scholarly journals Endurance exercise increases the protein levels of PGC-1α and respiratory chain complexes in mouse skeletal muscle during atorvastatin administration

2018 ◽  
Vol 69 (2) ◽  
pp. 327-333
Author(s):  
Koji Nonaka ◽  
Yutaka Ozaki ◽  
Kenichi Ito ◽  
Masahiro Sakita ◽  
Satsuki Une ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Respiratory Chain ◽  
Endurance Exercise ◽  
Respiratory Chain Complexes ◽  
Mouse Skeletal Muscle ◽  
Protein Levels ◽  
Chain Complexes

scholarly journals Evaluation of theIn VivoandIn VitroEffects of Fructose on Respiratory Chain Complexes in Tissues of Young Rats

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Ernesto António Macongonde ◽  
Thais Ceresér Vilela ◽  
Giselli Scaini ◽  
Cinara Ludvig Gonçalves ◽  
Bruna Klippel Ferreira ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cerebral Cortex ◽  
Respiratory Chain ◽  
Biological Fluids ◽  
Control Group ◽  
Respiratory Chain Complexes ◽  
Mitochondrial Energy Metabolism ◽  
Chain Complexes ◽  
Aldolase B

Hereditary fructose intolerance (HFI) is an autosomal-recessive disorder characterized by fructose and fructose-1-phosphate accumulation in tissues and biological fluids of patients. This disease results from a deficiency of aldolase B, which metabolizes fructose in the liver, kidney, and small intestine. We here investigated the effect of acute fructose administration on the activities of mitochondrial respiratory chain complexes, succinate dehydrogenase (SDH), and malate dehydrogenase (MDH) in cerebral cortex, liver, kidney, and skeletal muscle of male 30-day-old Wistar rats. The rats received subcutaneous injection of sodium chloride (0.9%; control group) or fructose solution (5 μmol/g; treated group). One hour later, the animals were euthanized and the cerebral cortex, liver, kidney, and skeletal muscle were isolated and homogenized for the investigations. Acute fructose administration increased complex I-III activity in liver. On the other hand, decreased complexes II and II-III activities in skeletal muscle and MDH in kidney were found. Interestingly, none of these parameters were affectedin vitro. Our present data indicate that fructose administration elicits impairment of mitochondrial energy metabolism, which may contribute to the pathogenesis of the HFI patients.

A fast method for high resolution oxymetry study of skeletal muscle mitochondrial respiratory chain complexes

2017 ◽  
Vol 528 ◽  
pp. 57-62 ◽  
Author(s):  
Jean-Claude Vienne ◽  
Catherine Cimetta ◽  
Marie Dubois ◽  
Thibault Duburcq ◽  
Raphaël Favory ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
High Resolution ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Fast Method ◽  
Respiratory Chain Complexes ◽  
Chain Complexes ◽  
Mitochondrial Respiratory

scholarly journals Selective and Reversible Disruption of Mitochondrial Inner Membrane Protein Complexes by Lipophilic Cations

2021 ◽  
Author(s):  
Anezka Kafkova ◽  
Lisa Tilokani ◽  
Filip Trčka ◽  
Veronika Šrámková ◽  
Marie Vancová ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Respiratory Chain ◽  
Mitochondrial Membrane ◽  
Mitochondrial Morphology ◽  
Respiratory Chain Complexes ◽  
Inner Membrane ◽  
Protein Levels ◽  
Mitochondrial Inner Membrane ◽  
Chain Complexes ◽  
The Impact

ABSTRACTMitochondria represent an attractive drug target in the treatment of many diseases. One of the most commonly used approaches to deliver therapeutics specifically into mitochondria is their conjugation to the triphenylphosphonium (TPP) moiety. While the TPP molecule is often regarded as biologically inert, there is evidence that the moiety itself has a significant impact on the activity of mitochondrial respiratory chain complexes.We studied the impact of a subchronic exposure of C2C12 mouse myoblasts to a set of TPP derivatives. Our results show that the alkyl-TPP cause dose- and hydrophobicity-dependent alterations of mitochondrial morphology and a selective decrease in the amounts of mitochondrial inner membrane (but not outer membrane) proteins including structural subunits of the respiratory chain complexes (such as MT-CO1 of complex IV or NDUFB8 of complex I), as well as components of the mitochondrial calcium uniporter complex (MCUC). The treatment with alkyl-TPP additionally resulted in OPA1-cleavage. Both the structural and functional effects of alkyl-TPP were found to be reversible. A similar effect was observed with the mitochondria-targeted antioxidant MitoQ. We further show that this effect on protein levels cannot be explained solely by a decrease in mitochondrial membrane potential.We conclude that TPP derivatives negatively affect mitochondrial structure and function at least in part through their effect on selective mitochondrial membrane protein levels via a reversible controlled process.

scholarly journals Impairment of Electron Transfer Chain Induced by Acute Carnosine Administration in Skeletal Muscle of Young Rats

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
José Roberto Macarini ◽  
Soliany Grassi Maravai ◽  
José Henrique Cararo ◽  
Nádia Webber Dimer ◽  
Cinara Ludvig Gonçalves ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Electron Transfer ◽  
Creatine Kinase ◽  
Respiratory Chain ◽  
Atp Depletion ◽  
Neurological Dysfunction ◽  
Control Group ◽  
Mrna Levels ◽  
Respiratory Chain Complexes ◽  
Chain Complexes

Serum carnosinase deficiency is an inherited disorder that leads to an accumulation of carnosine in the brain tissue, cerebrospinal fluid, skeletal muscle, and other tissues of affected patients. Considering that high levels of carnosine are associated with neurological dysfunction and that the pathophysiological mechanisms involved in serum carnosinase deficiency remain poorly understood, we investigated thein vivoeffects of carnosine on bioenergetics parameters, namely, respiratory chain complexes (I–III, II, and II-III), malate dehydrogenase, succinate dehydrogenase, and creatine kinase activities and the expression of mitochondrial-specific transcription factors (NRF-1, PGC-1α, andTFAM) in skeletal muscle of young Wistar rats. We observed a significant decrease of complexes I–III and II activities in animals receiving carnosine acutely, as compared to control group. However, no significant alterations in respiratory chain complexes, citric acid cycle enzymes, and creatine kinase activities were found between rats receiving carnosine chronically and control group animals. As compared to control group, mRNA levels ofNRF-1, PGC-1α, andTFAMwere unchanged. The present findings indicate that electron transfer through the respiratory chain is impaired in skeletal muscle of rats receiving carnosine acutely. In case these findings are confirmed by further studies and ATP depletion is also observed, impairment of bioenergetics could be considered a putative mechanism responsible for the muscle damage observed in serum carnosinase-deficient patients.

Relationships between the activity of respiratory-chain complexes in pre- (biopsy) or post-slaughter muscle samples and feed efficiency in random-bred Ghezel lambs

2017 ◽  
Vol 57 (8) ◽  
pp. 1674
Author(s):  
M. J. Zamiri ◽  
R. Mehrabi ◽  
G. R. Kavoosi ◽  
H. Rajaei Sharifabadi
Keyword(s):  
Respiratory Chain ◽  
Feed Intake ◽  
Enzyme Activities ◽  
Feed Efficiency ◽  
Average Daily Gain ◽  
Chain Complex ◽  
Respiratory Chain Complex ◽  
Respiratory Chain Complexes ◽  
Chain Complexes ◽  
Daily Gain

The present study was conducted to determine the relationship between the activity of mitochondrial respiratory chain complexes in pre- and post-slaughter muscle samples and residual feed intake (RFI) in Ghezel male lambs born as a result of random mating. The study was based on the hypothesis that random-bred lambs with lower feed (or higher) RFI have lower (or higher) respiratory chain-complex activity in muscle samples. Lambs (n = 30) were fed a diet consisting of 70% concentrate and 30% alfalfa hay during a 70-day period. Individual feed intake and average daily gain were recorded to calculate the RFI, feed-conversion ratio (FCR) and adjusted FCR (aFCR). On the basis of these calculations, the lambs were classified into low and high groups for RFI, with FCR and aFCR (n = 22) being one standard deviation above or below the means; this was corroborated by Student’s t-test (P < 0.01). At the end of the experiment, a 10-g biopsy sample was taken from the posterior side of the left femoral biceps. After 24 h, the lambs were slaughtered, and a sample from the posterior side of the right femoral biceps was dissected for determination of mitochondrial protein and respiratory chain-complex activities (Complexes I–V). The RFI was not correlated with the metabolic bodyweight and average daily gain, but was positively correlated (r = 0.56) with the average daily feed intake (P < 0.01); mean daily feed intake in the low-RFI group was 200 g less than that in the high-RFI group. The FCR and aFCR were not significantly (P > 0.05) correlated with average daily feed intake (r = 0.39 and r = 0.36 respectively), but showed a negative correlation (P < 0.01) with average daily gain (r = –0.73 and r = –0.76 respectively). Although very high negative correlations were recorded between the activities of all five respiratory-chain complexes and RFI in muscle samples obtained before (–0.91 to –0.97) and after (–0.92 to –0.97) slaughter, Complexes I and V showed small negative correlations (–0.40) with FCR or aFCR (P < 0.05). Enzyme activities of the respiratory-chain Complexes I, III and V were not significantly different between the pre- and post-slaughter biopsy samples; however, the enzyme activities of respiratory-chain Complexes II and IV were slightly higher in post-slaughter samples (P < 0.01). These results suggested that it may be possible to use the enzymatic activity of respiratory-chain complexes in muscle biopsy samples for screening of lambs for RFI, providing a useful procedure for genetic selection of lambs for this component of feed efficiency. These encouraging results need to be verified in further experiments using other sheep breeds and a larger number of lambs.

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