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[PMID]:26002813
[Au] Autor:Liu D; Lin X; Yu F; Zhang M; Chen H; Bao W; Wang X
[Ad] Endereço:Department of Nutrition and Food Hygiene, School of Public Health, Shandong University, 44 Wenhuaxi Road, Jinan, 250012, People's Republic of China.
[Ti] Título:Effects of 3,5-Diiodotyrosine and Potassium Iodide on Thyroid Function and Oxidative Stress in Iodine-Excess Wistar Rats.
[So] Source:Biol Trace Elem Res;168(2):447-52, 2015 Dec.
[Is] ISSN:1559-0720
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to investigate the effects of organic iodine (3,5-diiodotyrosine, DIT) and inorganic iodine (potassium iodine, KI) on thyroid function and oxidative stress in iodine-excess Wistar rats. Seventy-two Wistar rats were randomly divided into eight groups: normal control (NC), thyroid tablet-induced hyperthyroidism model (HM), low DIT (L-DIT), medium DIT (M-DIT), high DIT (H-DIT), low KI (L-KI), medium KI (M-KI), and high KI (H-KI). All rats were fed ad libitum for 30 days. Morphological changes in the thyroid, absolute and relative weights of the thyroid, thyroid function markers free triiodothyronine (FT3) and free thyroxine (FT4), urinary iodine level, and oxidative stress indicators were measured. Compared to the HM groups, the FT3 and FT4 levels decreased in the L-DIT groups; the thyroid weight and thyroid weight/body weight values decreased markedly in the L-DIT and M-DIT groups; serum superoxide dismutase/malondialdehyde increased markedly; glutathione peroxidase activity increased markedly in the L-DIT groups; and malondialdehyde levels decreased significantly in the M-DIT groups. However, the FT3 and FT4 levels decreased and glutathione peroxidase levels increased significantly in the DIT groups compared to their corresponding KI groups. Additionally, urinary iodine levels increased significantly in both DIT and KI groups, while the highest urinary iodine excretion was showed in the DIT groups among groups. When the addition of iodine with the same doses in iodine-excess rats, although neither DIT nor KI normalized iodine levels in the iodine-excess rats, the DIT did less damage than did KI to thyroid follicular cells. Therefore, DIT rather than KI had a protective effect by balancing the antioxidant system when exposed to supraphysiological iodine. These suggest that DIT may be used as a new alternative iodized salt in the universal salt iodization to avoid the potential damage of surplus KI.
[Mh] Termos MeSH primário: Di-Iodotirosina/química
Iodo/química
Estresse Oxidativo/efeitos dos fármacos
Iodeto de Potássio/química
Glândula Tireoide/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Masculino
Distribuição Aleatória
Ratos
Ratos Wistar
Espécies Reativas de Oxigênio/metabolismo
Cloreto de Sódio na Dieta
Superóxido Dismutase/metabolismo
Testes de Função Tireóidea
Tiroxina/sangue
Tri-Iodotironina/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Reactive Oxygen Species); 0 (Sodium Chloride, Dietary); 0 (iodized salt); 06LU7C9H1V (Triiodothyronine); 1C4QK22F9J (Potassium Iodide); 6L57Q44ZWW (Diiodotyrosine); 9679TC07X4 (Iodine); EC 1.15.1.1 (Superoxide Dismutase); Q51BO43MG4 (Thyroxine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150524
[St] Status:MEDLINE
[do] DOI:10.1007/s12011-015-0371-y


  2 / 603 MEDLINE  
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[PMID]:25089269
[Au] Autor:Chen KC; Lee WY; Chen HY; Chen CY
[Ad] Endereço:School of Pharmacy, China Medical University, Taichung 40402, Taiwan.
[Ti] Título:In silico investigation of potential TRAF6 inhibitor from traditional Chinese medicine against cancers.
[So] Source:Biomed Res Int;2014:429486, 2014.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been indicated that tumor necrosis factor receptor-associated factor-6 (TRAF6) will upregulate the expression of hypoxia-inducible factor-1α (HIF-1α) and promote tumor angiogenesis. TRAF6 proteins can be treated as drug target proteins for a differentiation therapy against cancers. As structural disordered disposition in the protein may induce the side-effect and reduce the occupancy for ligand to bind with target protein, PONDR-Fit protocol was performed to predict the disordered disposition in TRAF6 protein before virtual screening. TCM compounds from the TCM Database@Taiwan were employed for virtual screening to identify potent compounds as lead compounds of TRAF6 inhibitor. After virtual screening, the MD simulation was performed to validate the stability of interactions between TRAF6 proteins and each ligand. The top TCM compounds, tryptophan, diiodotyrosine, and saussureamine C, extracted from Saussurea lappa Clarke, Bos taurus domesticus Gmelin, and Lycium chinense Mill., have higher binding affinities with target protein in docking simulation. However, the docking pose of TRAF6 protein with tryptophan is not stable under dynamic condition. For the other two TCM candidates, diiodotyrosine and saussureamine C maintain the similar docking poses under dynamic conditions. Hence, we propose the TCM compounds, diiodotyrosine and saussureamine C, as potential candidates as lead compounds for further study in drug development process with the TRAF6 protein against cancer.
[Mh] Termos MeSH primário: Medicina Tradicional Chinesa/métodos
Neoplasias/tratamento farmacológico
Fator 6 Associado a Receptor de TNF/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Asparagina/análogos & derivados
Asparagina/química
Bovinos
Cristalografia por Raios X
Di-Iodotirosina/química
Seres Humanos
Ligações de Hidrogênio
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Ligantes
Simulação de Dinâmica Molecular
Neoplasias/patologia
Neovascularização Patológica
Ligação Proteica
Estrutura Secundária de Proteína
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Ligands); 0 (TNF Receptor-Associated Factor 6); 0 (saussureamine C); 6L57Q44ZWW (Diiodotyrosine); 7006-34-0 (Asparagine); 8DUH1N11BX (Tryptophan)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140805
[St] Status:MEDLINE
[do] DOI:10.1155/2014/429486


  3 / 603 MEDLINE  
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[PMID]:24809164
[Au] Autor:Tóth G; Noszál B
[Ti] Título:[Thyroid hormones and their precursors. II. Species-specific properties].
[Ti] Título:Pajzsmirigyhormonok és eloanyagaik. II. Részecske-specifikus tulajdonságok..
[So] Source:Acta Pharm Hung;84(1):21-37, 2014.
[Is] ISSN:0001-6659
[Cp] País de publicação:Hungary
[La] Idioma:hun
[Ab] Resumo:This paper surveys the species-specific physico-chemical parameters (basicity and lipophilicity) and related biological functions of thyroid hormones (thyroxine, liothyronine and reverse liothyronine) and their biological precursors (tyrosine, monoiodotyrosine and diiodotyrosine). The protonation macroconstants were determined by 1H NMR-pH titrations while the microconstants were determined by a multimodal spectroscopic-deductive methodology using auxiliary derivatives of reduced complexity. Our results show that the different number and/or position of iodine are the key factors to influence the phenolate basicity. The ionization state of the phenolate site is crucial in the biosynthesis and protein binding of thyroid hormones. The role of the protonation state in the receptor binding was investigated by an in silico docking method. Microspecies of thyroid hormones were docked to the thyroid hormone receptor isoforms. Our results quantitate at the molecular level how the ionization stage and the charge distribution influence the protein binding. The anionic form of the carboxyl group is essential for the protein binding, whereas the protonated form of the amino group loosens it. The protonation state of the phenolate plays a role of secondary importance in the receptor binding. The combined results of docking and microspeciation studies show that microspecies of the highest concentration at the pH of blood are not the strongest binding ones. The site-specific lipophilicity of our investigated molecules was determined with the measurement of distribution coefficients at different pH using carboxymethyl- and O-methyl-derivatives to mimic the partition of some of the individual microspecies. Correction factors were determined and introduced. Our data show that the iodinated aromatic ring system is the definitive structural element that fundamentally determines the lipophilicity of thyroid hormones, whereas the protonation state of the aliphatic part is essential in receptor binding. The membrane transport of thyroid hormones can be well interpreted in terms of the site-specific lipophilicity. At physiological pH these biomolecules are strongly amphipathic due to the lipophilic aromatic rings and hydrophilic amino acid side chains which can well be the reason why thyroid hormones cannot cross membranes by passive diffusion and they even become constituents of biological membranes. The site-specific physico-chemical characterization of the thyroid hormones is of fundamental importance to understand their (patho) physiological behavior and also, to influence the therapeutic properties of their drug candidate derivatives at the molecular level.
[Mh] Termos MeSH primário: Receptores dos Hormônios Tireóideos/metabolismo
Hormônios Tireóideos/química
Hormônios Tireóideos/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Simulação por Computador
Di-Iodotirosina/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Imagem por Ressonância Magnética
Monoiodotirosina/metabolismo
Prótons
Especificidade da Espécie
Hormônios Tireóideos/biossíntese
Tiroxina/metabolismo
Tri-Iodotironina/metabolismo
Tri-Iodotironina Reversa/metabolismo
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Protons); 0 (Receptors, Thyroid Hormone); 0 (Thyroid Hormones); 06LU7C9H1V (Triiodothyronine); 5817-39-0 (Triiodothyronine, Reverse); 6L57Q44ZWW (Diiodotyrosine); FRQ98U4U27 (Monoiodotyrosine); Q51BO43MG4 (Thyroxine)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:140509
[Lr] Data última revisão:
140509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140510
[St] Status:MEDLINE


  4 / 603 MEDLINE  
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[PMID]:24629858
[Au] Autor:Iglesias A; García-Nimo L; Cocho de Juan JA; Moreno JC
[Ad] Endereço:Molecular Thyroid Laboratory, Institute for Medical and Molecular Genetics (INGEMM), La Paz University Hospital, Madrid, Spain.
[Ti] Título:Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects.
[So] Source:Best Pract Res Clin Endocrinol Metab;28(2):151-9, 2014 Mar.
[Is] ISSN:1878-1594
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:DEHAL1 (also named IYD) is the thyroidal enzyme that deiodinates mono- and diiodotyrosines (MIT, DIT) and recycles iodine, a scarce element in the environment, for the efficient synthesis of thyroid hormone. Failure of this enzyme leads to the iodotyrosine deiodinase deficiency (ITDD), characterized by hypothyroidism, compressive goiter and variable mental retardation, whose diagnostic hallmark is the elevation of iodotyrosines in serum and urine. However, the specific diagnosis of this type of hypothyroidism is not routinely performed, due to technical and practical difficulties in iodotyrosine determinations. A handful of mutations in the DEHAL1 gene have been identified as the molecular basis for the ITDD. Patients harboring DEHAL1 defects so far described all belong to consanguineous families, and psychomotor deficits were present in some affected individuals. This is probably due to the lack of biochemical expression of the disease at the beginning of life, which causes ITDD being undetected in screening programs for congenital hypothyroidism, as currently performed. This worrying feature calls for efforts to improve pre-clinical detection of iodotyrosine deiodinase deficiency during the neonatal time. Such a challenge poses questions of patho-physiological (natural history of the disease, environmental factors influencing its expression) epidemiological (prevalence of ITDD) and technical nature (development of optimal methodology for safe detection of pre-clinical ITDD), which will be addressed in this review.
[Mh] Termos MeSH primário: Hipotireoidismo Congênito/diagnóstico
Hidrolases/deficiência
Hipotireoidismo/etiologia
Iodeto Peroxidase/deficiência
Proteínas de Membrana/deficiência
Proteínas de Membrana/genética
[Mh] Termos MeSH secundário: Biomarcadores/análise
Hipotireoidismo Congênito/epidemiologia
Di-Iodotirosina/metabolismo
Genótipo
Seres Humanos
Hidrolases/genética
Hipotireoidismo/diagnóstico
Recém-Nascido
Iodetos/metabolismo
Monoiodotirosina/sangue
Monoiodotirosina/metabolismo
Triagem Neonatal
Fenótipo
Prevalência
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); 0 (Iodides); 0 (Membrane Proteins); 6L57Q44ZWW (Diiodotyrosine); EC 1.11.1.8 (Iodide Peroxidase); EC 3.- (Hydrolases); EC 3.8.1.2 (iodotyrosine dehalogenase 1, human); FRQ98U4U27 (Monoiodotyrosine)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140318
[St] Status:MEDLINE


  5 / 603 MEDLINE  
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[PMID]:24153409
[Au] Autor:Phatarphekar A; Buss JM; Rokita SE
[Ad] Endereço:Department of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. rokita@jhu.edu.
[Ti] Título:Iodotyrosine deiodinase: a unique flavoprotein present in organisms of diverse phyla.
[So] Source:Mol Biosyst;10(1):86-92, 2014 Jan.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Iodide is required for thyroid hormone synthesis in mammals and other vertebrates. The role of both iodide and iodinated tyrosine derivatives is currently unknown in lower organisms, yet the presence of a key enzyme in iodide conservation, iodotyrosine deiodinase (IYD), is suggested by genomic data from a wide range of multicellular organisms as well as some bacteria. A representative set of these genes has now been expressed, and the resulting enzymes all catalyze reductive deiodination of diiodotyrosine with kcat/Km values within a single order of magnitude. This implies a physiological presence of iodotyrosines (or related halotyrosines) and a physiological role for their turnover. At least for Metazoa, IYD should provide a new marker for tracing the evolutionary development of iodinated amino acids as regulatory signals through the tree of life.
[Mh] Termos MeSH primário: Iodeto Peroxidase/genética
Iodeto Peroxidase/metabolismo
Hormônios Tireóideos/biossíntese
Tirosina/metabolismo
[Mh] Termos MeSH secundário: Animais
Domínio Catalítico
Di-Iodotirosina/metabolismo
Evolução Molecular
Regulação Enzimológica da Expressão Gênica
Halogenação
Iodeto Peroxidase/química
Iodetos/metabolismo
Camundongos
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Iodides); 0 (Thyroid Hormones); 42HK56048U (Tyrosine); 6L57Q44ZWW (Diiodotyrosine); EC 1.11.1.8 (Iodide Peroxidase)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131025
[St] Status:MEDLINE
[do] DOI:10.1039/c3mb70398c


  6 / 603 MEDLINE  
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[PMID]:23972456
[Au] Autor:Romarís-Hortas V; Bermejo-Barrera P; Moreda-Piñeiro A
[Ad] Endereço:Department of Analytical Chemistry, Nutrition and Bromatology, Faculty of Chemistry, University of Santiago de Compostela, Avenida das Ciencias s/n, 15782 Santiago de Compostela, Spain.
[Ti] Título:Ultrasound-assisted enzymatic hydrolysis for iodinated amino acid extraction from edible seaweed before reversed-phase high performance liquid chromatography-inductively coupled plasma-mass spectrometry.
[So] Source:J Chromatogr A;1309:33-40, 2013 Sep 27.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The combination of reverse phase high performance liquid chromatography (RP-HPLC) with inductively coupled plasma mass spectrometry (ICP-MS) was used for the determination of monoiodotyrosine (MIT) and diiodotyrosine (DIT) in edible seaweed. A sample pre-treatment based on ultrasound assisted enzymatic hydrolysis was optimized for the extraction of these iodinated amino acids. Pancreatin was selected as the most adequate type of enzyme, and parameters affecting the extraction efficiency (pH, temperature, mass of enzyme and extraction time) were evaluated by univariate approaches. In addition, extractable inorganic iodine (iodide) was also quantified by anion exchange high performance liquid chromatography (AE-HPLC) coupled with ICP-MS. The proposed procedure offered limits of detection of 1.1 and 4.3ngg(-1) for MIT and DIT, respectively. Total iodine contents in seaweed, as well as total iodine in enzymatic digests were measured by ICP-MS after microwave assisted alkaline digestion with tetramethylamonium hydroxide (TMAH) for total iodine assessment, and also by treating the pancreatin extracts (extractable total iodine assessment). The optimized procedure was successfully applied to five different types of edible seaweed. The highest total iodine content, and also the highest iodide levels, was found in the brown seaweed Kombu (6646±45µgg(-1)). Regarding iodinated amino acids, Nori (a red seaweed) was by far the one with the highest amount of both species (42±3 and 0.41±0.024µgg(-1) for MIT and DIT, respectively). In general, MIT concentrations were much higher than the amounts of DIT, which suggests that iodine from iodinated proteins in seaweed is most likely bound in the form of MIT residues.
[Mh] Termos MeSH primário: Cromatografia Líquida de Alta Pressão/métodos
Di-Iodotirosina/análise
Espectrometria de Massas/métodos
Monoiodotirosina/análise
Alga Marinha/química
Ultrassom/métodos
Verduras/química
[Mh] Termos MeSH secundário: Biocatálise
Di-Iodotirosina/isolamento & purificação
Hidrólise
Iodo/análise
Iodo/isolamento & purificação
Peso Molecular
Monoiodotirosina/isolamento & purificação
Pancreatina/química
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
6L57Q44ZWW (Diiodotyrosine); 8049-47-6 (Pancreatin); 9679TC07X4 (Iodine); FRQ98U4U27 (Monoiodotyrosine)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:130902
[Lr] Data última revisão:
130902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130827
[St] Status:MEDLINE


  7 / 603 MEDLINE  
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[PMID]:23926648
[Au] Autor:Tóth G; Noszál B
[Ad] Endereço:Semmelweis Egyetem, Gyógyszerészi Kémiai Intézet, Magyar Tudományos Akadémia Kábító- és Doppingszer-tudomdányi Társult Kutatócsoport, Budapest, Hogyes Endre utca 9. gergo.toth85@gmail.com
[Ti] Título:[Thyroid hormones and their precursors I. Biochemical properties].
[Ti] Título:Pajzsmirigyhormonok és eloanyagaik I. Biokémiai tulajdonságok..
[So] Source:Acta Pharm Hung;83(2):35-45, 2013.
[Is] ISSN:0001-6659
[Cp] País de publicação:Hungary
[La] Idioma:hun
[Ab] Resumo:This paper and the following one (see the next issue of Acta Pharmaceutica Hungarica) survey the biological roles and the related site-specific physico-chemical parameters (basicity and lipophilicity) of the presently known thyroid hormones (thyroxine, liothyronine and reverse liothyronine) and their biological precursors (monoiodotyrosine and diiodotyrosine). Here the literature of the thyroid hormone biochemistry, biosynthesis, plasma- and membrane transport is summarized, focusing on the pH-dependent processes. Biosyntheses of the thyroid hormones take place by oxidative coupling of two iodotyrosine residues catalyzed by thyreoperoxidase in thyreoglobulin. The protonation state of the precursors, especially that of the phenolic OH is crucial for the biosynthesis, since anionic iodotyrosine residues can only be coupled in the thyroid hormone biosyntheses. In the blood more than 99% of the circulating thyroid hormone is bound to plasma proteins among which the thyroxine-binding globulin and transthyretin are crucial. The amphiphilic character of the hormones is assumed to be the reason why their membrane transport is an energy-dependent, transport-mediated process, in which the organic anion transporter family, mainly OATP1C1, and the amino acid transporters, such as MCT8 play important roles. Liothyronine is the biologically active hormone; it binds the thyroid hormone receptor, a type of nuclear receptor. There are two major thyroid hormone receptor (TR) isoforms, alfa (TRalpha) and beta (TRbeta). The activation of the TRalpha is associated with modifications in cardiac behavior, while activation of the TRbeta is associated with increasing metabolic rates, resulting in weight loss and reduction of blood plasma lipid levels. The affinity of the thyroid hormones for different proteins depends on the ionization state of the ligands. The site-specific physico-chemical characterization of the thyroid hormones is of fundamental importance to understand their (patho)physiological behavior and also, to influence their therapeutic properties at the molecular level.
[Mh] Termos MeSH primário: Receptores dos Hormônios Tireóideos/metabolismo
Hormônios Tireóideos/química
Hormônios Tireóideos/metabolismo
[Mh] Termos MeSH secundário: Acetatos/química
Acetatos/farmacologia
Transporte Biológico/efeitos dos fármacos
Di-Iodotironinas/química
Di-Iodotironinas/metabolismo
Di-Iodotirosina/química
Di-Iodotirosina/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Proteínas de Membrana Transportadoras/metabolismo
Monoiodotirosina/química
Monoiodotirosina/metabolismo
Fenóis/química
Fenóis/farmacologia
Éteres Fenílicos/química
Éteres Fenílicos/farmacologia
Fenilacetatos/química
Fenilacetatos/farmacologia
Isoformas de Proteínas
Receptores dos Hormônios Tireóideos/efeitos dos fármacos
Relação Estrutura-Atividade
Hormônios Tireóideos/biossíntese
Tiroxina/química
Tiroxina/metabolismo
Globulina de Ligação a Tiroxina/química
Globulina de Ligação a Tiroxina/metabolismo
Tri-Iodotironina/química
Tri-Iodotironina/metabolismo
Tri-Iodotironina Reversa/química
Tri-Iodotironina Reversa/metabolismo
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acetates); 0 (Diiodothyronines); 0 (GC 1 compound); 0 (KB 141); 0 (Membrane Transport Proteins); 0 (Phenols); 0 (Phenyl Ethers); 0 (Phenylacetates); 0 (Protein Isoforms); 0 (Receptors, Thyroid Hormone); 0 (Thyroid Hormones); 0 (Thyroxine-Binding Globulin); 06LU7C9H1V (Triiodothyronine); 5817-39-0 (Triiodothyronine, Reverse); 6L57Q44ZWW (Diiodotyrosine); FRQ98U4U27 (Monoiodotyrosine); Q51BO43MG4 (Thyroxine)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130810
[St] Status:MEDLINE


  8 / 603 MEDLINE  
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[PMID]:23298914
[Au] Autor:Tóth G; Mazák K; Hosztafi S; Kökösi J; Noszál B
[Ad] Endereço:Department of Pharmaceutical Chemistry, Semmelweis University, Research Group of Drugs of Abuse and Doping Agents, Hungarian Academy of Sciences, Budapest H-1092, Hogyes Endre u. 9, Hungary.
[Ti] Título:Species-specific lipophilicity of thyroid hormones and their precursors in view of their membrane transport properties.
[So] Source:J Pharm Biomed Anal;76:112-8, 2013 Mar 25.
[Is] ISSN:1873-264X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A total of 30 species-specific partition coefficients of three thyroid hormones (thyroxine, liothyronine, reverse liothyronine) and their two biological precursors (monoiodotyrosine, diiodotyrosine) are presented. The molecules were studied using combined methods of microspeciation and lipophilicity. Microspeciation was carried out by (1)H NMR-pH and UV-pH titration techniques on the title compounds and their auxiliary derivatives of reduced complexity. Partition of some of the individual microspecies was mimicked by model compounds of the closest possible similarity, then correction factors were determined and introduced. Our data show that the iodinated aromatic ring system is the definitive structural element that fundamentally determines the lipophilicity of thyroid hormones, whereas the protonation state of the aliphatic part plays a role of secondary importance. On the other hand, the lipophilicity of the precursors is highly influenced by the protonation state due to the relative lack of overwhelmingly lipophilic moieties. The different logp values of the positional isomers liothyronine and reverse liothyronine represent the importance of steric and electronic factors in lipophilicity. Our investigations provided clear indication that overall partition, the best membrane transport - predicting physico-chemical parameter depends collectively on the site-specific basicity and species-specific partition coefficient. At physiological pH these biomolecules are strongly amphipathic due to the lipophilic aromatic rings and hydrophilic amino acid side chains which can well be the reason why thyroid hormones cannot cross membranes by passive diffusion and they are constituents of biological membranes. The lipophilicity profile of thyroid hormones and their precursors are calculated and depicted in terms of species-specific lipophilicities over the entire pH range.
[Mh] Termos MeSH primário: Tiroxina/química
Tri-Iodotironina Reversa/química
Tri-Iodotironina/química
[Mh] Termos MeSH secundário: Transporte Biológico
Di-Iodotirosina/química
Di-Iodotirosina/metabolismo
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Monoiodotirosina/química
Monoiodotirosina/metabolismo
Especificidade da Espécie
Tiroxina/metabolismo
Tri-Iodotironina/metabolismo
Tri-Iodotironina Reversa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
06LU7C9H1V (Triiodothyronine); 5817-39-0 (Triiodothyronine, Reverse); 6L57Q44ZWW (Diiodotyrosine); FRQ98U4U27 (Monoiodotyrosine); Q51BO43MG4 (Thyroxine)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130110
[St] Status:MEDLINE


  9 / 603 MEDLINE  
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[PMID]:22555933
[Au] Autor:Karthikraj R; Prabhakar S; Vairamani M
[Ad] Endereço:National Centre for Mass Spectrometry, Indian Institute of Chemical Technology, Hyderabad, 500 007 AP, India.
[Ti] Título:Differentiation of enantiomeric drugs by iodo-substituted L-amino acid references under electrospray ionization mass spectrometric conditions.
[So] Source:Rapid Commun Mass Spectrom;26(11):1385-91, 2012 Jun 15.
[Is] ISSN:1097-0231
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RATIONALE: In chiral differentiation by mass spectrometry, use of a single reference that differentiates various classes of compounds including drugs is ideal, but so far there are no such reports in the literature. We have successfully used iodo-substituted amino acids for the chiral differentiation of ten enantiomeric pairs of drugs. METHODS: To achieve the chiral differentiation, the trimeric Cu complex ion consisting of two chiral reference molecules and an analyte molecule was generated under positive ion electrospray ionization (ESI) conditions and subsequently subjected for collision- induced dissociation (CID) experiments using an LCQ ion trap mass spectrometer. The spectra were recorded under identical experimental conditions for both the enantiomers, and were averages of 30 scans. Cooks' kinetic method and chiral recognition ratio method (CR method) were used to arrive at the R(chiral) /CR values, respectively. RESULTS: The R(chiral) or CR values of the studied drugs are higher for 3,5-diiodo-L-tyrosine as the reference, than for 4-iodo-L-phenylalanine, except for isoproterenol and atenolol. Both the references show the same selectivity (R- or S-selectivity) towards all the studied drugs. With 3,5-diiodo-L-tyrosine as the reference, an R(chiral) value of 12.75 is obtained for DOPA and this is the highest reported value in the literature till now. The suitability of the current method in measuring enantiomeric excess is also demonstrated for DOPA. CONCLUSIONS: The use of 4-iodo-L-phenylalanine or 3,5-diiodo-L-tyrosine as a chiral reference for the chiral differentiation of ten enantiomeric pairs of pharmaceutically important drugs has been demonstrated. The chiral differentiation of pregabalin, tenofovir and pramipexole is reported for the first time. This study shows that it is possible to develop a single chiral reference compound for the differentiation of a group of chiral drugs having some similarities.
[Mh] Termos MeSH primário: Di-Iodotirosina/química
Preparações Farmacêuticas/química
Fenilalanina/análogos & derivados
Espectrometria de Massas por Ionização por Electrospray/métodos
[Mh] Termos MeSH secundário: Preparações Farmacêuticas/classificação
Fenilalanina/química
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Pharmaceutical Preparations); 47E5O17Y3R (Phenylalanine); 6L57Q44ZWW (Diiodotyrosine); J882Z73MPL (4-iodophenylalanine)
[Em] Mês de entrada:1208
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120505
[St] Status:MEDLINE
[do] DOI:10.1002/rcm.6237


  10 / 603 MEDLINE  
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[PMID]:22440665
[Au] Autor:Romarís-Hortas V; Bermejo-Barrera P; Moreda-Piñeiro A
[Ad] Endereço:Department of Analytical Chemistry, Nutrition and Bromatology, Faculty of Chemistry, University of Santiago de Compostela, Avenida das Ciencias s/n, 15782 Santiago de Compostela, Spain.
[Ti] Título:Development of anion-exchange/reversed-phase high performance liquid chromatography-inductively coupled plasma-mass spectrometry methods for the speciation of bio-available iodine and bromine from edible seaweed.
[So] Source:J Chromatogr A;1236:164-76, 2012 May 04.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Anion exchange high performance liquid chromatography hyphenated with inductively coupled plasma-mass spectrometry has been novelly applied to assess inorganic (iodide and iodate) and organic (3-iodotyrosine - MIT, and 3,5-diiodotyrosine - DIT) iodine species in a single chromatographic run. The optimized operating conditions (Dionex IonPac AS7, gradient elution with 175 mM ammonium nitrate plus 15% (v/v) methanol, pH 3.8, as a mobile phase and flow rates within the 0.5-1.5 mL min(-1) range) have also been used to perform inorganic bromine speciation analysis (bromide and bromate). The developed method has been applied for determining the bio-available contents of iodine and bromine species in dialyzates from edible seaweed. Reverse phase high performance liquid chromatography (Zorbax Eclipse XDB-C8, gradient elution with 0.2% (m/m) acetic acid, and 0.2% (m/m) acetic acid in methanol, as mobile phases, and a constant flow rate of 0.75 mL min(-1)) also hyphenated with inductively coupled plasma-mass spectrometry was used to confirm the presence of organic iodine species (MIT and DIT) in the dialyzates. The verification of the presence of iodinated amino acids (MIT and DIT) in the extracts was also performed by reverse phase high performance liquid chromatography-electrospray ionization-mass spectrometry (LTQ Orbitrap). The developed methods have provided good repeatability (RSD values lower than 10% for both anion exchange and reverse phase separations) and analytical recoveries within the 90-105% range for all cases. The in vitro bio-availability method consisted of a simulated gastric and an intestinal digestion/dialysis (10 kDa molecular weight cut-off - MWCO) two-stage procedure. Iodide and MIT were the main bio-available species quantified, whereas bromide was the major bromine species found in the extracts.
[Mh] Termos MeSH primário: Bromo/análise
Cromatografia por Troca Iônica/métodos
Iodo/análise
Espectrometria de Massas/métodos
Alga Marinha/química
[Mh] Termos MeSH secundário: Ácido Acético
Cromatografia Líquida de Alta Pressão/métodos
Cromatografia de Fase Reversa/métodos
Di-Iodotirosina/análise
Iodatos/análise
Iodetos/análise
Metanol
Peso Molecular
Monoiodotirosina/análise
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Iodates); 0 (Iodides); 6L57Q44ZWW (Diiodotyrosine); 9679TC07X4 (Iodine); FRQ98U4U27 (Monoiodotyrosine); Q40Q9N063P (Acetic Acid); SBV4XY874G (Bromine); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120324
[St] Status:MEDLINE
[do] DOI:10.1016/j.chroma.2012.03.019



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