Relevant bibliographies by topics / Iodotyrosine

Academic literature on the topic 'Iodotyrosine'

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Published: 14 March 2023

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Journal articles on the topic "Iodotyrosine"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Iodotyrosine"

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McTamney, Patrick Michael. "Catalytic features of the iodine salvaging enzyme iodotyrosine deiodinase." College Park, Md.: University of Maryland, 2009. http://hdl.handle.net/1903/9848.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2009.
Thesis research directed by: Dept. of Chemistry and Biochemistry. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
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Borsò, Marco. "HPLC-MS-MS analysis of thyroid hormones and iodotyrosines in knocked-out murine and natural human DEHAL-1 deficiency." Doctoral thesis, Università di Siena, 2021. http://hdl.handle.net/11365/1128063.

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Thyroid hormones (TH), namely 3,5,3’-triiodothyronine (T3) and its precursor thyroxine (T4), are key regulators of growth processes and development, and crucially control the energy metabolism. A proper availability of iodine within the thyroid is crucial for the synthesis of TH in order to maintain the homeostasis of circulating levels. The daily dietary iodine intake is not sufficient to sustain their synthesis and, in fact, most of the intra-thyroidal iodine is recycled through the activity of the Iodotyrosine Dehalogenase-1 (DEHAL-1) enzyme. Mono-iodotyrosine (MIT) and di-iodotyrosine (DIT) precursors produced in excess during TH synthesis, are deiodinated by DEHAL-1, leading to the production of I- and Tyr that are recycled and reused within the thyroid. In the last decade, human mutations of DEHAL1 causing the impairment of its catalytic activity were reported. The clinical picture caused by these mutations recapitulates the phenotype of what is known as Iodotyrosine deiodinase deficiency (ITDD), characterized by hypothyroidism, goitre and, if not treated during childhood, by intellectual impairments. A hallmark of ITDD resides in the increase of urinary and plasmatic MIT and DIT levels. High-performance liquid chromatography coupled to tandem mass spectrometry (HPLC-MS-MS) is a powerful technique characterized by high specificity and sensitivity. Even if clinical testing of TH is still performed using immunoassays, various HPLC-MS-MS methods to assay TH at low concentrations have been proposed. HPLC-MS-MS is now emerging as a powerful technique that complements traditional testing overcoming some of their limitations. Hitherto, only one HPLC-MS-MS method have been proposed in order to assay MIT and DIT levels in urine that has been used in the discovery of one of the most recent discovered human DEHAL1 mutations. The aim of my project was to develop a sensitive and robust HPLC-MS-MS method able to quantify MIT and DIT in urine and plasma, together with T3 and T4 in the latter case. The method was extensively validated and used to assay these molecules in urine and plasma collected from the novel Dehal1 knock-out mouse. Our method played a crucial role in the biochemical characterization of this first mammalian model of defective iodine recycling through DEHAL-1 deletion. We detected increased urinary and plasmatic levels of MIT and DIT in the knock-out mice and we demonstrated the presence of elevated concentrations of both molecules even at the first stage of life. The influence of iodine availability was tested, showing that mice were still euthyroid when levels of dietary iodine were sufficiently high. In the presence of scarce iodine availability, coupled to the impaired ability to recycle iodine through DEHAL-1, knock-out mice became hypothyroid. Our results demonstrated the importance of iodine availability in triggering hypothyroidism in the presence of ITDD. The importance of a powerful technique able to detect MIT and DIT was demonstrated assaying these molecules in human urine collected from a consanguineous family with a diagnosed DEHAL-1 deficiency. Our HPLC-MS-MS method was able to detect elevated urinary levels of MIT and DIT in the index patient that was clinically diagnosed with ITDD showing goitre and hypothyroidism. Remarkably, we detected a massive increase of both molecules in urine collected from one of the brothers that was healthy at the time of sample collection but that developed hypothyroidism and goitre several years later. In conclusion, our findings demonstrated the ability of our validated HPLC-MS-MS method to detect MIT, DIT together with T3 and T4 in urine and plasma samples. We showed the potential of MIT and DIT assay, especially in urine, for the early detection of hypothyroidism in DEHAL-1 deficiency. Considering the presence from the beginning of life, the detection of iodotyrosines could be potentially included in the human new-born screening for hypothyroidism.
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Watson, James Ambrose. "Insight into the structure and mechanism of iodotyrosine deiodinase, the first mammalian member of the NADH oxidase / flavin reductase superfamily." College Park, Md. : University of Maryland, 2006. http://hdl.handle.net/1903/3794.

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Thesis (Ph. D.)--University of Maryland, College Park, 2006.
Thesis research directed by: Chemistry. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
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Gnidehou, Sédami Carine. "Identification et clonage d'un nouveau gène thyroïdien : l'idotyrosine désiodase 1 ou iodotyrosine déhalogénase 1 (DEHAL1). Localisation, caractérisation biochimique et fonctionnelle des différentes isoformes." Paris 11, 2005. http://www.theses.fr/2005PA11T071.

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Gehelmann, Françoise. "Halopéridol-succinyl-glycyl-iodotyrosine : étude pharmacologique in vitro et application à la détection de récepteurs dopaminergiques sur des membranes de cellules en culture et de microdisques de striatum." Bordeaux 2, 1986. http://www.theses.fr/1986BOR22023.

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Book chapters on the topic "Iodotyrosine"

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Schomburg, Dietmar, and Ida Schomburg. "iodotyrosine deiodinase 1.22.1.1." In Class 1 Oxidoreductases, 708–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36265-1_105.

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Kirk, Kenneth L. "Iodotyrosine, Iodothyronines, and Thyroid Function." In Biochemistry of the Elemental Halogens and Inorganic Halides, 135–53. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-5817-6_6.

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Edwards, L. A., R. E. Huber, and T. J. Carne. "Methods of Separating, Detecting, Hydrolyzing and Storing Fluorotyrosine, Mono-Iodotyrosine and Di-Iodotyrosine." In Methods in Protein Sequence Analysis · 1986, 457–62. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-59259-480-1_37.

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Masini-Repiso, Ana M., Ana M. Cabanillas, and Marta C. Andrada. "Selective Inhibition by Monoamine Oxidase (MAO) Inhibitors of the Iodotyrosine Formation Induced by MAO Substrates in Bovine Thyroid Tissue." In Frontiers in Thyroidology, 613–17. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5260-0_111.

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Enna, S. J., and David B. Bylund. "Iodotyrosine." In xPharm: The Comprehensive Pharmacology Reference, 1–2. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.61948-8.

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Medeiros-Neto, Geraldo. "The Iodotyrosine Deiodinase Defect." In Inherited Disorders of the Thyroid System, edited by John Bruton Stanbury, 139–61. CRC Press, 2019. http://dx.doi.org/10.1201/9780429275388-8.

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