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Endocrinology, doi:10.1210/endo-113-3-851
Endocrinology Vol. 113, No. 3 851-854
Copyright © 1983 by the Endocrine Society.
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Preincubation of Thyroxine with Sulfhydryl-Reducing Agents Does Not Stimulate Thyroxine Inner or Outer Ring Deiodination*

BARRY L. SHULKIN, ROBERT D. UTIGER, CHARLES H. EMERSON, LEWIS E. BRAVERMAN and MADELEINE FAY

Division of Endocrinology, Department of Medicine, University of North Carolina School of Medicine Chapel Hill, North Carolina 27514;
The Division of Endocrinology and Metabolism, Department Medicine, University of Massachusetts Medical School , Worcester, Massachusetts 01605

Address requests for reprints to: Robert D. Utiger, M.D., Department of Medicine, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27514.

Abstract

Sulfhydryl reagents stimulate enzymatic conversion of T4 to T3 and rT3. A recent study suggested that such reagents stimulated T4 5'-deiodination by a direct interaction with T4. We therefore tested the ability of dithiothreitol (DTT) and other sulfhydryl reagents to enhance the susceptibility of T4 and rT3 to 5'-deiodination by liver homogenates and of T4 to 5- deiodination by placental homogenates. Preincubation of T4 with DTT in concentrations ranging from 0.5–80 mM did not result in increased T3 production from T4 in rat liver homogenates, nor was T3 production increased by preincubation of T4 with reduced glutathione or mercaptoethanol. Preincubation of rT3 with DTT also did not result in increased rT3 degradation by liver homogenates. T4 5-deiodination to rT3 by rat and human placental homogenates was not consistently increased by preincubation of T4 with DTT in concentrations ranging from 2.25– 450 mM. These results do not support the hypothesis that sulfhydryl stimulation of T4 deiodination occurs as a result of sulfhydryl-T4 interaction. (Endocrinology 113: 851,1983)

Footnotes

* Supported by USPHS Grants AM-18919, AM-07302, AM-26112,AM-27850, AM-07129, and RR-46.

Received October 8, 1982.







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Copyright © 1983 by The Endocrine Society