scholarly journals Exercise mitigates sleep loss-induced changes in glucose tolerance, mitochondrial function, sarcoplasmic protein synthesis, and diurnal rhythms

2020 ◽  
pp. 101110
Author(s):  
Nicholas J. Saner ◽  
Matthew J.-C. Lee ◽  
Jujiao Kuang ◽  
Nathan W. Pitchford ◽  
Gregory D. Roach ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Glucose Tolerance ◽  
Mitochondrial Function ◽  
Sleep Loss ◽  
Diurnal Rhythms ◽  
Sarcoplasmic Protein ◽  
Induced Changes

scholarly journals Exercise mitigates sleep-loss-induced changes in glucose tolerance, mitochondrial function, sarcoplasmic protein synthesis, and circadian rhythms

2020 ◽  
Author(s):  
Nicholas J Saner ◽  
Matthew J-C Lee ◽  
Jujiao Kuang ◽  
Nathan W Pitchford ◽  
Gregory D Roach ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Circadian Rhythms ◽  
Glucose Tolerance ◽  
Mitochondrial Function ◽  
Sleep Loss ◽  
Physiological Processes ◽  
Sarcoplasmic Protein ◽  
Concomitant Reduction ◽  
High Intensity Interval ◽  
Inadequate Sleep

AbstractSleep loss has emerged as a risk factor for the development of impaired glucose tolerance. The mechanisms underpinning this observation are unknown; however, both mitochondrial dysfunction and circadian misalignment have been proposed. Given that exercise improves glucose tolerance, mitochondrial function, and alters circadian rhythms, we investigated whether exercise may counteract the effects induced by inadequate sleep. We report that sleeping 4 hours per night, for five nights, reduced glucose tolerance, with novel observations of associated reductions in mitochondrial function, sarcoplasmic protein synthesis, and measures of circadian rhythmicity; however, incorporating three sessions of high-intensity interval exercise (HIIE) during this period mitigates these effects. These data demonstrate, for the first time, a sleep loss-induced concomitant reduction in a range of physiological processes linked to metabolic function. These same effects are not observed when exercise is performed during a period of inadequate sleep, supporting the use of HIIE as an intervention to mitigate the detrimental physiological effects of sleep loss.

Histone-induced changes of protein synthesis inEscherichia coli

1973 ◽  
Vol 18 (5) ◽  
pp. 368-375 ◽  
Author(s):  
E. Masnerová ◽  
S. Štrbáňová-Nečinová
Keyword(s):  
Protein Synthesis ◽  
Inescherichia Coli ◽  
Induced Changes

ConA induced changes in energy metabolism of rat thymocytes

1992 ◽  
Vol 12 (5) ◽  
pp. 381-386 ◽  
Author(s):  
F. Buttgereit ◽  
M. D. Brand ◽  
M. Müller
Keyword(s):  
Protein Synthesis ◽  
Oxygen Consumption ◽  
Energy Metabolism ◽  
Dna Synthesis ◽  
Atp Synthesis ◽  
Proton Leak ◽  
Ehrlich Ascites ◽  
Activated State ◽  
Ehrlich Ascites Tumour ◽  
Induced Changes

The influence of ConA on the energy metabolism of quiescent rat thymocytes was investigated by measuring the effects of inhibitors of protein synthesis, proteolysis, RNA/DNA synthesis, Na+K+-ATPase, Ca2+-ATPase and mitochondrial ATP synthesis on respiration. Only about 50% of the coupled oxygen consumption of quiescent thymocytes could be assigned to specific processes using two different media. Under these conditions the oxygen is mainly used to drive mitochondrial proton leak and to provide ATP for protein synthesis and cation transport, whereas oxygen consumption to provide ATP for RNA/DNA synthesis and ATP-dependent proteolysis was not measurable. The mitogen ConA produced a persistent increase in oxygen consumption by about 30% within seconds. After stimulation more than 80% of respiration could be assigned to specific processes. The major oxygen consuming processes of ConA-stimulated thymocytes are mitochondrial proton leak, protein synthesis and Na+K+-ATPase with about 20% each of total oxygen consumption, while Ca2+-ATPase and RNA/DNA synthesis contribute about 10% each. Quiescent thymocytes resemble resting hepatocytes in that most of the oxygen consumption remains unexplained. In constrast, the pattern of energy metabolism in stimulated thymocytes is similar to that described for Ehrlich Ascites tumour cells and splenocytes, which may also be in an activated state. Most of the oxygen consumption is accounted for, so the unexplained process(es) in unstimulated cells shut(s) off on stimulation.

scholarly journals Mechanisms Underlying Muscle Protein Imbalance Induced by Alcohol

2018 ◽  
Vol 38 (1) ◽  
pp. 197-217 ◽  
Author(s):  
Scot R. Kimball ◽  
Charles H. Lang
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Cardiac Contractility ◽  
Metabolic Phenotype ◽  
Alcoholic Myopathy ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway ◽  
Induced Changes ◽  
Skeletal Muscle Strength

Both acute intoxication and longer-term cumulative ingestion of alcohol negatively impact the metabolic phenotype of both skeletal and cardiac muscle, independent of overt protein calorie malnutrition, resulting in loss of skeletal muscle strength and cardiac contractility. In large part, these alcohol-induced changes are mediated by a decrease in protein synthesis that in turn is governed by impaired activity of a protein kinase, the mechanistic target of rapamycin (mTOR). Herein, we summarize recent advances in understanding mTOR signal transduction, similarities and differences between the effects of alcohol on this central metabolic controller in skeletal muscle and in the heart, and the effects of acute versus chronic alcohol intake. While alcohol-induced alterations in global proteolysis via activation of the ubiquitin-proteasome pathway are equivocal, emerging data suggest alcohol increases autophagy in muscle. Further studies are necessary to define the relative contributions of these bidirectional changes in protein synthesis and autophagy in the etiology of alcoholic myopathy in skeletal muscle and the heart.

ConA induced changes in energy metabolism of rat thymocytes

1992 ◽  
Vol 12 (2) ◽  
pp. 109-114 ◽  
Author(s):  
F. Buttgereit ◽  
M. D. Brand ◽  
M. Müller
Keyword(s):  
Protein Synthesis ◽  
Oxygen Consumption ◽  
Energy Metabolism ◽  
Dna Synthesis ◽  
Atp Synthesis ◽  
Proton Leak ◽  
Ehrlich Ascites ◽  
Activated State ◽  
Ehrlich Ascites Tumour ◽  
Induced Changes

The influence of ConA on the energy metabolism of quiescent rat thymocytes was investigated by measuring the effects of inhibitors of protein synthesis, proteolysis, RNA/DNA synthesis, Na+K+-ATPase, Ca2+-ATPase and mitochondrial ATP synthesis on respiration. Only about 50% of the coupled oxygen consumption of quiescent thymocytes could be assigned to specific processes using two different media. Under these conditions the oxygen is mainly used to drive mitochondrial proton leak and to provide ATP for protein synthesis and cation transport, whereas oxygen consumption to provide ATP for RNA/DNA synthesis and ATP-dependent proteolysis was not measurable. The mitogen ConA produced a persistent increase in oxygen consumption by about 30% within seconds. After stimulation more than 80% of respiration could be assigned to specific processes. The major oxygen consuming processes of ConA-stimulated thymocytes are mitochondrial proton leak, protein synthesis and Na+K+-ATPase with about 20% each of total oxygen consumption, while Ca2+-ATPase and RNA/DNA synthesis contribute about 10% each. Quiescent thymocytes resemble resting hepatocytes in that most of the oxygen consumption remains unexplained. In contrast, the pattern of energy metabolism in stimulated thymocytes is similar to that described for Ehrlich Ascites tumour cells and splenocytes, which may also be in an activated state. Most of the oxygen consumption is accounted for, so the unexplained process(es) in unstimulated cells shut(s) off on stimulation.

scholarly journals Hypoenergetic diet-induced reductions in myofibrillar protein synthesis are restored with resistance training and balanced daily protein ingestion in older men

2015 ◽  
Vol 308 (9) ◽  
pp. E734-E743 ◽  
Author(s):  
Caoileann H. Murphy ◽  
Tyler A. Churchward-Venne ◽  
Cameron J. Mitchell ◽  
Nathan M. Kolar ◽  
Amira Kassis ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Older Men ◽  
Myofibrillar Protein ◽  
Energy Restriction ◽  
Protein Distribution ◽  
Protein Meal ◽  
Fed State ◽  
Sarcoplasmic Protein ◽  
Myofibrillar Protein Synthesis

Strategies to enhance weight loss with a high fat-to-lean ratio in overweight/obese older adults are important since lean loss could exacerbate sarcopenia. We examined how dietary protein distribution affected muscle protein synthesis during energy balance (EB), energy restriction (ER), and energy restriction plus resistance training (ER + RT). A 4-wk ER diet was provided to overweight/obese older men (66 ± 4 yr, 31 ± 5 kg/m2) who were randomized to either a balanced (BAL: 25% daily protein/meal × 4) or skewed (SKEW: 7:17:72:4% daily protein/meal; n = 10/group) pattern. Myofibrillar and sarcoplasmic protein fractional synthetic rates (FSR) were measured during a 13-h primed continuous infusion of l-[ ring-13C6]phenylalanine with BAL and SKEW pattern of protein intake in EB, after 2 wk ER, and after 2 wk ER + RT. Fed-state myofibrillar FSR was lower in ER than EB in both groups ( P < 0.001), but was greater in BAL than SKEW ( P = 0.014). In ER + RT, fed-state myofibrillar FSR increased above ER in both groups and in BAL was not different from EB ( P = 0.903). In SKEW myofibrillar FSR remained lower than EB ( P = 0.002) and lower than BAL ( P = 0.006). Fed-state sarcoplasmic protein FSR was reduced similarly in ER and ER + RT compared with EB ( P < 0.01) in both groups. During ER in overweight/obese older men a BAL consumption of protein stimulated the synthesis of muscle contractile proteins more effectively than traditional, SKEW distribution. Combining RT with a BAL protein distribution “rescued” the lower rates of myofibrillar protein synthesis during moderate ER.

scholarly journals The amnestic agent anisomycin disrupts intrinsic membrane properties of hippocampal neurons via a loss of cellular energetics

2019 ◽  
Vol 122 (3) ◽  
pp. 1123-1135 ◽  
Author(s):  
C. J. Scavuzzo ◽  
M. J. LeBlancq ◽  
F. Nargang ◽  
H. Lemieux ◽  
T. J. Hamilton ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Function ◽  
Neural Activity ◽  
Memory Consolidation ◽  
Hippocampal Neurons ◽  
Membrane Properties ◽  
Long Term Memory ◽  
Term Memory ◽  
Cellular Energetics

The nearly axiomatic idea that de novo protein synthesis is necessary for long-term memory consolidation is based heavily on behavioral studies using translational inhibitors such as anisomycin. Although inhibiting protein synthesis has been shown to disrupt the expression of memory, translational inhibitors also have been found to profoundly disrupt basic neurobiological functions, including the suppression of ongoing neural activity in vivo. In the present study, using transverse hippocampal brain slices, we monitored the passive and active membrane properties of hippocampal CA1 pyramidal neurons using intracellular whole cell recordings during a brief ~30-min exposure to fast-bath-perfused anisomycin. Anisomycin suppressed protein synthesis to 46% of control levels as measured using incorporation of radiolabeled amino acids and autoradiography. During its application, anisomycin caused a significant depolarization of the membrane potential, without any changes in apparent input resistance or membrane time constant. Anisomycin-treated neurons also showed significant decreases in firing frequencies and spike amplitudes, and showed increases in spike width across spike trains, without changes in spike threshold. Because these changes indicated a loss of cellular energetics contributing to maintenance of ionic gradients across the membrane, we confirmed that anisomycin impaired mitochondrial function by reduced staining with 2,3,5-triphenyltetrazolium chloride and also impaired cytochrome c oxidase (complex IV) activity as indicated through high-resolution respirometry. These findings emphasize that anisomycin-induced alterations in neural activity and metabolism are a likely consequence of cell-wide translational inhibition. Critical reevaluation of studies using translational inhibitors to promote the protein synthesis dependent idea of long-term memory is absolutely necessary. NEW & NOTEWORTHY Memory consolidation is thought to be dependent on the synthesis of new proteins because translational inhibitors produce amnesia when administered just after learning. However, these agents also disrupt basic neurobiological functions. We show that blocking protein synthesis disrupts basic membrane properties of hippocampal neurons that correspond to induced disruptions of mitochondrial function. It is likely that translational inhibitors cause amnesia through their disruption of neural activity as a result of dysfunction of intracellular energetics.

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