism for Triac is probably different from that for T3.
