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Journal articles on the topic 'Iodotyrosine'

Author: Grafiati

Published: 14 March 2023

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1

Nasu, Michiyo, and Masahiro Sugawara. "Exogenous free iodotyrosine inhibits iodide transport through the sequential intracellular events." European Journal of Endocrinology 130, no. 6 (June 1994): 601–7. http://dx.doi.org/10.1530/eje.0.1300601.

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Nasu M, Sugawara M. Exogenous free iodotyrosine inhibits iodide transport through the sequential intracellular events. Eur J Endocrinol 1944;130:601–7. ISSN 0804–4643 We describe a new function of exogenous iodotyrosine as a regulator of iodide transport. Porcine thyroid follicles in culture were preincubated with 0–20 μmol/l monoiodotyrosine or diiodotyrosine (DIT) in the presence of bovine thyrotropin (TSH) for 24 h; these iodotyrosines inhibited iodide uptake in a dose–response manner. Extracellular [125I]DIT was actively transported to the thyroid follicle in the presence of TSH or (Bu)2cAMP. Inhibition of iodide uptake by iodotyrosine required preincubation with iodotyrosine in the presence of TSH; without TSH, iodotyrosine was ineffective. Follicles preincubated with DIT for 24 h inhibited TSH-mediated cAMP production, which is an important signal for iodide transport. Inhibition of iodide uptake and cAMP generation by iodotyrosine was negated characteristically by 3-nitro-l-tyrosine, an inhibitor of iodotyrosine deiodinase, or by methimazole, an inhibitor of thyroid peroxidase. Our findings suggest that iodotyrosine regulates iodide transport through the following sequential intracellular events: TSH-dependent iodotyrosine transport into the thyroid cell; deiodination of iodotyrosine and release in iodide; iodine organification by the peroxidase system; inhibition of cAMP generation by organified iodine; and inhibition of iodide transport. Thus, exogenous iodotyrosine can serve as an inhibitor of thyroid hormone formation only when TSH is present M Sugawara, Wadsworth VA Hospital (11 IM), Wilshire and Sawtelle Blvds, Los Angeles, CA 90073, USA

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2

De, Swapan K., Chayan K. Ganguly, Tapan K. Chakraborty, Arya K. Bose, and Ranajit K. Banerjee. "Endocrine control of extrathyroidal peroxidases and iodide metabolism." Acta Endocrinologica 110, no. 3 (November 1985): 383–87. http://dx.doi.org/10.1530/acta.0.1100383.

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Abstract. The role of the thyroid and adrenal glands on iodide transport and peroxidase-catalyzed formation of iodotyrosines in extrathyroidal tissues such as stomach and submaxillary glands has been investigated. Thyroidectomy stimulates iodide concentration and iodotyrosine formation in stomach, sensitive to the administration of thyroxine but having no effect on the peroxidase activity. In contrast, although thyroidectomy stimulates the submaxillary peroxidase which is reversed on treatment with thyroxine, it has no effect on iodide concentration and organification in the submaxillary gland. Gastric peroxidase activity is specifically stimulated by adrenalectomy and is inhibited by glucocorticoids which also inhibit iodotyrosine formation in stomach.

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3

Bolshakova, Larisa, and Dmitry Lukin. "Absorption of iodotyrosine from iodized milk protein in animals." Foods and Raw Materials 8, no. 1 (February 26, 2020): 60–66. http://dx.doi.org/10.21603/2308-4057-2020-1-60-66.

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Introduction. One of the ways to the solve iodine deficiency problem is the addition of iodine to farm animal feed. It allows producing iodized livestock products. Promising sources of organic iodine are iodotyrosine-containing iodized milk proteins. Organic iodine accumulation in organs and tissues has not been sufficiently studied. Study objects and methods. We determined iodotyrosine content in rat blood plasma and in pig muscle tissue. For this purpose, high performance liquid chromatography with mass spectrometric detection and cathodic stripping voltammetry were used. Results and discussion. At the first stage of the study, we examined iodotyrosines in rat blood plasma after a single administration of iodized milk protein or potassium iodide (30 μg I/kg weight) at specific time intervals. A significant increase in the concentration of monoiodotyrosine and diiodotyrosine was recorded 4 and 24 h after the administration. At the second stage, we studied the accumulation of iodotyrosines in the muscle tissue of pigs during their fattening period (104 days). The diet of the control animal group included potassium iodide (0.6 mg I/kg of feed). The experimental groups A and B got iodized milk protein (0.3 and 0.6 mg I/kg of feed, respectively). Monoiodotyrosin content in the muscle tissue of pigs of the experimental groups was 3.0 and 5.2 times higher than that in the control group. Diiodotyrosine content was 4.9 and 8.2 times higher. In the experimental group A, iodine content in muscle tissues was 26% higher than that in the control group, in the experimental group B it was 72% higher. Calculations of iodine intake balance and its accumulation in muscle tissues showed that in animals whose diet included iodized milk protein, the iodine assimilation was much higher (0.70 and 0.53%) than in the control group (0.21%). Conclusion. Iodotyrosines from iodized milk protein are absorbed by the gastrointestinal tract in an unchanged form and accumulate in muscle tissues. The findings give more clear understanding of physiological and biochemical mechanisms of organic iodine absorption in animals.

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4

Aon, M. A., and J. A. Curtino. "Protein-bound glycogen is linked to tyrosine residues." Biochemical Journal 229, no. 1 (July 1, 1985): 269–72. http://dx.doi.org/10.1042/bj2290269.

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Tyrosine-glycogen obtained from retina proteoglycogen by exhaustive proteolytic digestion was radiolabelled with 125I. The 125I-labelled tyrosine-glycogen was degraded by amylolytic digestion to a very small radioactive product, which was identified as iodotyrosine by h.p.l.c. The amylolytic mixture used released glucose and maltose that were alpha-linked to the phenolic hydroxy group of p-nitrophenol. No free iodotyrosine was found before or after the intact [125I]iodotyrosine-glycogen was subjected to two cycles of the Edman degradation procedure. The linkage between protein and glycogen was alkali-stable. Therefore it is concluded that the protein-bound glycogen was O-glycosidically linked to the phenolic hydroxy group of tyrosine. The amino acid has not been heretofore found to be involved in the linkage of carbohydrates to proteins.

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5

Hu, Jimin, Qi Su, Jamie L. Schlessman, and Steven E. Rokita. "Redox control of iodotyrosine deiodinase." Protein Science 28, no. 1 (October 17, 2018): 68–78. http://dx.doi.org/10.1002/pro.3479.

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6

Solis-S, JC, P. Villalobos, A. Orozco, and C. Valverde-R. "Comparative kinetic characterization of rat thyroid iodotyrosine dehalogenase and iodothyronine deiodinase type 1." Journal of Endocrinology 181, no. 3 (June 1, 2004): 385–92. http://dx.doi.org/10.1677/joe.0.1810385.

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The initial characterization of a thyroid iodotyrosine dehalogenase (tDh), which deiodinates mono-iodotyrosine and di-iodotyrosine, was made almost 50 years ago, but little is known about its catalytic and kinetic properties. A distinct group of dehalogenases, the so-called iodothyronine deiodinases (IDs), that specifically remove iodine atoms from iodothyronines were subsequently discovered and have been extensively characterized. Iodothyronine deiodinase type 1 (ID1) is highly expressed in the rat thyroid gland, but the co-expression in this tissue of the two different dehalogenating enzymes has not yet been clearly defined. This work compares and contrasts the kinetic properties of tDh and ID1 in the rat thyroid gland. Differential affinities for substrates, cofactors and inhibitors distinguish the two activities, and a reaction mechanism for tDh is proposed. The results reported here support the view that the rat thyroid gland has a distinctive set of dehalogenases specialized in iodine metabolism.

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7

Ohmori, T., O. Tarutani, and T. Hosoya. "Improved assay method for activity of thyroid peroxidase-catalysed coupling of iodotyrosine residues of thyroglobulin utilizing h.p.l.c. for analysis of iodothyronines." Biochemical Journal 262, no. 1 (August 15, 1989): 209–14. http://dx.doi.org/10.1042/bj2620209.

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The coupling of iodotyrosine residues of thyroglobulin (Tg) catalysed by thyroid peroxidase (TPO) has scarcely been studied with respect to the TPO of abnormal human thyroid glands. The present paper proposes a rapid and convenient assay method applicable for determining the coupling activity of a sample of less than 500 mg from each patient's thyroid. The main characteristics of the method are as follows: (i) mitochondrial/microsomal fractions of thyroid glands were treated with sodium cholate plus trypsin, and the supernatants obtained by ultracentrifugation were directly used for the assay of coupling and peroxidase activity of TPO; (ii) the formation of iodotyrosine residues catalysed by TPO was performed by using chemically iodinated Graves'-disease Tg containing 41 iodine atoms per molecule and with a high iodotyrosine and a low iodothyronine content; (iii) newly synthesized iodothyronine residues (thyroxine, 3,5,3′-tri-iodothyronine, and 3,3′,5′-tri-iodothyronine) were analysed by h.p.l.c. after hydrolysis of Tg with proteinases and extraction of iodothyronines with ethyl acetate.

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8

Errington, Neil, Stephen E. Harding, Lisbeth Illum, and Etienne H. Schacht. "Physico-chemical studies on di-iodotyrosine dextran." Carbohydrate Polymers 18, no. 4 (January 1992): 289–94. http://dx.doi.org/10.1016/0144-8617(92)90094-7.

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9

Watson, James A., Patrick M. McTamney, Jennifer M. Adler, and Steven E. Rokita. "Flavoprotein Iodotyrosine Deiodinase Functions without Cysteine Residues." ChemBioChem 9, no. 4 (March 3, 2008): 504–6. http://dx.doi.org/10.1002/cbic.200700562.

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10

Schott, M. "Mutations in the Iodotyrosine Deiodinase Gene and Hypothyroidism." Yearbook of Medicine 2008 (January 2008): 541–43. http://dx.doi.org/10.1016/s0084-3873(08)79307-6.

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11

Burniat, Agnès, Isabelle Pirson, Catheline Vilain, Willem Kulik, Gijs Afink, Rodrigo Moreno-Reyes, Bernard Corvilain, and Marc Abramowicz. "Iodotyrosine Deiodinase Defect Identified via Genome-Wide Approach." Journal of Clinical Endocrinology & Metabolism 97, no. 7 (July 2012): E1276—E1283. http://dx.doi.org/10.1210/jc.2011-3314.

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12

Moreno, José C., Willem Klootwijk, Hans van Toor, Graziella Pinto, Mariella D'Alessandro, Aubène Lèger, David Goudie, Michel Polak, Annette Grüters, and Theo J. Visser. "Mutations in the Iodotyrosine Deiodinase Gene and Hypothyroidism." New England Journal of Medicine 358, no. 17 (April 24, 2008): 1811–18. http://dx.doi.org/10.1056/nejmoa0706819.

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13

Hendrickson, T. L. "Proofreading optimizes iodotyrosine insertion into the genetic code." Proceedings of the National Academy of Sciences 105, no. 37 (September 10, 2008): 13699–700. http://dx.doi.org/10.1073/pnas.0807442105.

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14

Schott, M. "Mutations in the Iodotyrosine Deiodinase Gene and Hypothyroidism." Yearbook of Endocrinology 2008 (January 2008): 184–86. http://dx.doi.org/10.1016/s0084-3741(08)79032-2.

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15

Das, Tomi Nath. "Redox Chemistry of 3-Iodotyrosine in Aqueous Medium." Journal of Physical Chemistry A 102, no. 2 (January 1998): 426–33. http://dx.doi.org/10.1021/jp9716344.

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16

Phatarphekar, Abhishek, and Steven E. Rokita. "Functional analysis of iodotyrosine deiodinase from drosophila melanogaster." Protein Science 25, no. 12 (September 26, 2016): 2187–95. http://dx.doi.org/10.1002/pro.3044.

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17

Nlend, Marie-Christine, David M. Cauvi, Nicole Venot, and Odile Chabaud. "Role of Sulfated Tyrosines of Thyroglobulin in Thyroid Hormonosynthesis." Endocrinology 146, no. 11 (November 1, 2005): 4834–43. http://dx.doi.org/10.1210/en.2005-0197.

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Our previous studies showed that sulfated tyrosines (Tyr-S) are involved in thyroid hormone synthesis and that Tyr5, the main hormonogenic site of thyroglobulin (Tg), is sulfated. In the present paper, we studied the role of Tyr-S in the formation and activity of the peroxidase-Tg complex. Results show that noniodinated 35SO3-Tg specifically binds (Kd = 1.758 μm) to immobilized lactoperoxidase (LPO) via Tyr-S linkage by using saturation binding and competition experiments. We found that NIFEY-S, a 15-amino acid peptide corresponding to the NH2-end sequence of Tg and containing the hormonogenic acceptor Tyr5-S, was a better competitor than cholecystokinin and Tyr-S. 35SO3-Tg, iodinated without peroxidase, bound to LPO with a Kd (1.668 μm) similar to that of noniodinated Tg, suggesting that 1) its binding occurs via Tyr-S linkage and 2) Tyr-S requires peroxidase to be iodinated, whereas nonsulfated Tyr does not. Iodination of NIFEY-S with [125I]iodide showed that Tyr5-S iodination increased with LPO concentration, whereas iodination of a nonsulfated peptide containing the donor Tyr130 was barely dependent on LPO concentration. Enzymatic hydrolysis of iodinated Tg or NIFEY-S showed that the amounts of sulfated iodotyrosines also depended on LPO amount. Sulfated iodotyrosines were detectable in the enzyme-substrate complex, suggesting they have a short life before the coupling reaction occurs. Our data suggest that after Tyr-S binding to peroxidase where it is iodinated, the sulfate group is removed, releasing an iodophenoxy anion available for coupling with an iodotyrosine donor.

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18

Han, Kyung Ho, Britni M. Arlian, Chih-Wei Lin, Hyun Yong Jin, Geun-Hyung Kang, Sahmin Lee, Peter Chang-Whan Lee, and Richard A. Lerner. "Agonist Antibody Converts Stem Cells into Migrating Brown Adipocyte-Like Cells in Heart." Cells 9, no. 1 (January 20, 2020): 256. http://dx.doi.org/10.3390/cells9010256.

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We present data showing that Iodotyrosine Deiodinase (IYD) is a dual-function enzyme acting as a catalyst in metabolism and a receptor for cooperative stem cell differentiation. IYD is present both in thyroid cells where it is critical for scavenging iodine from halogenated by-products of thyroid hormone production and on hematopoietic stem cells. To close the cooperative loop, the mono- and di-Iodotyrosine (MIT and DIT) substrates of IYD in the thyroid are also agonists for IYD now acting as a receptor on bone marrow stem cells. While studying intracellular combinatorial antibody libraries, we discovered an agonist antibody, H3 Ab, of which the target is the enzyme IYD. When agonized by H3 Ab, IYD expressed on stem cells induces differentiation of the cells into brown adipocyte-like cells, which selectively migrate to mouse heart tissue. H3 Ab also binds to IYD expressed on human myocardium. Thus, one has a single enzyme acting in different ways on different cells for the cooperative purpose of enhancing thermogenesis or of regenerating damaged heart tissue.

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19

Kopp, Peter A. "Reduce, Recycle, Reuse — Iodotyrosine Deiodinase in Thyroid Iodide Metabolism." New England Journal of Medicine 358, no. 17 (April 24, 2008): 1856–59. http://dx.doi.org/10.1056/nejme0802188.

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20

Sun, Zuodong, Qi Su, and Steven E. Rokita. "The distribution and mechanism of iodotyrosine deiodinase defied expectations." Archives of Biochemistry and Biophysics 632 (October 2017): 77–87. http://dx.doi.org/10.1016/j.abb.2017.07.019.

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21

SUGAWARA, MASAHIRO. "Coupling of Iodotyrosine Catalyzed by Human Thyroid Peroxidase in Vitro*." Journal of Clinical Endocrinology & Metabolism 60, no. 6 (June 1985): 1069–75. http://dx.doi.org/10.1210/jcem-60-6-1069.

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22

Mathi, Anupama A., Tekchand C. Gaupale, Corinne Dupuy, Nishikant Subhedar, and Shobha Bhargava. "Expression pattern of iodotyrosine dehalogenase 1 (DEHAL1) during chick ontogeny." International Journal of Developmental Biology 54, no. 10 (2010): 1501–6. http://dx.doi.org/10.1387/ijdb.092932am.

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23

Afink, Gijs, Willem Kulik, Henk Overmars, Janine de Randamie, Truus Veenboer, Arno van Cruchten, Margarita Craen, and Carrie Ris-Stalpers. "Molecular Characterization of Iodotyrosine Dehalogenase Deficiency in Patients with Hypothyroidism." Journal of Clinical Endocrinology & Metabolism 93, no. 12 (December 1, 2008): 4894–901. http://dx.doi.org/10.1210/jc.2008-0865.

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24

Sun, Zuodong, and Steven E. Rokita. "Toward a Halophenol Dehalogenase from Iodotyrosine Deiodinase via Computational Design." ACS Catalysis 8, no. 12 (November 7, 2018): 11783–93. http://dx.doi.org/10.1021/acscatal.8b03587.

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25

Farah, K., and N. Farouk. "Copper catalyzed radioiodination of 3-iodotyrosine and 4-iodophenyl alanine." Journal of Labelled Compounds and Radiopharmaceuticals 39, no. 11 (November 1997): 915–26. http://dx.doi.org/10.1002/(sici)1099-1344(199711)39:11<915::aid-jlcr42>3.0.co;2-o.

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26

Salter, A. M., M. Bugaut, J. Saxton, S. C. Fisher, and D. N. Brindley. "Effects of preincubation of primary monolayer cultures of rat hepatocytes with low- and high-density lipoproteins on the subsequent binding and metabolism of human low-density lipoprotein." Biochemical Journal 247, no. 1 (October 1, 1987): 79–84. http://dx.doi.org/10.1042/bj2470079.

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1. There are two distinct binding sites (Site 1 and Site 2) for human low-density lipoprotein (LDL) on rat hepatocytes in monolayer culture [Salter, Saxton & Brindley (1986) Biochem. J. 240, 549-557]. 2. Binding of 125I-LDL to Site 1, but not to Site 2, is up-regulated between 20 and 44 h in culture by preincubation of the cells with human high-density lipoprotein 3 (HDL3). 3. A similar preincubation with HDL2 had no significant effect on binding to either site. 4. Preincubation with human LDL led to a partial down-regulation of subsequent binding of 125I-LDL to Site 1. Since binding after incubation with LDL was measured at 37 degrees C, binding to Site 2 could not be distinguished from LDL that had been internalized by the cells. 5. Hepatocytes were shown to degrade 125I-LDL, resulting in the accumulation of [125I]iodotyrosine in the medium. Evidence was found that iodotyrosine may be further degraded by deiodinase produced by the cells. 6. Regulation of binding to Site 1 by preincubation with LDL or HDL3 was found to lead to a parallel regulation of LDL degradation. 7. It is concluded that rat hepatocytes not only bind but also metabolize human LDL and that these processes are under metabolic regulation.

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27

Fujimoto, Kenta, Kazuo Matsuura, Biswajit Das, Liezhen Fu, and Yun-Bo Shi. "Direct Activation of Xenopus Iodotyrosine Deiodinase by Thyroid Hormone Receptor in the Remodeling Intestine during Amphibian Metamorphosis." Endocrinology 153, no. 10 (October 1, 2012): 5082–89. http://dx.doi.org/10.1210/en.2012-1308.

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Abstract Thyroid hormone (TH) plays critical roles during vertebrate postembryonic development. TH production in the thyroid involves incorporating inorganic iodide into thyroglobulin. The expression of iodotyrosine deiodinase (IYD; also known as iodotyrosine dehalogenase 1) in the thyroid gland ensures efficient recycling of iodine from the byproducts of TH biosynthesis: 3′-monoiodotyrosine and 3′, 5′-diiodotyrosine. Interestingly, IYD is known to be expressed in other organs in adult mammals, suggesting iodine recycling outside the thyroid. On the other hand, the developmental role of iodine recycling has yet to be investigated. Here, using intestinal metamorphosis as a model, we discovered that the Xenopus tropicalis IYD gene is strongly up-regulated by TH during metamorphosis in the intestine but not the tail. We further demonstrated that this induction was one of the earliest events during intestinal metamorphosis, with IYD being activated directly through the binding of liganded TH receptors to a TH response element in the IYD promoter region. Because iodide is mainly taken up from the diet in the intestine and the tadpole stops feeding during metamorphosis when the intestine is being remodeled, our findings suggest that IYD transcription is activated by liganded TH receptors early during intestinal remodeling to ensure efficient iodine recycling at the climax of metamorphosis when highest levels of TH are needed for the proper transformations of different organs.

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28

TAKASUGI, Noboru, Taisen IGUCHI, Minoru TAKASE, and Toshiharu TAKEI. "Regression of mammary and adrenocortical tumors transplanted into iodotyrosine-pretreated mice." Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 62, no. 7 (1986): 252–56. http://dx.doi.org/10.2183/pjab.62.252.

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29

Banerjee, R. K., A. K. Bose, T. K. Chakraborty, S. K. De, and A. G. Datta. "Peroxidase-catalysed iodotyrosine formation in dispersed cells of mouse extrathyroidal tissues." Journal of Endocrinology 106, no. 2 (August 1985): 159–65. http://dx.doi.org/10.1677/joe.0.1060159.

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ABSTRACT A method has been developed for the isolation of cells, high in iodine uptake and peroxidase activity, from the stomach and submaxillary gland of mice. The isolated cells could produce protein-bound monoiodotyrosine, di-iodotyrosine and an unknown iodocompound. The reactions were catalysed by peroxidase and were sensitive to antithyroid drugs and haemoprotein inhibitors but were insensitive to TSH. In-vitro iodination of stomach or submaxillary soluble proteins with the respective peroxidase yielded similar iodocompounds while thyroxine was produced when thyroglobulin was used instead. J. Endocr. (1985) 106, 159–165

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30

Bobyk, Kostyantyn D., David P. Ballou, and Steven E. Rokita. "Rapid Kinetics of Dehalogenation Promoted by Iodotyrosine Deiodinase from Human Thyroid." Biochemistry 54, no. 29 (July 20, 2015): 4487–94. http://dx.doi.org/10.1021/acs.biochem.5b00410.

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31

Phatarphekar, Abhishek, Jennifer M. Buss, and Steven E. Rokita. "Iodotyrosine deiodinase: a unique flavoprotein present in organisms of diverse phyla." Mol. BioSyst. 10, no. 1 (2014): 86–92. http://dx.doi.org/10.1039/c3mb70398c.

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32

Rao, R. K., W. Thornburg, M. Korc, L. M. Matrisian, B. E. Magun, and O. Koldovsky. "Processing of epidermal growth factor by suckling and adult rat intestinal cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 250, no. 6 (June 1, 1986): G850—G855. http://dx.doi.org/10.1152/ajpgi.1986.250.6.g850.

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Preparations of intestinal villus and crypt cells were isolated from jejunal segments of suckling (14-day-old) and adult (6- to 7-wk-old) rats. These cell preparations were incubated with 125I-labeled epidermal growth factor (EGF) at 37 degrees C to determine the extent of cellular processing of 125I-EGF in vitro. 125I-EGF bound specifically to both crypt and villus cells of suckling rats and was internalized and degraded to similar extents in both cell preparations. Analysis of the 125I radioactivity in the medium and cellular extract by gel filtration on Sephadex G-25 columns demonstrated the presence of [125I]iodotyrosine (24–31%) following 30 min of incubation. This degradation of EGF was accompanied by a loss in the capacity to bind to anti-EGF antibodies (34–52%) and A431 cells (28–48%). Binding, internalization, and processing of 125I-EGF by crypt cell preparations of adult rats was similar to that of suckling rats. In contrast, little degradation of 125I-EGF to iodotyrosine and loss of cell binding capability occurred following incubation with adult villus cells. However, a considerable loss in binding to anti-EGF antibody was detected (48%). The results indicate that isolated intestinal cells are capable of degrading 125I-EGF in vitro in a manner similar to that seen after oral feeding in vivo. They also indicate differences in the processing of 125I-EGF by isolated villus cells of adult compared with suckling rat.

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33

Brown, N. F., A. M. Salter, R. Fears, and D. N. Brindley. "Glucagon, cyclic AMP and adrenaline stimulate the degradation of low-density lipoprotein by cultured rat hepatocytes." Biochemical Journal 262, no. 2 (September 1, 1989): 425–29. http://dx.doi.org/10.1042/bj2620425.

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Rat hepatocytes were preincubated for 16 h with hormones or drugs and then for a further 8 h with 125I-human low-density lipoprotein (LDL). Glucagon (via cyclic AMP) and adrenaline (via cyclic AMP and alpha-effects) increased the binding of 125I-LDL to the LDL receptor, and the degradation of LDL to [125I]iodotyrosine. The effects on degradation were antagonized by dexamethasone, and the action of cyclic AMP on binding and degradation was inhibited by actinomycin D. The results are discussed in relation to the control of lipoprotein metabolism in diabetes.

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34

Obaid, A., S. Basahl, A. Diefallah, and R. Abu-Eittah. "Spectral Investigations of the Effects of 60Co-Gamma Irradiation on Iodothyronine and Iodotyrosines." Applied Spectroscopy 41, no. 1 (January 1987): 74–79. http://dx.doi.org/10.1366/0003702874867918.

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Solids of 3-iodo-, 3–5–di-iodotyrosine and 3,5-di-iodothyronine were irradiated by 60Co-gamma irradiation for a period of about twenty hours. The effects of irradiation were investigated through a study of the UV and IR spectra of irradiated samples. UV spectra showed the presence of a new band at 360 nm which was assigned to the formation of IO−. IR spectra showed a strong carbonyl absorption and the removal of the carboxylate band in the case of thyronine only. For comparison, the spectra of the studied compounds were investigated before irradiation.

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35

Yoshihara, Aya, Yuqian Luo, Yuko Ishido, Kensei Usukura, Kenzaburo Oda, Mariko Sue, Akira Kawashima, Naoki Hiroi, and Koichi Suzuki. "Inhibitory effects of methimazole and propylthiouracil on iodotyrosine deiodinase 1 in thyrocytes." Endocrine Journal 66, no. 4 (2019): 349–57. http://dx.doi.org/10.1507/endocrj.ej18-0380.

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36

Ingavat, Nattha, Jennifer M. Kavran, Zuodong Sun, and Steven E. Rokita. "Active Site Binding Is Not Sufficient for Reductive Deiodination by Iodotyrosine Deiodinase." Biochemistry 56, no. 8 (February 16, 2017): 1130–39. http://dx.doi.org/10.1021/acs.biochem.6b01308.

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37

Shimizu, Ryo, Masafumi Yamaguchi, Naoto Uramaru, Hiroaki Kuroki, Shigeru Ohta, Shigeyuki Kitamura, and Kazumi Sugihara. "Structure–activity relationships of 44 halogenated compounds for iodotyrosine deiodinase-inhibitory activity." Toxicology 314, no. 1 (December 2013): 22–29. http://dx.doi.org/10.1016/j.tox.2013.08.017.

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38

Kőhidai, L., N. Schiess, and G. Csaba. "Chemotactic selection of Tetrahymena pyriformis GL induced with histamine, di-iodotyrosine or insulin." Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology 126, no. 1 (May 2000): 1–9. http://dx.doi.org/10.1016/s0742-8413(00)00088-8.

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Hutton, Craig A., and Ojia Skaff. "A convenient preparation of dityrosine via Miyaura borylation–Suzuki coupling of iodotyrosine derivatives." Tetrahedron Letters 44, no. 26 (June 2003): 4895–98. http://dx.doi.org/10.1016/s0040-4039(03)01081-5.

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40

Olker, Jennifer H., Joseph J. Korte, Jeffrey S. Denny, Jonathan T. Haselman, Phillip C. Hartig, Mary C. Cardon, Michael W. Hornung, and Sigmund J. Degitz. "In vitro screening for chemical inhibition of the iodide recycling enzyme, iodotyrosine deiodinase." Toxicology in Vitro 71 (March 2021): 105073. http://dx.doi.org/10.1016/j.tiv.2020.105073.

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41

Garrigues, A. M., F. Gehelmann, J. M. Girault, M. Delaage, and J. Labouesse. "Haloperidol-succinylglycyl[125 I]iodotyrosine, a novel iodinated ligand for dopamine D2 receptors." FEBS Letters 224, no. 2 (November 30, 1987): 267–71. http://dx.doi.org/10.1016/0014-5793(87)80467-2.

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42

Steer, Andrew M., Hannah L. Bolt, William D. G. Brittain, and Steven L. Cobb. "A direct route for the preparation of Fmoc/O t Bu protected iodotyrosine." Tetrahedron Letters 59, no. 27 (July 2018): 2644–46. http://dx.doi.org/10.1016/j.tetlet.2018.05.061.

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43

Iglesias, Ainhoa, Laura García-Nimo, José A. Cocho de Juan, and José C. Moreno. "Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects." Best Practice & Research Clinical Endocrinology & Metabolism 28, no. 2 (March 2014): 151–59. http://dx.doi.org/10.1016/j.beem.2013.10.009.

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Bagchi, N., and T. R. Brown. "Repeated thyrotrophin stimulation of thyroid secretion: lack of refractoriness in vivo." Journal of Endocrinology 106, no. 2 (August 1985): 153–57. http://dx.doi.org/10.1677/joe.0.1060153.

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ABSTRACT It has been reported that prior exposure of thyroid tissue to TSH in vitro induces a state of refractoriness to new challenges of the hormone. We have investigated the effect of repeated TSH treatment on thyroid secretion to determine whether such refractoriness exists in vivo. The rate of thyroid secretion was estimated by measuring the rate of hydrolysis of labelled thyroglobulin from mouse thyroid glands in vitro. The thyroid glands were labelled in vivo with 131I and then cultured for 20 h in the presence of mononitrotyrosine, an inhibitor of iodotyrosine deiodinase. The rate of hydrolysis of labelled thyroglobulin was measured as the percentage of radioactivity released as free iodotyrosines and iodothyronines into the gland and the medium at the end of incubation. Thyrotrophin was administered in vivo at hourly intervals for 2–4 injections. The corresponding control group received saline injections every hour except for the last injection when they received TSH. The peak rates of thyroglobulin hydrolysis, measured 2 h following the last injection, were similar in animals receiving two, three or four TSH injections and were not different from those in the control groups. Serum tri-iodothyronine and thyroxine concentrations 2 h after the last injection were higher in the groups receiving multiple TSH injections. Thyroidal cyclic AMP accumulation in response to TSH was markedly depressed in the group receiving multiple injections compared with the group receiving a single injection of TSH in vivo. These data indicate that (1) the stimulatory effect of TSH on thyroidal secretion is not diminished by prior administration of the hormone in vivo, (2) repeated TSH administrations in vivo cause refractoriness of the adenylate cyclase response to TSH and (3) a dichotomy exists between the secretory response and the adenylate cyclase response to repeated administrations of TSH. J. Endocr. (1985) 106, 153–157

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Bagchi, Nandalal, Birdie Shivers, and Thomas R. Brown. "Studies on the mechanism of acute inhibition of thyroglobulin hydrolysis by iodine." Acta Endocrinologica 108, no. 4 (April 1985): 511–17. http://dx.doi.org/10.1530/acta.0.1080511.

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Abstract. Iodine in excess is known to acutely inhibit thyroidal secretion. In the present study we have characterized the time course of the iodine effect in vitro and investigated the underlying mechanisms. Labelled thyroid glands were cultured in vitro in medium containing mononitrotyrosine, an inhibitor of iodotyrosine deiodinase. The rate of hydrolysis of labelled thyroglobulin was measured as the proportion of labelled iodotyrosines and iodothyronines recovered at the end of culture and was used as an index of thyroidal secretion. Thyrotrophin (TSH) administered in vivo acutely stimulated the rate of thyroglobulin hydrolysis. Addition of Nal to the culture medium acutely inhibited both basal and TSH-stimulated thyroglobulin hydrolysis. The effect of iodide was demonstrable after 2 h, maximal after 6 h and was not reversible upon removal of iodide. Iodide abolished the dibutyryl cAMP induced stimulation of thyroglobulin hydrolysis. Iodide required organic binding of iodine for its effect but new protein or RNA synthesis was not necessary. The inhibitory effects of iodide and lysosomotrophic agents such as NH4C1 and chloroquin on thyroglobulin hydrolysis were additive suggesting different sites of action. Iodide added in vitro altered the distribution of label in prelabelled thyroglobulin in a way that suggested increased coupling in the thyroglobulin molecule. These data indicate that 1) the iodide effect occurs progressively over a 6 h period, 2) continued presence of iodide is not necessary once the inhibition is established, 3) iodide exerts its action primarily at a post cAMP, prelysosomal site and 4) the effect requires organic binding of iodine, but not new RNA or protein synthesis. Our data are consistent with the hypothesis that excess iodide acutely inhibits thyroglobulin hydrolysis by increasing the resistance of thyroglobulin to proteolytic degradation through increased iodination and coupling.

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Masini-Repiso, Ana, Ana Cabanillas, Marta Andrada, and A. Coleoni. "Monoamine Oxidase A Mediates Iodotyrosine Formation Induced by Monoamines in Bovine Thyroid Particulate Fraction." Hormone and Metabolic Research 22, no. 02 (February 1990): 80–84. http://dx.doi.org/10.1055/s-2007-1004856.

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Friedman, Jessica E., James A. Watson, David W. H. Lam, and Steven E. Rokita. "Iodotyrosine Deiodinase Is the First Mammalian Member of the NADH Oxidase/Flavin Reductase Superfamily." Journal of Biological Chemistry 281, no. 5 (November 29, 2005): 2812–19. http://dx.doi.org/10.1074/jbc.m510365200.

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Sun, Qingyu, Sheng Yin, Joseph A. Loo, and Ryan R. Julian. "Radical Directed Dissociation for Facile Identification of Iodotyrosine Residues Using Electrospray Ionization Mass Spectrometry." Analytical Chemistry 82, no. 9 (May 2010): 3826–33. http://dx.doi.org/10.1021/ac100256v.

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Moreno, José C., and Theo J. Visser. "Genetics and phenomics of hypothyroidism and goiter due to iodotyrosine deiodinase (DEHAL1) gene mutations." Molecular and Cellular Endocrinology 322, no. 1-2 (June 30, 2010): 91–98. http://dx.doi.org/10.1016/j.mce.2010.03.010.

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Schiess, N., G. Csaba, and L. Kőhidai. "Chemotactic selection with insulin, di-iodotyrosine and histamine alters the phagocytotic responsiveness of Tetrahymena." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 128, no. 4 (April 2001): 521–30. http://dx.doi.org/10.1016/s1532-0456(01)00169-7.

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