Correlations between a nuclear and a mitochondrial mRNA of cytochrome c oxidase subunits, enzymatic activity and total mRNA content, in rat tissues

Gagnon, Jacques; Kurowski, T. T.; Wiesner, Rudolf J.; Zak, Radovan

doi:10.1007/bf02424572

Cited by 47 publications

(25 citation statements)

References 20 publications

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“…Thus COX represents an excellent model for the study of holoenzyme assembly and mitochondrial biogenesis in response to physiological stimuli. Previous studies have indicated that the expression of nuclear and mitochondrial COX subunits is coordinated among tissues possessing a wide range of COX enzyme activities (12,17). However, the current evidence suggests that this may not be the case in response to T 3 at the mRNA level (40,44).…”

Section: Discussionmentioning

confidence: 65%

Tissue-specific regulation of cytochromecoxidase subunit expression by thyroid hormone

Sheehan¹,

Kumar²,

Hood³

2004

American Journal of Physiology-Endocrinology and Metabolism

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.-The influence of thyroid hormone (T3) on respiration is partly mediated via its effect on the cytochrome c oxidase (COX) enzyme, a multi-subunit complex within the mitochondrial respiratory chain. We compared the expression of COX subunits I, III, Vb, and VIc and thyroid receptors (TR)␣1 and TR␤1 with functional changes in COX activity in tissues that possess high oxidative capacities. In response to 5 days of T3 treatment, TR␤1 increased 1.6-fold in liver, whereas TR␣1 remained unchanged. T3 also induced concomitant increases in the protein and mRNA expression of nuclear-encoded subunit COX Vb in liver, matched by a 1.3-fold increase in binding to a putative thyroid response element (TRE) within the COX Vb promoter in liver, suggesting transcriptional regulation. In contrast, T3 had no effect on COX Vb expression in heart. T3 produced a significant increase in COX III mRNA in liver but decreased COX III mRNA in heart. These changes were matched by parallel alterations in mitochondrial transcription factor A expression in both tissues. In contrast, COX I protein increased in both liver and heart 1.7-and 1.5-fold (P Ͻ 0.05), respectively. These changes in COX I closely paralleled the T3-induced increases in COX activity observed in both of these tissues. In liver, T3 induced a coordinated increase in the expression of the nuclear (COX Vb) and mitochondrial (COX I) genomes at the protein level. However, in heart, the main effect of T3 was restricted to the expression of mitochondrial DNA subunits. Thus our data suggest that T3 regulates the expression of COX subunits by both transcriptional and posttranscriptional mechanisms. The nature of this regulation differs between tissues possessing a high mitochondrial content, like liver and heart.

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Section: Discussionmentioning

confidence: 65%

Tissue-specific regulation of cytochromecoxidase subunit expression by thyroid hormone

Sheehan¹,

Kumar²,

Hood³

2004

American Journal of Physiology-Endocrinology and Metabolism

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“…Support for a transcriptional coordination between nuclear and mitochondrial genes has been provided by numerous reports (Hood et al 1989;Gagnon et al 1991;Van den Bogert et al 1993;Connor et al 1996;Heddi et al 1999). However, data from analysis of changes in mitochondrial transcription in response to thyroid hormones (Enriquez et al 1999) as well as data from reporter gene activity (Sewards et al 1994) have indicated that mitochondrial and nuclear transcription systems operate independently.…”

Section: Discussionmentioning

confidence: 93%

Large Functional Range of Steady-State Levels of Nuclear and Mitochondrial Transcripts Coding for the Subunits of the Human Mitochondrial OXPHOS System

Duborjal¹,

Beugnot²,

Camaret³

et al. 2002

Genome Res.

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We have measured, by reverse transcription and real-time quantitative PCR, the steady-state levels of the mitochondrial and nuclear transcripts encoding several subunits of the human oxidative phosphorylation (OXPHOS) system, in different normal tissues (muscle, liver, trachea, and kidney) and in cultured cells (normal fibroblasts, 143B osteosarcoma cells, 143B206 0 cells). Five mitochondrial transcripts and nine nuclear transcripts were assessed. The measured amounts of these OXPHOS transcripts in muscle samples corroborated data obtained by others using the serial analysis of gene expression (SAGE) method to appraise gene expression in the same type of tissue. Steady-state levels for all the transcripts were found to range over more than two orders of magnitude. Most of the time, the mitochondrial H-strand transcripts were present at higher levels than the nuclear transcripts. The mitochondrial L-strand transcript ND6 was usually present at a low level. Cultured 143B cells contained significantly reduced amounts of mitochondrial transcripts in comparison with the tissue samples. In 143B206 0 cells, fully depleted of mitochondrial DNA, the levels of nuclear OXPHOS transcripts were not modified in comparison with the parental cells. This observation indicated that nuclear transcription is not coordinated with mitochondrial transcription. We also observed that in the different tissues and cells, there is a transcriptional coregulation of all the investigated nuclear genes. Nuclear OXPHOS gene expression seems to be finely regulated.[The following individual kindly provided reagents, samples, or unpublished information as indicated in the paper: G. Attardi.]Through the process of oxidative phosphorylation (OXPHOS), mitochondria provide most of the ATP to eukaryotic cells. Oxidative phosphorylation corresponds to the terminal stage of substrate oxidation in mitochondria, and is catalyzed by the OXPHOS system, which functionally associates the mitochondrial respiratory chain, composed of four complexes (complexes I, II, III, and IV), and ATP synthase (complex V) for ATP synthesis. The biogenesis of all these enzymatic complexes, except complex II, requires expression of genes located at the level of both the nuclear and the mitochondrial genomes. Mechanisms that putatively coordinate the expression of these genes are poorly understood at present.

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“…The parallel increase of nuclear and mitochondrial message may be simply due to similar effects of temperature on both nuclear and mitochondrial mRNA turnover, or it may involve a regulatory coordination of the two genomes via signal transduction pathways. A coordinate expression of nuclear and mitochondrially encoded subunits of CCO has been shown in different tissues of rat (14,20). Furthermore, an equimolar upregulation of mitochondrial and nuclear CCO gene products occurs during biogenesis of mitochondria induced by chronic stimulation of rat skeletal muscle or cold exposure of brown adipose tissue (21,24).…”

Section: R512 Temperature-dependent Cco Expressionmentioning

confidence: 99%

Temperature-dependent expression of cytochrome-coxidase in Antarctic and temperate fish

Hardewig

Dijk

Moyes

et al. 1999

American Journal of Physiology-Regulatory, Integrative and Comp

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Seasonal acclimation versus permanent adaptation to low temperatures leads to a differential response in the expression of cytochrome- c oxidase (CCO) in temperate and Antarctic eelpouts. Although eurythermal eelpout from the North Sea ( Zoarces viviparus) displayed a cold-induced rise of CCO activity in white muscle, enzyme activity in the cold stenothermal Antarctic eelpout Pachycara brachycephalum failed to reflect such a compensatory increase. In Antarctic eelpout, CCO activity correlates with transcript levels of mitochondrial encoded subunits of CCO (CCO I and CCO II), whereas cold-acclimated eelpout from the North Sea show lower enzyme activities than expected on the basis of mitochondrial mRNA levels. In these animals, CCO expression at low temperatures may be limited either by nuclear CCO transcripts or by posttranscriptional processes. These may comprise translation of the subunits or assembly of the CCO holoenzyme. mRNA levels of CCO IV, one of the nuclear encoded subunits, increased strongly during cold acclimation, indicating that the expression of CCO is likely not message limited in cold-acclimated Z. viviparus. Our data suggest that seasonal cold acclimation of Z. viviparus results in a modification of the relationship between transcription and translation or posttranslational processes. In permanently cold-adapted P. brachycephalum, on the other hand, CCO expression shows similar characteristics as in the warm-acclimated confamilial species, e.g., low levels of enzyme activity correlated with low levels of mitochondrial message.

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Correlations between a nuclear and a mitochondrial mRNA of cytochrome c oxidase subunits, enzymatic activity and total mRNA content, in rat tissues

Cited by 47 publications

References 20 publications

Tissue-specific regulation of cytochromecoxidase subunit expression by thyroid hormone

Tissue-specific regulation of cytochromecoxidase subunit expression by thyroid hormone

Large Functional Range of Steady-State Levels of Nuclear and Mitochondrial Transcripts Coding for the Subunits of the Human Mitochondrial OXPHOS System

Temperature-dependent expression of cytochrome-coxidase in Antarctic and temperate fish

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