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At least 19 recordsLinked to original sources
PubMed1994

Rapid stimulation in vitro of rat liver cytochrome oxidase activity by 3,5-diiodo-L-thyronine and by 3,3'-diiodo-L-thyronine.

The effect of the iodothyronines (thyroxine (T4), 3,5,3'-triiodo-L-thyronine (L-T3), 3,5-diiodo-L-thyronine (3,5-T2), 3,3'-diiodo-L-thyronine (3,3'-T2), 3',5'-diiodo-L-thyronine (3',5'-T2), 3'-monoiodo-L-thyronine (3'-T1), 3-monoiodo-L-thyronine (3-T1) and thyronine (T0)) on rat liver cytochrome oxidase (COX) activity after their addition to rat liver homogenate and isolated mitochondria from normal and hypothyroid rats has been investigated. The addition of 3,3'-T2 and 3,5-T2 (T2s) to the liver homogenate from hypothyroid rats, but not from normal rats, significantly enhanced COX activity. The addition of T3 had a remarkably lower effect that was almost completely abolished when the propylthiouracil (PTU), an inhibitor of the type I deiodinase activity, was also added to the incubation mixture. After the addition of T2s the maximum effect was obtained at a concentration of about 10(-6) M for both 3,3'-T2 and 3,5-T2, while a 50% increase was obtained at a concentration of about 10(-9) M in both cases. The effects of T2s were rapid and already evident after 5 min of incubation (+40-50%). The maximal effect was reached after only 30 min of incubation. The above effects were not observed after the addition of T2s to the isolated mitochondria. The results clearly demonstrate that both 3,3'-T2 and 3,5-T2 directly stimulate mitochondrial COX activity which is possibly achieved through a cytoplasmic factor. The addition of the other iodothyronines (T4, 3',5'-T2, 3'-T1, 3-T1 and T0).

Animals↗
PubMed1984

Thyromimetic effects of 3,5-dimethyl,3'-isopropyl thyronine (DIMIT) and 3,5-diethyl,3'-isopropyl thyronine (DIET) in various tissues of the rat.

We have examined the effects of treatment of the rat with 3,5-dimethyl-3'-isopropyl thyronine (DIMIT) and 3,5-diethyl-3'-isopropyl thyronine (DIET) on serum thyrotropin (TSH) concentration, heart weight, hepatic outer ring (5'-) monodeiodination of T4 to T3, cardiac outer ring monodeiodination of 3'-5'-diiodothyronine (3',5'-T2) to 3'-monoiodothyronine (3'-T1), and cerebral cortical monodeiodination of 3,5-T2 in the inner ring to 3-T1. Groups of four to seven rats were injected intraperitoneally either once a day or at eight-hour intervals for three days with saline or thyronines. Serum TSH was measured by radioimmunoassay. The various monodeiodinations were studied in homogenates of the tissues at optimal pH (7.35 for outer ring monodeiodinations and 8.0 for inner ring monodeiodination) and temperature (37 degrees C) in the presence of an excess of dithiothreitol. DIMIT was clearly active in all thyromimetic effects studied. It was about 10% as active as T4 in suppression of TSH. It stimulated hepatic monodeiodination of T4 to T3 in a similar manner to T4. DIMIT was also more comparable to T4 than to T3 in effect on heart weight and cardiac metabolism of 3',5'-T2 to 3'-T1. It was highly active, apparently more so than either T4 or T3, in cerebral cortical stimulation of metabolism of 3,5-T2 to 3-T1. In distinction to DIMIT, DIET had very little thyromimetic activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1984

Mass spectral properties of volatile derivatives of thyronine (T0) and use of these in the study of thyronine excretion in eu-, hyper- and hypothyroidism.

The mass spectral properties of four classes of derivatives of thyronine are discussed ( oxazolidinone , O-methyl oxazolidinone , O-acetyl oxazolidinone and N,O- diheptafluorobutyryl methyl ester). An assay for thyronine in human urine is described based on the N,O- diheptafluorobutyryl methyl ester. Results of T0 excretion in euthyroid humans were compared with those obtained previously using an assay based on the O-acetyl oxazolidinone derivative. Patients with frank hyperthyroidism had significantly higher T0 excretion than euthyroid subjects (2 alpha less than 0.002) and hypothyroid patients lower T0 excretions than euthyroid subjects (2 alpha less than 0.002). Some overlap between the two pathological ranges and the normal euthyroid range was evident.

Humans↗
PubMed1983

3'-isopropyl-3,5-diiodo-L-thyronine: a potent synthetic thyromimetic thyronine analog. Studies of its kinetics and biological potency in man and rats and its toxicology.

In order to compare phenolic and tyrosyl ring monodeiodination, we investigated 3'-isopropyl-3,5-diiodo-L-thyronine (DIIP), a potent thyronine analog which can only be monodeiodinated on the tyrosyl ring. A specific RIA was developed. The in vivo metabolism and biological potency of DIIP and T3 were compared. DIIP and T3 kinetic studies were performed in vivo using 40 male SIVZ rats who received 5 micrograms DIIP and 0.5 microCi 131I-T3. Blood samples were obtained for up to 15 h. The MCR of DIIP was 2.8 ml/h/100 g BW and the volume of distribution was 27 ml/100 g BW, corresponding values for T3 being 34 ml/h/100 g BW and 175 ml/100 g BW. Subacute toxicology studies in rats showed that DIIP was not more toxic than T3. On the basis of these results, experiments were performed in man. Five male subjects received 40 micrograms DIIP p.o. and blood samples were collected over 17 days. The MCR was 54 ml/kg . day, the volume of distribution 188 ml/kg and the fractional disappearance rate 0.0119/h. When given to an hypothyroid patient, 16-20 micrograms DIIP daily was sufficient to restore clinical and biochemical euthyroidism. These studies demonstrate that a decreased MCR can be accompanied by increased biological activity. It is suggested that the limited monodeiodination of DIIP is one of the factors explaining the differences observed in the potency and metabolism of DIIP and T3.

Adult↗
PubMed1998

3,5-Diiodo-L-thyronine and 3,5,3'-triiodo-L-thyronine both improve the cold tolerance of hypothyroid rats, but possibly via different mechanisms.

The effects of 3,5-diiodo-L-thyronine (3,5-T2, 2.5-10 microg/100 g BW) on cold tolerance, energy expenditure and oxidative capacity of four metabolically very active tissues (brown adipose tissue, skeletal muscle, liver and heart) were determined in hypothyroid, cold-exposed rats. Hypothyroid rats survived cold for only 3-4 days. 3,5-T2 improved survival dose dependently; with 10 microg/100 g BW the rats survived 3 weeks (limit of observation). This effect was paralleled by an increased energy expenditure of the whole animal for the entire 3 weeks. Similar effects were observed in hypothyroid rats treated with 3,3',5-triiodo-L-thyronine (T3). 3,5-T2 stimulated the specific oxidative capacity (expressed as cytochrome oxidase activity per milligram protein) of all four tissues dose dependently. When the oxidative capacity was expressed as total activity (cytochrome oxidase activity times organ weight), the percentage increases were of the same order. T3 exerted similar effects, but the changes in total activity were much greater than in specific activity, indicating an effect on the tissue trophism. The effect of 3,5-T2 on cold tolerance thus mimics the effect of T3, but via different cellular mechanisms. T3 seems to act primarily on the trophism of the tissues, while 3,5-T2 may act directly on mitochondria without an effect on tissue trophism.

Adaptation, Physiological↗
PubMed2002

Biosensor for the enantioselective analysis of the thyroid hormones (+)-3,3',5-triiodo-L-thyronine (T3) and (+)-3,3',5,5'-tetraiodo-L-thyronine (T4).

An amperometric biosensor based on L-aminoacid oxidase is proposed for enantioselective assay of (+)-3,3',5-triiodo-L-thyronine (L-T3) and (+)-3,3',5,5'-tetraiodo-L-thyronine (L-T4), due to the fact that only the L enantiomer has the hormonal activity. The construction of the amperometric biosensor is simple and reproducible. The analytical information obtained from enantioselective analysis are reliable. The RSD <1% assured by using the amperometric biosensors for L enantiomers assay as raw materials, and from tablets, demonstrated their suitability for the analysis of T3 and T4 at ppb concentration levels.

Amino Acid Oxidoreductases↗
PubMed1987

[Metabolic effects of 3,5-dimethyl-3'-isopropyl-L-thyronine and 3,5,3'-triiodo-L-thyronine in the brain and liver of hypothyroid rats. Similarities and differences].

The metabolic effects of 3,5-dimethyl-3'-isopropyl-L-thyronine (DIMIT) on subcellular activities in brain and liver, have been compared to those of T3. Thyroidectomized hypothyroid rats were treated for 10 days with DIMIT (8 micrograms/100 g/day) or T3 (0.25 microgram/100 g/day). In liver mitochondrial oxidative phosphorylation, succinate cytochrome c reductase activities and nuclear RNA polymerases I and II activities were restored to normal level by DIMIT as well as by T3 treatment. In brain T3 treatment normalized both nuclear and mitochondrial activities. On the other hand daily injection of DIMIT restored like T3 nuclear activities whereas that of brain mitochondria were unaffected. We have also examined the early effects of a single injection of T3 (2.5 micrograms/100 g) or DIMIT (80 micrograms/100 g), 20 minutes prior sacrifice. DIMIT is as active as T3 in stimulation of oxidative phosphorylation and succinate cytochrome c reductase activity in liver mitochondria. However DIMIT treatment does not affect the properties of brain mitochondria. On the basis of these observations, it is suggested that there is a tissue specificity of mitochondrial receptors to DIMIT administration as it was shown at the nuclear level.

Animals↗
PubMed1993

Thyroid hormone deiodination in brain, liver, gill, heart and muscle of Atlantic salmon (Salmo salar) during photoperiodically-induced parr-smolt transformation. II. Outer- and inner-ring 3,5,3'-triiodo-L-thyronine and 3,3',5'-triiodo-L-thyronine (reverse T3) deiodination.

Outer-ring deiodinase (ORD) and inner-ring deiodinase (IRD) pathways for 3,5,3'-triiodo-L-thyronine (T3) and 3,3',5'-T3 (reverse T3, rT3) were examined in microsomal fractions of liver, heart, gill, brain, and skeletal muscle of 20-month-old Atlantic salmon induced to undergo parr-smolt transformation (PST) in late February and March by imposing a 16-hr photoperiod. All tissues showed negligible T3ORD activity. T3IRD activity was detected in both the liver (Km = 0.65 nM; Vmax = 15.5 pmol T3 deiodinated.hr-1.mg microsomal protein-1) and brain of smolts, but not in gill, heart, or skeletal muscle. rT3ORD was detected in liver, brain, and muscle, and at very low levels in gill and heart. rT3IRD activity occurred to some extent in all tissues except brain. T3IRD activity changed in brain during PST, and was low in brain and liver of post-smolts examined in late October. We conclude that (i) deiodination of T3 proceeds exclusively through an IRD pathway, which may permit regulation of T3 degradation independently of the ORD pathway responsible for T3 formation; (ii) deiodination of rT3 proceeds mainly through an ORD pathway but rT3IRD activity does occur in some tissues; and (iii) the altered brain T3IRD activity during PST suggests regulation of T3 turnover in the brain at this time.

Animals↗
PubMed1994

The novel effects of 3,5,3'-triiodo-L-thyronine on myocyte contractile function and beta-adrenergic responsiveness in dilated cardiomyopathy.

Medical management of patients with chronic left ventricular dysfunction continues to be a difficult problem. Recent clinical and experimental studies have suggested that 3,5,3'-triiodo-L-thyronine improves left ventricular pump function. However, whether 3,5,3'-triiodo-L-thyronine directly improves myocyte contractile function in cardiomyopathic states is unknown. Accordingly, this study examined the direct effects of 3,5,3'-triiodo-L-thyronine on isolated myocyte contractile function in cardiocytes obtained from control (n = 6) pigs and pigs with tachycardia-induced dilated cardiomyopathy (atrial pacing at 240 beats/min for 3 weeks; n = 6). Myocyte percent shortening and velocity of shortening were obtained at baseline and in the presence of 3,5,3'-triiodo-L-thyronine doses of 80 and 100 pmol/L. For both control and dilated cardiomyopathy groups, 3,5,3'-triiodo-L-thyronine caused a significant increase in myocyte contractile function. For example, a 100 pmol/L dose of 3,5,3'-triiodo-L-thyronine increased myocyte velocity of shortening by 51% in control myocytes and by 54% in dilated cardiomyopathy myocytes compared with baseline. A second series of experiments was performed to determine whether 3,5,3'-triiodo-L-thyronine altered the responsiveness of the beta-adrenergic receptor system in control and dilated cardiomyopathy myocytes. Myocyte contractile function was examined during beta-adrenergic stimulation with isoproterenol alone and in myocytes preincubated with 3,5,3'-triiodo-L-thyronine doses of 80 and 100 pmol/L to which isoproterenol was added. Isoproterenol alone increased velocity of shortening by 139% in control and by 233% in dilated cardiomyopathy myocytes compared with baseline. This was significantly greater than the increase with 3,5,3'-triiodo-L-thyronine alone. 3,5,3'-triiodo-L-thyronine followed by isoproterenol increased velocity of shortening by 245% in control and 313% in dilated cardiomyopathy myocytes compared with baseline. This was significantly greater than the response with 3,5,3'-triiodo-L-thyronine or isoproterenol alone and appeared to be greater than an additive response. The results from this study clearly demonstrated that 3,5,3'-triiodo-L-thyronine directly augmented myocyte contractile function in both control and dilated cardiomyopathy myocytes. In addition, 3,5,3'-triiodo-L-thyronine enhanced the contractile response to beta-adrenergic stimulation in dilated cardiomyopathy. This study provides unique evidence to suggest that 3,5,3'-triiodo-L-thyronine may be a useful adjunct to conventional inotropic support in the setting of advanced left ventricular dysfunction.

Animals↗
PubMed1998

Effects of iodotyrosines, thyronines, iodothyroacetic acids and thyromimetic analogues on in vitro copper-induced oxidation of low-density lipoproteins.

We studied the effect of different thyroid compounds [(I2, monoiodo-L-tyrosine (MIT), diiodo-L-tyrosine (DIT), L-thyronine (T0), 3,5-diiodo-L-thyronine (T2), 3,5,3'-triiodo-L-thyronine (T3), 3,3',5'-triiodo-L-thyronine (rT3), 3,5,3',5'-tetraiodo-L-thyronine (T4), 3,5-diiodothyroacetic acid (TA2), 3,5,3'-triiodothyroacetic acid (TA3) and 3,5,3',5'-tetraiodothyroacetic acid (TA4)] or thyromimetics [(3,5-dimethyl-3'-isopropyl-L-thyronine (DIMIT) and 3,5-diiodo-3'-isopropyl-thyroacetic acid (IpTA2)] on in vitro copper-induced oxidation of low-density lipoproteins (LDL). Human native LDL (0.05 g protein/L) oxidation was induced by 2.5 micromol/L of CuCl2. Conjugated dienes were measured spectrophotometrically for up to 10 hr. The length of the lag phase (Tlag), maximum velocity of the reaction (Vmax) and the maximum amount of generated dienes were obtained from kinetic data. T3 increased Tlag and decreased Vmax with a dependence upon concentration (0 to 3 micromol/L). There was no difference between the Dmax obtained with Cu2+ alone or in the presence of the various compounds (1 micromol/L). I2, MIT and DIT did not modify any parameter of the oxidation kinetic. T0 and T2 had the same antioxidant efficiency as T3, whereas T4 only decreased Vmax. rT3 increased Tlag less than did T3, whereas DIMIT was the thyronine that had the most important effect. TA2 and TA, were the most efficient antioxidant compounds. TA4 decreased Tlag less than TA3 did, whereas IpTA2 had an effect weaker than that of the physiological acetic derivatives. The data suggest that thyroid hormones and derivatives have LDL-antioxidant properties, their importance being related to their 4'-hydroxy diphenyl ether structure and depending upon the nature and the position of substituents in this structure.

Acetates↗
PubMed1995

Thyronines and probucol inhibition of human capillary endothelial cell-induced low density lipoprotein oxidation.

Oxidized lipoproteins have been implicated as important factors in the pathogenicity of atherosclerosis. Thus, antioxidants play a significant role in inhibiting a critical step in atheroma progression. Previously, we demonstrated that thyronine analogs inhibit Cu(2+)-induced low density lipoprotein (LDL) oxidation. In the present study, we examined the effect of thyronine analogs on endothelial cell (EC)-induced LDL oxidation. LDL was incubated with or without EC in the presence or absence of various concentrations of thyronine, vitamin C, or probucol at 37 degrees in a humidified atmosphere (95% air, 5% CO2). Thyronine analogs, probucol, and vitamin C inhibited EC-induced LDL oxidation in a concentration-dependent manner. The concentration of each agent (microM) producing 50% inhibition (IC50) of EC-induced LDL oxidation for thiobarbituric acid reactive substances (TBARS) and electrophoretic mobility, respectively, was as follows: 0.294 and 0.417 for levothyroxine (L-T4); 0.200 and 0.299 for L-triiodothyronine (L-T3); 0.125 and 0.264 for dextro-thyroxine (D-T4); 0.203 and 0.304 for reversed triiodothyronine (rT3); 1.02 and 1.44 for probucol; and 13.6 and 14.9 for vitamin C. Thyroid binding globulin (TBG) inhibited EC-induced LDL oxidation; further, thyronines bound to TBG exhibited more antioxidant activity than unbound thyronines. Pretreatment of EC with any of the thyronines decreased the ability of EC to oxidize LDL. Also, our results showed that a synergistic interaction exists between vitamin C and T4 in the inhibition of EC-induced LDL oxidation. The T4 and TBG concentrations that inhibited LDL oxidation were in the physiological range. We conclude that T4, like the pharmacological agent probucol, reduces oxidative modification of LDL and thus may act as a natural inhibitor of atherogenesis.

Anticholesteremic Agents↗
PubMed1994

In vitro binding of 3,5-di-iodo-L-thyronine to rat liver mitochondria.

In this study we have demonstrated that specific binding sites for 3,5-di-iodo-L-thyronine (3,5-T2) can be detected in rat liver mitochondria. After incubation with the homogenate, liver mitochondria bound only a small portion of [3,5-125I]T2. The addition of a 100-fold excess of unlabelled 3,5-T2 caused the displacement of on average 50-60% of the [3,5-125I]T2 bound. Specific binding of 3,5-T2 to rat liver mitochondria occurred rapidly; a maximum was achieved after 5 min. Maximal binding was obtained at 37 degrees C, while at 0 degrees C and 20 degrees C the values were only slightly lower. Binding was maximal at pH 7.0; mean (+/- S.E.M.) values for the apparent association constant and the binding capacity (calculated at pH 7.0, 0 degrees C and after 30 min of incubation) were 0.5 +/- 0.04 x 10(8) M-1 and 0.4 +/- 0.04 pmol/mg mitochondrial protein respectively. The specificity of binding, examined in competition studies, followed the order: 3,5-T2 > 3,3'-di-iodo-L-thyronine > 3',3,5-tri-iodo-L-thyronine > thyroxine. Other iodothyronines (3',5'-di-iodo-L-thyronine, 3,5-di-iodo-D-thyronine, 3,3',5'-tri-iodo-L-thyronine, 3-iodo-L-thyronine and 3,5-di-iodothyroacetic acid) showed little or no competition. This suggests that the specific 3,5-T2 binding sites could be of biological relevance with respect to the understanding of the mechanism of physiological action of thyroid hormones at the cellular level.

Adenosine Triphosphate↗
PubMed1991

Synthesis and characterization of N-bromoacetyl-3,3',5-triiodo-L-thyronine.

N-Bromoacetyl-3,3',5-triiodo-L-thyronine and carrier-free [3'-125I]-N-bromoacetyl-3,3',5-triiodo-L-thyronine, to be used for affinity labeling of thyroid hormone receptors, were synthesized using a one-step procedure: a solution of the thyroid hormone 3,3',5-triiodo-L-thyronine and bromoacetyl bromide in ethyl acetate was refluxed for an optimal period of time which depends on the amount of hormone processed. The bromoacetylated hormone thus obtained was then fractionated by high-speed counter-current chromatography which yielded N-bromoacetyl-3,3',5-triiodo-L-thyronine that was pure by the criteria of high-performance liquid chromatography and thin-layer chromatography with different solvent systems. The pure product was well separated from all contaminants including one which in high-performance liquid chromatography was not easily separated from N-bromoacetyl-3,3',5-triiodo-L-thyronine. The latter was characterized by 1H nuclear magnetic resonance, plasma desorption mass spectrometry, thin-layer chromatography, high-performance liquid chromatography, UV spectrophotometry, and melting point. Amounts of 3,3',5-triiodo-L-thyronine ranging from picograms, including carrier-free 125I-labeled triiodothyronine, to 200 to 300 mg can be processed with the equipment used in the present investigation.

Affinity Labels↗