Developmentally regulated expression of cytochrome-c oxidase isoforms in regenerating rat skeletal muscle

The developmental expression of tissue-specific isoforms of cytochrome- c oxidase (COX) subunit VIII [heart (COX VIII-H) and liver (COX VIII-L)] and the influence of innervation were examined in regenerating fast [extensor digitorum longus (EDL)] and slow (soleus) muscles. In adult muscles, COX VIII-H was the predominant isoform. The COX VIII-L mRNA was expressed 3 days after induction of regeneration, and it progressively decreased after 7, 10, 14, and 30 days of regeneration in both muscles. In contrast, the expression of COX VIII-H mRNA accumulated as myogenesis proceeded to the myotube stage between 7 and 10 days of regeneration and progressively increased to near control levels by 30 days. The influence of innervation on the expression of COX VIII and α-actin isoforms was examined in control, innervated, and denervated regenerating muscles at 3 and 10 days. The relative expression of COX VIII-L mRNA in denervated regenerating EDL muscles was significantly greater, while that of COX VIII-H was significantly less than in innervated regenerating EDL muscles after 10 days of regeneration. Similarly, cardiac α-actin mRNA levels were elevated in denervated regenerating EDL muscles after 10 days of regeneration. In conclusion, motor innervation influences the transition from the COX VIII-L to COX VIII-H isoform during myogenesis in regenerating muscles.

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Developmentally regulated expression of a human "finger"-containing gene encoded by the 5' half of the ret transforming gene

Molecular and Cellular Biology ◽

10.1128/mcb.8.4.1853-1856.1988 ◽

1988 ◽

Vol 8 (4) ◽

pp. 1853-1856

Author(s):

M Takahashi ◽

Y Inaguma ◽

H Hiai ◽

F Hirose

Keyword(s):

Human Gene ◽

Mrna Levels ◽

Nucleic Acid Binding ◽

Developmentally Regulated ◽

Unique Transcript ◽

Binding Domains ◽

Regulated Expression ◽

Pachytene Spermatocytes ◽

Human Finger ◽

Transforming Gene

We isolated and sequenced a cDNA clone of the human gene encoded by the 5' half of the ret transforming gene. The nucleotide sequence indicates that it encodes a protein with "finger" structures which represent putative metal- and nucleic acid-binding domains. Transcription of this gene was detected at high levels in a variety of human and rodent tumor cell lines, mouse testis, and embryos. In addition, a unique transcript was observed in testis RNA. When the expression of the unique transcript was examined at different stages of spermatogenesis, a striking increase in mRNA levels accompanied progression from meiotic prophase pachytene spermatocytes to postmeiotic round spermatids. This finger-containing gene may thus function in male germ cell development.

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Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei

Molecular and Cellular Biology ◽

10.1128/mcb.8.11.4625-4633.1988 ◽

1988 ◽

Vol 8 (11) ◽

pp. 4625-4633

Author(s):

A F Torri ◽

S L Hajduk

Keyword(s):

Steady State ◽

Cytochrome C ◽

Trypanosoma Brucei ◽

Posttranscriptional Regulation ◽

Mitochondrial Protein ◽

Developmental Cycle ◽

Mrna Levels ◽

Developmentally Regulated ◽

Partial Cdna ◽

Steady State Levels

We examined the expression of a nucleus-encoded mitochondrial protein, cytochrome c, during the life cycle of Trypanosoma brucei. The bloodstream forms of T. brucei, the long slender and short stumpy trypanosomes, have inactive mitochondria with no detectable cytochrome-mediated respiration. The insect form of T. brucei, the procyclic trypanosomes, has fully functional mitochondria. Cytochrome c is spectrally undetectable in the bloodstream forms of trypanosomes, but during differentiation to the procyclic form, spectrally detected holo-cytochrome c accumulates rapidly. We have purified T. brucei cytochrome c and raised antibodies that react to both holo- and apo-cytochrome c. In addition, we isolated a partial cDNA to trypanosome cytochrome c. An examination of protein expression and steady-state mRNA levels in T. brucei indicated that bloodstream trypanosomes did not express cytochrome c but maintained significant steady-state levels of cytochrome c mRNA. The results suggest that in T. brucei, cytochrome c is developmentally regulated by a posttranscriptional mechanism which prevents either translation or accumulation of cytochrome c in the bloodstream trypanosomes.

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Expression of a duplicate Na,K-ATPase β1-isoform in the European eel (Anguilla anguilla)

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.2000.279.1.r222 ◽

2000 ◽

Vol 279 (1) ◽

pp. R222-R229 ◽

Cited By ~ 15

Author(s):

Christopher P. Cutler ◽

Stephane Brezillon ◽

Songul Bekir ◽

Ian L. Sanders ◽

Neil Hazon ◽

...

Keyword(s):

Amino Acid ◽

Functional Role ◽

Intestinal Epithelial Cells ◽

Anguilla Anguilla ◽

European Eel ◽

Mrna Levels ◽

Intestinal Epithelial ◽

Developmentally Regulated ◽

Regulated Expression ◽

Seawater Acclimation

Recent studies on teleost fish have suggested that their genomes have undergone ancient polyploidization events resulting in the duplication of the genome. A duplicate copy of the Na,K-ATPase β1-isoform (called β233) has been identified in the European eel ( Anguilla anguilla). The β233-isoform shares high levels of nucleotide (74.8%) and amino acid (69.9%) homology with the eel β1-subunit as well as other vertebrate β1-sequences. Compared with the widely expressed β1-isoform, expression of β233-mRNA is mainly restricted to epithelial tissues. Seawater acclimation induced increases in β233-mRNA levels in kidney, gill, and intestine of migratory “silver” but not the nonmigratory “yellow” adult eels, suggesting that the factors responsible for this upregulation are themselves developmentally regulated. Expression of a variably glycosylated 40- to 52-kDa β233-protein in both gill “chloride” and intestinal epithelial cells suggests that the β233-isoform of Na,K-ATPase may play an important functional role in the major osmoregulatory tissues of euryhaline fish such as the eel.

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Co-ordinate decrease in the expression of the mitochondrial genome and nuclear genes for mitochondrial proteins in the lactation-induced mitochondrial hypotrophy of rat brown fat

Biochemical Journal ◽

10.1042/bj3080749 ◽

1995 ◽

Vol 308 (3) ◽

pp. 749-752 ◽

Cited By ~ 12

Author(s):

I Martin ◽

M Giralt ◽

O Viñas ◽

R Iglesias ◽

T Mampel ◽

...

Keyword(s):

Cytochrome C ◽

Mitochondrial Genome ◽

Cytochrome C Oxidase ◽

Molecular Mechanisms ◽

Uncoupling Protein ◽

Relative Content ◽

Nuclear Genes ◽

Mitochondrial Proteins ◽

Mrna Levels ◽

Brown Adipose

The relative abundance of the mitochondrial-encoded mRNAs for cytochrome c oxidase subunit II and NADH dehydrogenase subunit I was lower in brown adipose tissue (BAT) from lactating rats than in virgin controls. This decrease was in parallel with a significant decrease in mitochondrial 16 S rRNA levels and in the relative content of mitochondrial DNA in the tissue. BAT from lactating rats showed lowered mRNA expression of the nuclear-encoded genes for the mitochondrial uncoupling protein, subunit IV of cytochrome c oxidase and the adenine nucleotide translocase isoforms ANT1 and ANT2, whereas mRNA levels for the ATP synthase beta-subunit were unchanged. However, the relative content of this last protein was lower in BAT mitochondria from lactating rats than in virgin controls. It is concluded that lactation-induced mitochondrial hypotrophy in BAT is associated with a co-ordinate decrease in the expression of the mitochondrial genome and nuclear genes for mitochondrial proteins. This decrease is caused by regulatory events acting at different levels, including pre- and post-transcriptional regulation. BAT appears to be a useful model with which to investigate the molecular mechanisms involved in the co-ordination of the expression of the mitochondrial and nuclear genomes during mitochondrial biogenesis.

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Arterial smooth muscle cells in vivo: relationship between actin isoform expression and mitogenesis and their modulation by heparin.

The Journal of Cell Biology ◽

10.1083/jcb.107.5.1939 ◽

1988 ◽

Vol 107 (5) ◽

pp. 1939-1945 ◽

Cited By ~ 107

Author(s):

A W Clowes ◽

M M Clowes ◽

O Kocher ◽

P Ropraz ◽

C Chaponnier ◽

...

Keyword(s):

Smooth Muscle ◽

Smooth Muscle Cells ◽

Muscle Cells ◽

In Vitro Translation ◽

In Vivo Model ◽

Growth Fraction ◽

Mrna Levels ◽

Actin Isoforms ◽

Actin Mrna

Quiescent smooth muscle cells (SMC) in normal artery express a pattern of actin isoforms with alpha-smooth muscle (alpha SM) predominance that switches to beta predominance when the cells are proliferating. We have examined the relationship between the change in actin isoforms and entry of SMC into the growth cycle in an in vivo model of SMC proliferation (balloon injured rat carotid artery). alpha SM actin mRNA declined and cytoplasmic (beta + gamma) actin mRNAs increased in early G0/G1 (between 1 and 8 h after injury). In vivo synthesis and in vitro translation experiments demonstrated that functional alpha SM mRNA is decreased 24 h after injury and is proportional to the amount of mRNA present. At 36 h after injury, SMC prepared by enzymatic digestion were sorted into G0/G1 and S/G2 populations; only the SMC committed to proliferate (S/G2 fraction) showed a relative slight decrease in alpha SM actin and, more importantly, a large decrease in alpha SM actin mRNA. A switch from alpha SM predominance to beta predominance was present in the whole SMC population 5 d after injury. To determine if the change in actin isoforms was associated with proliferation, we inhibited SMC proliferation by approximately 80% with heparin, which has previously been shown to block SMC in late G0/G1 and to reduce the growth fraction. The switch in actin mRNAs and synthesis at 24 h was not prevented; however, alpha SM mRNA and protein were reinduced at 5 d in the heparin-treated animals compared to saline-treated controls. These results suggest that in vivo the synthesis of actin isoforms in arterial SMC depends on the mRNA levels and changes after injury in early G0/G1 whether or not the cells subsequently proliferate. The early changes in actin isoforms are not prevented by heparin, but they are eventually reversed if the SMC are kept in the resting state by the heparin treatment.

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MicroRNA-338 Regulates Local Cytochrome c Oxidase IV mRNA Levels and Oxidative Phosphorylation in the Axons of Sympathetic Neurons

Journal of Neuroscience ◽

10.1523/jneurosci.3338-08.2008 ◽

2008 ◽

Vol 28 (47) ◽

pp. 12581-12590 ◽

Cited By ~ 157

Author(s):

A. Aschrafi ◽

A. D. Schwechter ◽

M. G. Mameza ◽

O. Natera-Naranjo ◽

A. E. Gioio ◽

...

Keyword(s):

Cytochrome C ◽

Oxidative Phosphorylation ◽

Cytochrome C Oxidase ◽

Sympathetic Neurons ◽

Mrna Levels

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δ-Aminolaevulinate synthase expression in muscle after contractions and recovery

Biochemical Journal ◽

10.1042/bj2910219 ◽

1993 ◽

Vol 291 (1) ◽

pp. 219-223 ◽

Cited By ~ 18

Author(s):

M Takahashi ◽

D T M McCurdy ◽

D A Essig ◽

D A Hood

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Mitochondrial Biogenesis ◽

Mrna Stability ◽

Tibialis Anterior ◽

Fold Increase ◽

Mrna Levels ◽

Mrna Content

The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.

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The Developmental Expression of the Maize Regulatory Gene Hopi Determines Germination-Dependent Anthocyanin Accumulation

Genetics ◽

10.1093/genetics/155.1.323 ◽

2000 ◽

Vol 155 (1) ◽

pp. 323-336

Author(s):

Katia Petroni ◽

Eleonora Cominelli ◽

Gabriella Consonni ◽

Giuliana Gusmaroli ◽

Giuseppe Gavazzi ◽

...

Keyword(s):

Single Gene ◽

Regulatory Gene ◽

Developmental Competence ◽

Developmental Expression ◽

Anthocyanin Synthesis ◽

Anthocyanin Accumulation ◽

Developmentally Regulated ◽

Regulated Expression ◽

Anthocyanin Production ◽

Germinating Seeds

Abstract The Hopi gene is a member of the maize r1 gene family. By genetic and molecular analyses we report that Hopi consists of a single gene residing on chromosome 10 ~4.5 cM distal to r1. Hopi conditions anthocyanin deposition in aleurone, scutellum, pericarp, root, mesocotyl, leaves, and anthers, thus representing one of the broadest specifications of pigmentation pattern reported to date of all the r1 genes. A unique feature of the Hopi gene is that seeds are completely devoid of pigment at maturity but show a photoinducible germination-dependent anthocyanin accumulation in aleurone and scutellum. Our analysis has shown that the Hopi transcript is not present in scutellum of developing seeds but is induced only upon germination and that the simultaneous presence of both C1 and Hopi mRNAs is necessary to achieve A1 activation in scutella. We conclude that the expression pattern of the Hopi gene accounts for the germination-dependent anthocyanin synthesis in scutella, whereas the developmental competence of germinating seeds to induce anthocyanin production in scutella results from the combination of the light-inducible expression of C1 and the developmentally regulated expression of the Hopi gene.

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Coordination of nuclear and mitochondrial gene expression during the development of cardiac hypertrophy in rats

AJP Cell Physiology ◽

10.1152/ajpcell.1994.267.1.c229 ◽

1994 ◽

Vol 267 (1) ◽

pp. C229-C235 ◽

Cited By ~ 38

Author(s):

R. J. Wiesner ◽

V. Aschenbrenner ◽

J. C. Ruegg ◽

R. Zak

Keyword(s):

Gene Expression ◽

Cytochrome C ◽

Cardiac Hypertrophy ◽

Cytochrome C Oxidase ◽

Mitochondrial Gene ◽

Nuclear Gene ◽

Hormone Treatment ◽

Mrna Levels ◽

Mitochondrial Gene Expression ◽

Mitochondrial Rrna

We studied the coordination of nuclear and mitochondrial gene expression during cardiac hypertrophy following aortic stenosis or thyroid hormone treatment in rats. We measured mRNA levels for representative subunits of cytochrome-c oxidase, two encoded by mitochondrial DNA and two encoded by the nucleus, as well as the levels of one mitochondrial rRNA. In both models of hypertrophy, an increase of total tissue RNA, reflecting mainly cytosolic ribosomes, accompanied the increase in ventricular weight. Relative levels of mitochondrial rRNA remained unchanged, indicating a net synthesis of mitochondrial ribosomes as well. In both models, cytochrome-c oxidase activity and nuclear-encoded mRNAs remained fairly constant, whereas levels of mitochondrial mRNAs were transiently decreased 24 h after the growth stimulus. We conclude that, in the initial phase of hypertrophy, the signal regulating the synthesis of mitochondrial rRNA is synchronized with nuclear gene expression, whereas the signal regulating mitochondrial mRNA synthesis is not. We postulate that differential regulation of mitochondrial transcription and premature termination of the polycistronic transcript (the latter giving rise to the mitochondrial rRNAs) account for the observed results.

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The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA

Biochemical Journal ◽

10.1042/bj20040469 ◽

2004 ◽

Vol 382 (1) ◽

pp. 331-336 ◽

Cited By ~ 113

Author(s):

Fenghao XU ◽

Charles MORIN ◽

Grant MITCHELL ◽

Cameron ACKERLEY ◽

Brian H. ROBINSON

Keyword(s):

Cytochrome C ◽

Cytochrome Oxidase ◽

Cytochrome C Oxidase ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Mrna Levels ◽

Cytochrome C Oxidase I ◽

Pentatricopeptide Repeat ◽

Mitochondrial Translation ◽

Northern Blots

Leigh syndrome French Canadian (LSFC) is a variant of cytochrome oxidase deficiency found in Québec and caused by mutations in the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene. Northern blots showed that the LRPPRC mRNA levels seen in skeletal muscle>heart>placenta>kidney>liver>lung=brain were proportionally almost opposite in strength to the severity of the enzymic cytochrome oxidase defect. The levels of COX (cytochrome c oxidase) I and COX III mRNA visible on Northern blots were reduced in LSFC patients due to the common (A354V, Ala354→Val) founder mutation. The amount of LRPPRC protein found in both fibroblast and liver mitochondria from LSFC patients was consistently reduced to <30% of control levels. Import of [35S]methionine LRPPRC into rat liver mitochondria was slower for the mutant (A354V) protein. A titre of LRPPRC protein was also found in nuclear fractions that could not be easily accounted for by mitochondrial contamination. [35S]Methionine labelling of mitochondrial translation products showed that the translation of COX I, and perhaps COX III, was specifically reduced in the presence of the mutation. These results suggest that the gene product of LRPPRC, like PET 309p, has a role in the translation or stability of the mRNA for mitochondrially encoded COX subunits. A more diffuse distribution of LRPPRC in LSFC cells compared with controls was evident when viewed by immunofluorescence microscopy, with less LRPPRC present in peripheral mitochondria.

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