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Fernando Goglia - One of the best experts on this subject based on the ideXlab platform.
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the effects of 3 5 Diiodothyronine on energy balance
Frontiers in Physiology, 2015Co-Authors: Fernando GogliaAbstract:Thyroid hormones (THs) have been known to affect energy metabolism (calorigenic effect) for over a century (Magnus-Levy, 1895; Thompson et al., 1929). In 1985 Magnus-Levy observed that patients with mixedema exhibited an abnormal low oxygen consumption when compared to normal individuals and that unusually higher amount of oxygen was consumed by hyperthyroid patients. 3,3′,5-triiodo-L-thyronine (T3) is the active form of THs and it is a major regulator of growth and development and of cellular and tissue metabolism (both intermediate and energy metabolism) throughout the body. Metabolic actions include regulation of: basal metabolic rate in homeotherms, synthesis of mitochondrial respiratory enzymes and membranes, oxidative phosphorylation and energy transduction, movement of water and Na+ ions across cell membranes; calcium and phosphorus metabolism, lipids synthesis and storage, catabolism of fatty acids, cholesterol, carbohydrate; and nitrogen (urea, creatine) metabolism; growth and developmental actions include actions on: rate of postnatal growth of many mammalian and avian tissue, maturation of fetal brain and bone, amphibian larval metamorphosis, and molting in birds. It is now recognized that T3 affects gene expression in target tissues/cells by binding to its cognate nuclear receptors (TR) which are ligand-inducible transcription factors. Two TR genes α and β encode four T3-binding receptor isoforms (α1, β1, β2, and β3). The transcriptional activity of TRs is regulated at multiple levels. Besides being regulated by T3, transcriptional activity is also regulated: (i) by the type of thyroid hormone response elements located on the promoters of T3 target genes, (ii) by the developmental- and tissue-dependent expression of TR isoforms, and (iii) by a host of nuclear coregulatory proteins (corepressors and coactivators). These nuclear proteins modulate the transcription activity of TRs in a T3-dependent manner. In the absence of T3, corepressors act to repress the basal transcriptional activity, whereas in the presence of T3, coactivators act to activate transcription. The activities regulated via the previous described mechanisms are described as “genomic actions.” However, between the mid-1980's and the beginning of the 1990's it became evident that some TH effects are non-genomic in origin. Indeed, high-affinity binding sites for thyroid hormones have for many years been recognized on the plasma membrane and other cellular sites such as mitochondria and cytoplasm (for review see Cheng et al., 2010). Recently, a structural protein of the plasma membrane, integrin αvβ3, has been shown to contain a binding domain for iodothyronines that is an initiation site for hormone-directed complex cellular events, such as cell division and angiogenesis (Bergh et al., 2005) and this qualifies the binding site for characterization as a receptor. Examples of non-genomic action of thyroid hormones are activation of: membrane Ca2-ATPase activity, 2-Deoxyglucose transport, Na, K-ATPase activity, Na+ current in myocardiocytes, Na+ current in sensory neuron, Na+/H+ exchanger, cancer cell proliferation, angiogenesis (for review see Cheng et al., 2010). In addition to this, it is now recognized that other iodothyronines or THs analogs/derivatives are able to exert relevant biological actions (for recent review, see Moreno et al., 2008; Senese et al., 2014; Zucchi et al., 2014). This article is particularly intended to describe the effects of the 3,5 diiodo-L-thyronine (T2) on energy balance (Moreno et al., 1997; Goglia, 2005).
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Impact Factor: 3.53 · DOI: 10.3389/fphys.2014.00528 · Source: PubMed CITATIONS
2014Co-Authors: See Profile, Fernando GogliaAbstract:The effects of 3,5-Diiodothyronine on energy balanc
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Responses of skeletal muscle lipid metabolism in rat gastrocnemius to hypothyroidism and iodothyronine administration: a putative role for FAT/CD36
American Journal of Physiology-endocrinology and Metabolism, 2012Co-Authors: Assunta Lombardi, Rita De Matteis, Maria Moreno, Laura Napolitano, Rosa Anna Busiello, Rosalba Senese, Pieter De Lange, Antonia Lanni, Fernando GogliaAbstract:Iodothyronines such as triiodothyronine (T3) and 3,5-Diiodothyronine (T2) influence energy expenditure and lipid metabolism. Skeletal muscle contributes significantly to energy homeostasis, and the...
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3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP
European journal of biochemistry, 1998Co-Authors: Susanne Arnold, Fernando Goglia, Bernhard KadenbachAbstract:The short-term effects of thyroid hormones, which do not occur via gene expression, were postulated to be based on interaction of Diiodothyronines with mitochondria. We demonstrate specific binding of labelled 3,5-Diiodothyronine to subunit Va of cytochrome-c oxidase from bovine heart. 3,5-Diiodothyronine, and to a small extent triiodothyronine, but not thyroxine and thyronine, abolish the allosteric inhibition of ascorbate respiration of reconstituted cytochrome c oxidase by ATP [Arnold, S. & Kadenbach, B. (1997) Eur. J. Biochem. 249, 350-354]. This abolition of ATP-inhibition by 3,5-Diiodothyronine is completely prevented by a monoclonal antibody to subunit Va. The results explain at the molecular level the short-term action of thyroid hormones on basal metabolic rate.
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Interaction of Diiodothyronines with isolated cytochrome c oxidase.
FEBS letters, 1994Co-Authors: Fernando Goglia, Antonia Lanni, J. Barth, Bernhard KadenbachAbstract:Abstract Diiodothyronines (3,3′-T2 and 3,5-T2) stimulate the activity of isolated cytochromec oxidase (COX) from bovine heart mitochondria. Maximal stimulation of activity (about 50%) is obtained with 3,3′-T2 at pH 6.4 and with 3,5-T2 at pH 7.4. In contrast, 3,5,3′-triiodothyronine (T3) exhibited no or little stimulation of COX activity. Binding of the hormones to COX leads to conformational changes as shown by modified visible spectra of the oxidized enzyme. It is suggested that ‘short-term’ effects of thyroid hormones on mitochondrial respiration are at least partly due to the allosteric interaction of Diiodothyronines with the COX complex.
Michael W H Coughtrie - One of the best experts on this subject based on the ideXlab platform.
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sulfation of thyroid hormone and dopamine during human development ontogeny of phenol sulfotransferases and arylsulfatase in liver lung and brain
The Journal of Clinical Endocrinology and Metabolism, 2001Co-Authors: Kerry Richard, Emma L Stanley, Robert Hume, Ellen Kaptein, Theo J. Visser, Michael W H CoughtrieAbstract:Sulfation is an important mechanism for regulating the biological activity of numerous hormones and neurotransmitters in man. Here we have investigated the ontogeny of sulfotransferases (SULT) and sulfatase (ARS) involved in the metabolism of thyroid hormone and dopamine. SULT1A1 enzyme activity was lower in postnatal liver and lung than in fetal tissues. Hepatic SULT1A3 (dopamine) was expressed at high levels early in development, but decreased substantially in late fetal/early neonatal liver and was essentially absent from the adult liver. In lung, significant SULT1A3 activity was observed in the fetus, but neonatal levels were considerably lower. In brain, the highest activity was observed in the choroid plexus for SULT1A1, with low and widespread activity for both SULT1A1 and SULT1A3 in other brain regions. SULT activity with 3,3′-Diiodothyronine (3,3′-T2) as substrate was measured in all tissues and correlated significantly with SULT1A1 activity (4-nitrophenol), suggesting that SULT1A1 is primarily r...
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Sulfation of thyroid hormone by estrogen sulfotransferase.
The Journal of Clinical Endocrinology and Metabolism, 1999Co-Authors: Monique H. A. Kester, C. H. Van Dijk, Alan M. Hood, N. J. M. Rose, U Pabel, C N Falany, Walter Meinl, Dick Tibboel, Hansruedi Glatt, Michael W H CoughtrieAbstract:Sulfation is one of the pathways by which thyroid hormone is inactivated. Iodothyronine sulfate concentrations are very high in human fetal blood and amniotic fluid, suggesting important production of these conjugates in utero. Human estrogen sulfotransferase (SULT1E1) is expressed among other tissues in the uterus. Here we demonstrate for the first time that SULT1E1 catalyzes the facile sulfation of the prohormone T4, the active hormone T3 and the metabolites rT3 and 3,3′-Diiodothyronine (3,3′-T2) with preference for rT3 ≈ 3,3′-T2 > T3 ≈ T4. Thus, a single enzyme is capable of sulfating two such different hormones as the female sex hormone and thyroid hormone. The potential role of SULT1E1 in fetal thyroid hormone metabolism needs to be considered.
Wensheng Huang - One of the best experts on this subject based on the ideXlab platform.
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3,3'-Diiodothyronine sulfate excretion in maternal urine reflects fetal thyroid function in sheep.
Pediatric research, 2001Co-Authors: Wensheng Huang, Delbert A. Fisher, Warner H. Florsheim, Kent Kashiwai, Daniel H. PolkAbstract:3,3′-Diiodothyronine Sulfate Excretion in Maternal Urine Reflects Fetal Thyroid Function in Sheep
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identification of 3 3 t2s as a fetal thyroid hormone derivative in maternal urine in sheep
American Journal of Physiology-endocrinology and Metabolism, 1995Co-Authors: Singyung Wu, Daniel Polk, A L Reviczky, Wensheng Huang, D A Fisher, Weilian ChenAbstract:We measured 3,3'-Diiodothyronine sulfate (T2S) in serum and urine (n = 5–6) obtained from euthyroid fetal (94–145 days of gestation, term = 150 days), newborn, and adult sheep and in serum and urin...
Antonia Lanni - One of the best experts on this subject based on the ideXlab platform.
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Non-Thyrotoxic Prevention of Diet-Induced Insulin Resistance by 3,5-Diiodo-L-Thyronine in Rats
2016Co-Authors: Antonia LanniAbstract:OBJECTIVE—High-fat diets (HFDs) are known to induce in-sulin resistance. Previously, we showed that 3,5-Diiodothyronine (T2), concomitantly administered to rats on a 4-week HFD, pre-vented gain in body weight and adipose mass. Here we investi-gated whether and how T2 prevented HFD-induced insulin resistance. RESEARCH DESIGN AND METHODS—We investigated the biochemical targets of T2 related to lipid and glucose homeosta-sis over time using various techniques, including genomic and proteomic profiling, immunoblotting, transient transfection, and enzyme activity analysis. RESULTS—Here we show that, in rats, HFD feeding induced insulin resistance (as expected), whereas T2 administration prevented its onset. T2 did so by rapidly stimulating hepatic fatty acid oxidation, decreasing hepatic triglyceride levels, an
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Nonthyrotoxic Prevention of Diet-Induced Insulin Resistance by 3,5-Diiodo-L-Thyronine in Rats
2016Co-Authors: Antonia LanniAbstract:OBJECTIVE—High-fat diets (HFDs) are known to induce in-sulin resistance. Previously, we showed that 3,5-Diiodothyronine (T2), concomitantly administered to rats on a 4-week HFD, pre-vented gain in body weight and adipose mass. Here we investi-gated whether and how T2 prevented HFD-induced insulin resistance. RESEARCH DESIGN AND METHODS—We investigated the biochemical targets of T2 related to lipid and glucose homeosta-sis over time using various techniques, including genomic and proteomic profiling, immunoblotting, transient transfection, and enzyme activity analysis. RESULTS—Here we show that, in rats, HFD feeding induced insulin resistance (as expected), whereas T2 administration pre-vented its onset. T2 did so by rapidly stimulating hepatic fatty acid oxidation, decreasing hepatic triglyceride levels, and improv
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Responses of skeletal muscle lipid metabolism in rat gastrocnemius to hypothyroidism and iodothyronine administration: a putative role for FAT/CD36
American Journal of Physiology-endocrinology and Metabolism, 2012Co-Authors: Assunta Lombardi, Rita De Matteis, Maria Moreno, Laura Napolitano, Rosa Anna Busiello, Rosalba Senese, Pieter De Lange, Antonia Lanni, Fernando GogliaAbstract:Iodothyronines such as triiodothyronine (T3) and 3,5-Diiodothyronine (T2) influence energy expenditure and lipid metabolism. Skeletal muscle contributes significantly to energy homeostasis, and the...
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Interaction of Diiodothyronines with isolated cytochrome c oxidase.
FEBS letters, 1994Co-Authors: Fernando Goglia, Antonia Lanni, J. Barth, Bernhard KadenbachAbstract:Abstract Diiodothyronines (3,3′-T2 and 3,5-T2) stimulate the activity of isolated cytochromec oxidase (COX) from bovine heart mitochondria. Maximal stimulation of activity (about 50%) is obtained with 3,3′-T2 at pH 6.4 and with 3,5-T2 at pH 7.4. In contrast, 3,5,3′-triiodothyronine (T3) exhibited no or little stimulation of COX activity. Binding of the hormones to COX leads to conformational changes as shown by modified visible spectra of the oxidized enzyme. It is suggested that ‘short-term’ effects of thyroid hormones on mitochondrial respiration are at least partly due to the allosteric interaction of Diiodothyronines with the COX complex.
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Effect of 3,3'-Diiodothyronine and 3,5-Diiodothyronine on rat liver oxidative capacity.
Molecular and cellular endocrinology, 1992Co-Authors: Antonia Lanni, Maria Moreno, M. Cioffi, Fernando GogliaAbstract:We report that 3,5,3'-triiodothyronine (T3) as well as two other iodothyronines (3,3'-Diiodothyronine and 3,5-Diiodothyronine (T2s)) stimulate rat liver oxidative capacity (measured as cytochrome oxidase activity (COX)). In hypothyroid rats COX activity and mitochondrial protein content are significantly lower than in normal control animals. The administration of both T3 and T2s to hypothyroid rats significantly enhances hepatic COX activity with T3 having the greatest effect (+60%); moreover, T3 restores the mitochondrial protein content whereas the T2s are ineffective. Administration of T2s results in a faster stimulation (already significant 1 h after the injection) of hepatic COX activity than T3 injection. Our results suggest that T3 acts on the protein synthesis mechanism involved in the regulation of the mitochondrial mass while T2s would act directly at the mitochondrial level.
Gary W. Conrad - One of the best experts on this subject based on the ideXlab platform.
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Differentiation of Diiodothyronines using electrospray ionization tandem mass spectrometry.
Journal of mass spectrometry : JMS, 2006Co-Authors: Yuntao Zhang, Abigail H. Conrad, Rudy Thoma, Gary W. ConradAbstract:Diiodothyronines 3,5-Diiodothyronine (3,5-T2), 3',5'-Diiodothyronine (3',5'-T2), and 3,3'-Diiodothyronine (3,3'-T2) are important metabolites of 3,5,3'-triiodothyronine (T3) and 3,3',5'-triiodothyronine (rT3; reverse T3). In this paper, a novel and rapid method for identifying and quantifying 3,5-T2, 3',5'-T2 and 3,3'-T2 has been introduced using electrospray ionization tandem mass spectrometry (ESI-MS/MS). Fragmentation patterns were proposed on the basis of our data obtained by ESI-MS/MS. MS2 spectra in either negative ionization mode or positive ionization mode can be used to differentiate 3,5-T2, 3',5'-T2 and 3,3'-T2. On the basis of the relative abundance of fragment ions in MS2 spectra under the positive ionization mode, quantification of the 3,5-T2, 3',5'-T2 and 3,3'-T2 isomers in mixtures is also achieved without prior separation.