Thyroid hormone uptake into the cell and its subsequent localisation to the mitochondria

Hafner, Roderick P.

doi:10.1016/0014-5793(87)80464-7

Cited by 17 publications

(4 citation statements)

References 38 publications

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“…T 3 acts in a complex way at different cellular levels and time. Actions of T 3 at diverse cellular loci, such as plasmamembrane, cytoplasmic proteins, mitochondria, and nucleus are well-known (Hafner 1987;Luvisetto 1997). During postnatal period, the action of T 3 is mostly genomic in the cerebral cortex ,which gradually fades away at adulthood and is possibly replaced by a short-term rapid nongenomic effect (Eayrs 1961;Iniguez et al 1992;Davis and Davis 1996).…”

Section: Discussionmentioning

confidence: 99%

Rise of Intrasynaptosomal Ca2+ Level and Activation of Nitric Oxide Synthase in Adult Rat Cerebral Cortex Pretreated with 3-5-3′-L-Triiodothyronine

Chakrabarti

Ray

2000

Neuropsychopharmacology

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Section: Discussionmentioning

confidence: 99%

Rise of Intrasynaptosomal Ca2+ Level and Activation of Nitric Oxide Synthase in Adult Rat Cerebral Cortex Pretreated with 3-5-3′-L-Triiodothyronine

Chakrabarti

Ray

2000

Neuropsychopharmacology

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“…We ascribe these changes to a long-term regulation of mitochondrial respiration rather than short-term regulation. There are reports in the literature of tri-iodo-L-thyroninebinding proteins in the inner mitochondrial membrane and direct effects of thyroid hormone on these (reviewed in [29]). Our main evidence for suggesting that the effects we report are long-term changes is our failure to observe a large effect on the leak (slip) properties of the mitochondria within 24 h of L-thyroxine treatment and lack of reversibility by albumin.…”

Section: Discussionmentioning

confidence: 99%

Altered relationship between protonmotive force and respiration rate in non‐phosphorylating liver mitochondria isolated from rats of different thyroid hormone status

Hafner

Nobes

McGOWN

et al. 1988

European Journal of Biochemistry

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146

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We have determined the relationship between rate of respiration and protonmotive force in oligomycininhibited liver mitochondria isolated from euthyroid, hypothyroid and hyperthyroid rats. Respiration ratc was titrated with the respiratory-chain inhibitor malonate. At any given respiration rate mitochondria isolated from hypothyroid rats had a protonmotive force greater than mitochondria isolated from euthyroid controls, and mitochondria isolated from hyperthyroid rats had a protonmotive force less than mitochondria isolated from euthyroid controls, In the absence of malonate mitochondrial respiration rate increased in the order hypothyroid < euthyroid < hyperthyroid, while protonmotive force increased in the order hyperthyroid < euthyroid < hypothyroid. These findings are consistent with a thyroid-hormone-induced increase in the proton conductance of the inner mitochondrial membrane or a decrease in the H+/O ratio of the respiratory chain at any given protonmotive force. Thus the altered proton conductance or H+/O ratio of mitochondria isolated from rats of different thyroid hormone status controls the respiration rate required to balance the backflow of protons across the inner mitochondrial membrane. We discuss the possible relevance of these findings to the control of state 3 and state 4 respiration by thyroid hormone.Mitochondria isolated from hypothyroid rats chardcteristically show decreased state 4 and state 3 (nomenclature of Chance and Williams [I]) respiration rates relative to control rat mitochondria, while mitochondria from hyperthyroid rats show elevated statc 4 and state 3 respiration rates (see [2] for a review). The stimulation of state 4 respiration rate following administration of tri-iodo-L-thyronine to hypothyroid rats is not a consequence of increased ATP turnover as the respiration rates of these mitochondria remains faster (relative to mitochondria from hypothyroid rats) in the presence of oligomycin to inhibit the ATP synthase [3].The control of non-phosphorylating respiration (i. e. in the presence of oligomycin) is relatively simple. As Ap rises the permeability of the inner mitochondrial membrane to protons increases rapidly above about 130 mV Ahhrcviatians. Albumin, bovine serum albumin; FCCP, carbonyl cyanidc p-trifluoromethoxyphenylhydrazone; Me4N+, tetramethylammonium; Ph3MeP*, mcthyltriphenylphosphonium cation; SEM, standard error of the mean; H+/O, number of protons rclcased to the external bulk phase/oxygen atom reduced; Ap, difference in electrical potential across the mitochondrial inner membrane; A p , protonmotive force across the mitochondrial inner membrane, ApH, pH gradient across the mitochondrial inner membrane.istics of the mitochondrial inner membrane to protons (leak), the kinetic behaviour of the proton-pumping respiratory chain and the H+/O ratio of the respiratory chain. In the present analysis we do not discriminate between a decrease in stoichiometry and an increase in the proton permeability of the mitochondrial inner membrane. The effect of either of these ...

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“…But, although specific binding sites for T3 have been reported to occur in isolated mitochondria [9][10][11][12][13], the described short-term effects of thyroid hormones are discussed in a controversial way [2,14]. Recently, however, several authors described 'short-term' effects of diiodothyronines (3,3'-T2 and 3,5-T2) on mitochondrial respiration [15][16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Interaction of diiodothyronines with isolated cytochromec oxidase

et al. 1994

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Diiodothyronines (3,3'-T2 and 3,5-T2) stimulate the activity of isolated cytochrome c 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 (TO 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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Thyroid hormone uptake into the cell and its subsequent localisation to the mitochondria

Cited by 17 publications

References 38 publications

Rise of Intrasynaptosomal Ca2+ Level and Activation of Nitric Oxide Synthase in Adult Rat Cerebral Cortex Pretreated with 3-5-3′-L-Triiodothyronine

Rise of Intrasynaptosomal Ca2+ Level and Activation of Nitric Oxide Synthase in Adult Rat Cerebral Cortex Pretreated with 3-5-3′-L-Triiodothyronine

Altered relationship between protonmotive force and respiration rate in non‐phosphorylating liver mitochondria isolated from rats of different thyroid hormone status

Interaction of diiodothyronines with isolated cytochromec oxidase

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