Development of a Radioimmunoassay for Triiodothyronine Sulfate

Sj, Eelkman Rooda; Kaptein, Ellen; Loon, van; Tj, Visser

doi:10.1080/15321818808057036

Cited by 39 publications

(3 citation statements)

References 8 publications

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“…To achieve this, the displacement of D% obtained for every bleeding was plotted against the duration of the immunization schedule. This corresponds to Roada et al, who drew the immunoresponse profile curve between the displacement on the Y-axis and the time of each immunization on the Xaxis, and the highest point on the curve was the time of the maximum immunoresponse [22] . The three groups recorded the maximum immunoresponse after 3 weeks following the third booster.…”

Section: Discussionmentioning

confidence: 81%

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Preparation and Evaluation of Primary Reagents for the Radioimmunoassay of Hepatitis B Surface Antigen (HBsAg) for its Diagnosis in Human Sera

Hany,

Shoman,

El Bayomy

et al. 2024

Egyptian Journal of Pure and Applied Science

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Section: Discussionmentioning

confidence: 81%

“…Immunoresponse profile of the individual immunized rabbits with HBsAgs was carried out to keep track of the ideal timing for obtaining the best antibody with the maximum displacement and titer. This was performed by plotting the displacement D% obtained for every bleeding against time duration of the immunization schedule [22] .…”

Section: Immunoresponse Profilementioning

confidence: 99%

Preparation and Evaluation of Primary Reagents for the Radioimmunoassay of Hepatitis B Surface Antigen (HBsAg) for its Diagnosis in Human Sera

Hany,

Shoman,

El Bayomy

et al. 2024

Egyptian Journal of Pure and Applied Science

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“…3,3'-T2S and [ 125 I]-T2S were prepared by the method of Eelkman-Rooda et. al., Mol and Visser [12,13]. T2S was further purified and quantitatively recovered by reverse-phase high-pressure liquid chromatography (HPLC) with a preparative column, as described previously [14,15].…”

Section: T2s Radioimmunoassaymentioning

confidence: 99%

Maternal 3,3’-Diiodothyronine Sulfate Formation from Guinea Pig Placenta Perfused with 3,3’,5-Triodothyronine

Wu¹,

Emerson²,

Tjioe³

et al. 2021

JED

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Objective: Serum 3, 3’,5-triiodothyronine (T3) remains low in near-term fetus to prevent the growing fetus from undue exposure to its active catabolic effect in mammals. The present study was undertaken to gain insight in the role of placenta in T3 metabolism, fetal to maternal transfer of T3, and its metabolites by in situ placenta perfusion with outer-ring labeled [125I]-T3 in pregnant guinea pig, a species showing increased sulfated 3, 3’-diiodothyronine (T2S) levels in maternal serum in late pregnancy (term = 65 days), similarly to humans in pregnancy. Materials and Methods: One-pass placenta perfusions performed on pregnant guinea pigs were studied between 58 - 65 days of gestation. In two separate experiments, the umbilical artery of the guinea pig placenta was perfused in situ at 37°C with outer-ring labeled [125I]-T3. Maternal sera and umbilical effluents were obtained for analysis at the end of a 60-minute perfusion, when the steady-state levels of radioactivity were reached in the placenta effluent after 30-minute. Results: Sulfated [125I]-T2S was readily detected in the maternal serum as the major metabolite of T3 following the perfusion of placenta with [125I]-T3, suggesting that placental inner-ring deiodinase and sulfotransferase may play an important role in fetal T3 homeostasis and in the fetal to maternal transfer of sulfated iodothyronine metabolites. Conclusions: The expression of type 3 deiodinase (D3) and thyroid hormone sulfotransferase activity in placenta may play an important role to protect developing organs against undue exposure to active thyroid hormone in late gestation in the fetus. The combined activities of D3 and sulfotransferase promoted a placental transfer of T2S into maternal circulation. The maternal circulation of T2S is fetal T3 in origin and its role as a fetal thyroid function biomarker deserves further evaluations and studies.

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Halogen Bonding Controls the Regioselectivity of the Deiodination of Thyroid Hormones and their Sulfate Analogues

Manna

Mondal

Mugesh

2014

Chemistry A European J

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The type 1 iodothyronine deiodinase (1D-1) in liver and kidney converts the L-thyroxine (T4), a prohormone, by outer-ring (5') deiodination to biologically active 3,3',5-triiodothyronine (T3) or by inner-ring (5) deiodination to inactive 3,3',5'-triiodothronine (rT3). Sulfate conjugation is an important step in the irreversible inactivation of thyroid hormones. While sulfate conjugation of the phenolic hydroxyl group stimulates the 5-deiodination of T4 and T3, it blocks the 5'-deiodination of T4. We show that thyroxine sulfate (T4S) undergoes faster deiodination as compared to the parent thyroid hormone T4 by synthetic selenium compounds. It is also shown that ID-3 mimics, which are remarkably selective to the inner-ring deiodination of T4 and T3, changes the selectivity completely when T4S is used as a substrate. From the theoretical investigations, it is observed that the strength of halogen bonding increases upon sulfate conjugation, which leads to a change in the regioselectivity of ID-3 mimics towards the deiodination of T4S. It has been shown that these mimics perform both the 5'- and 5-ring deiodinations by an identical mechanism.

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Development of a Radioimmunoassay for Triiodothyronine Sulfate

Cited by 39 publications

References 8 publications

Preparation and Evaluation of Primary Reagents for the Radioimmunoassay of Hepatitis B Surface Antigen (HBsAg) for its Diagnosis in Human Sera

Preparation and Evaluation of Primary Reagents for the Radioimmunoassay of Hepatitis B Surface Antigen (HBsAg) for its Diagnosis in Human Sera

Maternal 3,3’-Diiodothyronine Sulfate Formation from Guinea Pig Placenta Perfused with 3,3’,5-Triodothyronine

Halogen Bonding Controls the Regioselectivity of the Deiodination of Thyroid Hormones and their Sulfate Analogues

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