Search Results
Search for other papers by Alvaro Souto Padron in
Google Scholar
PubMed
Laboratório de Fisiologia Endócrina Doris Rosenthal, Laboratório de Biologia do Exercício, Instituto de Biofísica Carlos Chagas Filho and Instituto de Pesquisa Translacional em Saúde e Ambiente na Região Amazônica (INPeTAM), CCS-Bloco G- Cidade Universitria, Ilha do Fundo, Rio de Janeiro 21949-900, Brazil
Search for other papers by Ruy Andrade Louzada Neto in
Google Scholar
PubMed
Search for other papers by Thiago Urgal Pantaleão in
Google Scholar
PubMed
Search for other papers by Maria Carolina de Souza dos Santos in
Google Scholar
PubMed
Search for other papers by Renata Lopes Araujo in
Google Scholar
PubMed
Search for other papers by Bruno Moulin de Andrade in
Google Scholar
PubMed
Search for other papers by Monique da Silva Leandro in
Google Scholar
PubMed
Search for other papers by João Pedro Saar Werneck de Castro in
Google Scholar
PubMed
Search for other papers by Andrea Claudia Freitas Ferreira in
Google Scholar
PubMed
Search for other papers by Denise Pires de Carvalho in
Google Scholar
PubMed
Introduction Compound 3,3′,5-triiodothyronine (T 3 ) exerts many important effects on the basal metabolic rate and increases oxygen consumption. Several years ago, it was shown that 3,5-diiodothyronine (3,5-T2) is responsible for certain non
Search for other papers by A. Lanni in
Google Scholar
PubMed
Search for other papers by M. Moreno in
Google Scholar
PubMed
Search for other papers by M. Cioffi in
Google Scholar
PubMed
Search for other papers by F. Goglia in
Google Scholar
PubMed
ABSTRACT
In the present study we report that 3,3′,5-tri-iodothyronine (T3) as well as two iodothyronines (3,5-diiodothyronine (3,5-T2) and 3,3′-di-iodothyronine (3,3′-T2)) significantly influence rat liver mitochondrial activity.
Liver oxidative capacity (measured as cytochrome oxidase activity/g wet tissue) in hypothyroid compared with normal rats was significantly reduced (21%, P > 0·01) and the administration of T3 and both iodothyronines restored normal values. At the mitochondrial level, treatment with T3 stimulated respiratory activity (state 4 and state 3) and did not influence cytochrome oxidase activity. On the other hand, both the mitochondrial respiratory rate and specific cytochrome oxidase activity significantly increased in hypothyroid animals after treatment with 3,3′-T2 or 3,5-T2 (about 50 and 40% respectively). The actions of both iodothyronines were rapid and evident by 1 h after the injection. The hepatic mitochondrial protein content which decreased in hypothyroid rats (9·6 mg/g liver compared with 14·1 in normal controls, P < 0·05) was restored by T3 injection, while neither T2 was able to restore it.
Our results suggest that T3 and both iodothyronines have different mechanisms of action. T3 acts on both mitochondrial mass and activity; the action on mitochondrial activity was not exerted at the cytochrome oxidase complex level. The action of the iodothyronines, on the other hand, is exerted directly on the cytochrome oxidase complex without any noticeable action on the mitochondrial mass.
Journal of Endocrinology (1993) 136, 59–64
Search for other papers by M Cimmino in
Google Scholar
PubMed
Search for other papers by F Mion in
Google Scholar
PubMed
Search for other papers by F Goglia in
Google Scholar
PubMed
Search for other papers by Y Minaire in
Google Scholar
PubMed
Search for other papers by A Géloën in
Google Scholar
PubMed
Abstract
The objective of the present study was to test in vivo the metabolic effects of 3,5-di-iodothyronine (3,5-T2) in unanesthetized and unrestrained male Sprague–Dawley rats. Amino acid and lipid metabolisms were investigated by breath tests using as tracers the 13C-carboxyl-labeled molecules of leucine, α-ketoisocaproic acid (KIC) and octanoic acid, in four different groups of rats: hypothyroid animals (receiving propylthiouracil (PTU) and iopanoic acid), hypothyroid animals treated with either a daily i.p. injection of 3,5-T2 (25 μg/100 g body weight), or triiodothyronine (T3) (1 μg/100 g body weight), and control euthyroid animals receiving equivalent volumes of the vehicle solutions. Energy expenditure was measured by continuous monitoring of O2 consumption and CO2 production in these different groups. Daily energy expenditure was decreased by 30% in PTU-treated rats. The chronic treatments with 3,5-T2 and T3 restored daily energy expenditure to the control level. 13CO2 recovered in breath following the i.v. injection of octanoic acid-[1-13C] was decreased in hypothyroid animals compared with control animals (P<0·05) and restored to control values by T3 and 3,5-T2 treatments. The 13CO2 recovered in breath after i.v. injection of leucine-[1-13C]was increased in PTU-treated compared with control animals (P<0·05). Chronic treatment with either 3,5-T2 or T3 restored 13CO2 to control values. Excretion of 13CO2 recovered in breath following the i.v. injection of KIC-[1-13C] was increased in PTU-treated compared with control animals. Chronic treatments with either 3,5-T2 or T3 did not restore KIC decarboxylation. These results suggest that 3,5-T2 exerts metabolic effects on energy expendi ture, on both lipid β-oxidation and leucine metabolism in hypothyroid rats. We conclude that 3,5-T2 is a metabolically active iodothyronine.
Journal of Endocrinology (1996) 149, 319–325
Search for other papers by Gabriela Hernández-Puga in
Google Scholar
PubMed
Search for other papers by Arturo Mendoza in
Google Scholar
PubMed
Search for other papers by Alfonso León-del-Río in
Google Scholar
PubMed
Search for other papers by Aurea Orozco in
Google Scholar
PubMed
by the presence of a nine amino-acid insert located in the ligand-binding domain (LBD) of L-Trb1. Previous work from our laboratory has shown that 3,5-diiodothyronine (T 2 ) is a specific ligand for L-Trb1, whereas S-Trb1 activates transcription only
Search for other papers by E Brzezińska-Ślebodzińska in
Google Scholar
PubMed
Search for other papers by A B Ślebodziński in
Google Scholar
PubMed
Search for other papers by E Krysin in
Google Scholar
PubMed
Abstract
Thyroxine (T4), 3,3′,5′-tri-iodothyronine (reverse T3; rT3) and di-iodothyronines (3,3′-T2 and 3′,5′-T2) were measured in pig amniotic fluid (AF) and allantoic fluid (Al) between 32 and 113 days of normal pregnancy. Low but measurable quantities of T4 in AF and Al (2·1 ± 0·3 and 3·2 ±0·5 nmol/l respectively) were found before the onset of fetal thyroid gland function, which indicates the maternal source of T4. The presence of rT3 (55·8 ±4·1 pmol/l in AF and 49·8 ± 5·3 pmol/l in Al), 3,3′-T2 (45·5 ± 0·6 pmol/l in AF and 49·2 ±9·2 pmol/l in Al) and 3′,5′-T2 (20·8 ±2·6 pmol/l in AF and 24·0 ± 2·2 pmol/l in Al) may be attributed to the monodeiodinase system already active in fetal pig tissues in early pregnancy, as demonstrated previously. T3 concentration was undetectable in both AF and Al. An approximately twofold increase in the levels of T4, rT3 and T2s in AF and Al at mid-gestation was observed. T4 and rT3 in AF showed a positive correlation with protein concentrations. AF rT3 concentration (but not T4) correlated with rT3 in the cord and maternal serum. The 3,3′-T2 and 3′,5′-T2 in AF and Al showed parallel changes to rT3, while the rT3/3,3′-T2 and rT3/3′,5′-T2 molar ratios remained constant. T4 concentrations in AF and Al were markedly lower than in corresponding maternal and fetal serum; the rT3 concentration in Al was equal to that in AF and two to four times lower than in fetal serum. In spite of differences between serum hormone patterns in the pig and human near term, iodothyronine concentrations in AF showed some similarities, mainly the following: undetectable T3, a strong correlation between rT3, T4 and AF total protein and the presence of 3,3′-T2 and 3′,5′-T2 in measurable levels. Comparative data for Al, except the ones in the present study in the pig, are not available.
Journal of Endocrinology (1995) 147, 245–251
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by E Mezosi in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by J Szabo in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by E V Nagy in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by A Borbely in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by E Varga in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by G Paragh in
Google Scholar
PubMed
Department of Microbiology, Medical and Health Science Centre, University of Debrecen, Hungary
Search for other papers by Z Varga in
Google Scholar
PubMed
onset of actions ( Davis & Davis 1996 ). Genomic actions are exerted by l -3,5,3′-tri-iodothyronine (T 3 ) while l -thyroxine (T 4 ), reverse T 3 (rT 3 ) or l -3,5-di-iodothyronine (T 2 ) have predominantly nongenomic activity ( Davis & Davis 1996
Search for other papers by X Li in
Google Scholar
PubMed
Search for other papers by DL Clemens in
Google Scholar
PubMed
Search for other papers by Cole JR in
Google Scholar
PubMed
Search for other papers by RJ Anderson in
Google Scholar
PubMed
Sulfotransferase 1A1 (SULT1A1) (thermostable phenol sulfotransferase, TS PST1, P-PST) is important in the metabolism of thyroid hormones. SULT1A1 isolated from human platelets displays wide individual variations not only in the levels of activity, but also in thermal stability. The activity of the allelic variant or allozyme SULT1A1*1, which possesses an arginine at amino acid position 213 (Arg213) has been shown to be more thermostable than the activity of the SULT1A1*2 allozyme which possesses a histidine at this position (His213) when using p-nitrophenol as the substrate. We isolated a SULT1A1*1 cDNA from a human liver cDNA library and expressed both SULT1A1*1 and SULT1A1*2 in eukaryotic cells. The allozymes were assayed using iodothyronines as the substrates and their biochemical properties were compared. SULT1A1*1 activity was more thermostable and more sensitive to NaCl than was SULT1A1*2 activity when assayed with 3,5,3'-triiodothyronine (T(3)). Sensitivities to 2,6-dichloro-4-nitrophenol (DCNP) and apparent K(m) values for SULT1A1*1 and for SULT1A1*2 with iodothyronines were similar. Based on K(m) values, the preferences of these SULT1A1 allozymes for iodothyronine substrates were the same (3,3'-diiodothyronine (3,3'-T(2))>3', 5',3-triiodothyronine (rT(3))>T(3)>thyroxine (T(4))>>3,5-diiodothyronine (3,5-T(2))). SULT1A1*1 activity was significantly higher than the SULT1A1*2 activity with T(3) as the substrate. Potential differences in thyroid hormone sulfation between individuals with predominant SULT1A1*1 versus SULT1A1*2 allozymes are most likely due to differences in catalytic activity rather than substrate specificity.
Search for other papers by Rosalba Senese in
Google Scholar
PubMed
Search for other papers by Federica Cioffi in
Google Scholar
PubMed
Search for other papers by Pieter de Lange in
Google Scholar
PubMed
Search for other papers by Fernando Goglia in
Google Scholar
PubMed
Search for other papers by Antonia Lanni in
Google Scholar
PubMed
,5,3'triiodo- l -thyronine induces SREBP-1 expression by non-genomic actions in human HEP G2 cells . Journal of Cellular Physiology 227 2388 – 2397 . Goglia F 2005 Biological effects of 3,5-diiodothyronine (T 2 ) . Biochemistry 70 164 – 172
Search for other papers by Elena Grasselli in
Google Scholar
PubMed
Search for other papers by Adriana Voci in
Google Scholar
PubMed
Search for other papers by Ilaria Demori in
Google Scholar
PubMed
DIPTERIS, Dipartimento di Scienze Biomolecolari, Dipartimento di Scienze Biologiche ed Ambientali, Dipartimento di Scienze della Vita, Istituto Nazionale Biostrutture e Biosistemi (INBB), Università di Genova, Genova, Italy
Search for other papers by Laura Canesi in
Google Scholar
PubMed
Search for other papers by Rita De Matteis in
Google Scholar
PubMed
Search for other papers by Fernando Goglia in
Google Scholar
PubMed
Search for other papers by Antonia Lanni in
Google Scholar
PubMed
Search for other papers by Gabriella Gallo in
Google Scholar
PubMed
DIPTERIS, Dipartimento di Scienze Biomolecolari, Dipartimento di Scienze Biologiche ed Ambientali, Dipartimento di Scienze della Vita, Istituto Nazionale Biostrutture e Biosistemi (INBB), Università di Genova, Genova, Italy
Search for other papers by Laura Vergani in
Google Scholar
PubMed
via oxidized LDL receptor 1 . Journal of Clinical Investigation 115 2244 – 2256 . doi:10.1172/JCI24130 . Cimmino M Mion F Goglia F Minaire Y Geloen A 1996 Demonstration of in vivo metabolic effects of 3,5-di-iodothyronine
Search for other papers by Elena Grasselli in
Google Scholar
PubMed
Search for other papers by Adriana Voci in
Google Scholar
PubMed
Dipartimento di Biologia, Dipartimento di Scienze Biologiche ed Ambientali, Istituto Nazionale Biostrutture e Biosistemi (INBB), Università di Genova, Corso Europa 26, Genova 16132, Italy
Search for other papers by Laura Canesi in
Google Scholar
PubMed
Search for other papers by Fernando Goglia in
Google Scholar
PubMed
Search for other papers by Silvia Ravera in
Google Scholar
PubMed
Search for other papers by Isabella Panfoli in
Google Scholar
PubMed
Search for other papers by Gabriella Gallo in
Google Scholar
PubMed
Dipartimento di Biologia, Dipartimento di Scienze Biologiche ed Ambientali, Istituto Nazionale Biostrutture e Biosistemi (INBB), Università di Genova, Corso Europa 26, Genova 16132, Italy
Search for other papers by Laura Vergani in
Google Scholar
PubMed
Kadenbach B 1998 3,5-Diiodothyronine binds to subunit Va of cytochrome- c oxidase and abolishes the allosteric inhibition of respiration by ATP . European Journal of Biochemistry 252 325 – 330 doi:10.1046/j.1432-1327.1998.2520325.x . Ball SG
