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Muscle protein synthesis definition, bench step ups with weight - Plans Download

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KEY POINTS Dietary protein ingestion immediately after exercise increases muscle protein synthesis rates during the acute stages of post-exercise recovery.
Muscle protein synthesis rates are low during overnight sleep even when dietary protein is ingested after exercise.
Plasma [1-13C]phenylalanine enrichments following ingestion of intrinsically [1-13C]phenylalanine labeled protein (PRO) or placebo(PLA) prior to sleep.
Rates of whole-body protein breakdown and synthesis, protein oxidation rates and net protein balance in the protein (PRO, white bar) and placebo (PLA, black bar) experiments measured during 7.5 h of overnight recovery. Dietary protein ingestion prior to sleep stimulates muscle protein synthesis during overnight recovery. Practical recommendations for the athlete regarding dietary protein intake during and after an exercise session to optimize protein synthesis.
If dietary protein is made available to the intestine during sleep, protein is normally digested and absorbed thereby increasing plasma amino acid availability and increasing muscle protein synthesis rates. Fractional synthesis rate (FSR) of mixed muscle protein during overnight recovery from a single bout of resistance type exercise. SUMMARY Dietary protein ingestion immediately after exercise increases postexercise muscle protein synthesis rates, thereby facilitating the skeletal muscle adaptive response to prolonged exercise training. Their fraction varies from tissue to tissue, ranging from <1% (volume) in white blood cells to 35% in heart muscle cells. Dietary protein ingested prior to sleep is effectively digested and absorbed during the night, thereby increasing plasma amino acid availability and stimulating post-exercise muscle protein accretion during overnight sleep. However, the post-exercise increase in muscle protein synthesis rate is not maintained during subsequent overnight sleep. Hood, Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. Ingestion of dietary protein prior to sleep may represent an effective dietary strategy to facilitate the skeletal muscle adaptive response to exercise training and to further improve exercise training efficiency. Recent work shows that protein ingested prior to sleep is effectively digested and absorbed during the night, thereby increasing plasma amino acid availability and stimulating post-exercise muscle protein accretion during post-exercise overnight sleep. Consequently, dietary protein ingestion prior to sleep may represent an effective dietary strategy to inhibit muscle protein breakdown, stimulate muscle protein synthesis, facilitate the skeletal muscle adaptive response to exercise training and improve exercise training effectiveness. A typical matrix-destined precursor like Tfam is unfolded and directed to the import machinery by a cytosolic chaperone, either cytosolic 70-kDa heat shock protein (cHSP70) or mitochondrial import stimulating factor (MSF).
Some subunits of the holoenzyme may be derived from the mitochondrial genome (mtDNA), which also undergoes transcription and translation to synthesize a limited number (13) of proteins that are essential components of the electron transport chain. As whole-body protein synthesis rates do not necessarily reflect muscle protein, we also collected skeletal muscle biopsies in the evening and after waking up in the morning. However, the IMF mitochondria were found to have higher rates of protein synthesises, enzyme activities and respiration (1). The latter also allowed us to assess muscle protein synthesis, showing ~22% higher fractional muscle protein synthesis rates throughout post-exercise overnight sleep (Figure 3). Protein Ingestion Prior to Sleep The conclusion that nocturnal dietary protein administration may stimulate overnight muscle protein accretion provides many intriguing opportunities. These data show that provision of dietary protein prior to sleep represents an effective nutritional intervention to increase plasma amino acid availability, stimulate post-exercise muscle protein synthesis and improve whole-body protein balance during overnight sleep. For example, the application of nocturnal protein provision in sports practice may optimize post-exercise recovery during overnight sleep.
The latter may provide an effective supplementation strategy to further augment the skeletal muscle adaptive response to exercise training and, as such, to improve training efficiency. In this process, a proton gradient across the inner membrane is coupled to ATP synthesis at complex V (2). All athletes were provided with appropriate recovery nutrition (20 g protein plus 60 g CHO) immediately after cessation exercise (21:00 h). Thereafter, 30 min prior to sleep (23:30 h), subjects ingested either a beverage with or without 40 g of specially produced intrinsically [1-13C]phenylalanine casein protein. ROS are small, highly reactive molecules that can be generated by mitochondrial respiration and in active skeletal muscle. Using contemporary stable isotope methodology combined with the use of intrinsically labeled protein, we were able to assess both dietary protein digestion and absorption kinetics as well as whole-body and muscle protein synthesis rates during overnight sleep. After ingestion of the protein, we observed a rapid increase in [1-13C]phenylalanine enrichment in the blood, providing evidence that the ingested protein was being properly digested and absorbed, resulting in a continued provision of dietary protein derived amino acids into the circulation (Figure 1). The greater overnight amino acid availability increased post-exercise muscle protein synthesis rates, thereby improving overnight whole-body protein balance (Figure 2). Coingestion of carbohydrate and protein hydrolysate stimulates muscle protein synthesis during exercise in young men, with no further increase during subsequent overnight recovery. Within skeletal muscle, ATP is primarily required for the energy-dependent cross-bridge cycling between actin and myosin, as well as for Ca2+ cycling.
Proliferation of mitochondria occurs in muscle in response to endurance exercise training, chronic electrical stimulation and thyroid hormone, while loss of mitochondria is associated with inactivity and aging.2.
It is well established that chronic contractile activity, in the form of repeated bouts of endurance exercise, usually interspersed with recovery periods, results in the altered expression of a wide variety of gene products, leading to an altered muscle phenotype with improved fatigue resistance.
Additionally, it has been suggested that an age-related accumulation of dysfunctional mitochondria may result in progressive reactive oxygen species-induced damage, producing a further impairment of oxidative capacity in aged muscle. Moreover, dysfunctional mitochondria have also been implicated in the age-related loss of muscle mass known as sarcopenia.
Mitochondrial biogenesis requers the corporation of the nuclear and mitochondrial genomesOne of the most fascinating aspects of mitochondrial synthesis is that it requires the cooperation of the nuclear and mitochondrial genomes (Figure-1).
Impact of protein coingestion on muscle protein synthesis during continuous endurance type exercise. First, these thirteen components comprise only a small fraction of the total respiratory chain proteins.
Some act as single protein subunits, but many are combined nuclear-encoded proteins to form multisubunit holoenzymes, like COX or NADH dehydrogenase (Figure-1). Given the diverse promoter regions of nuclear genes encoding mitochondrial proteins, as well as the sequences of the mtDNA promoters, it is not surprising that this coordination can be disrupted. In addition, some evidence for a coordinated regulation of the two genomes was found during the mitochondrial biogenesis induced by cardiac hypertrophy, as well as in human muscle when trained and untrained individuals were compared. Protein import machinery (PIM)The expansion of the mitochondrial reticulum in skeletal muscle is a highly regulated and complex process that appears to require the co-ordinated expression of a large number of genes. Thus, an important aspect of mitochondrial biogenesis is the import machinery regulating the transport of nuclear encoded precursor proteins into the organelle. The vast majority of mitochondrial proteins (>90%) are encoded by nuclear genes and synthesized in the cytosol as preproteins containing a mitochondria import sequence. Notwithstanding the importance of the mitochondrial genome in contributing proteins to the mitochondrial respiratory chain, it is nevertheless true that most mitochondrial proteins are derived from nuclear DNA.
Therefore, a mechanism must exist for targeting these proteins to specific mitochondrial compartments once they have been synthesized in the cytosol. Although pathways of protein targeting to the outer membrane, inner membrane, matrix, or intermembrane space differ somewhat from each other (9), the most widely studied path is that of proteins destined for the matrix. Intragastric protein administration stimulates overnight muscle protein synthesis in elderly men. Cytosolic chaperones include 70-kDa heat shock protein (HSP70) and mitochondrial import stimulating factor (MSF). One of these, consisting of the Tom20 and Tom22 receptors, is the preferential route for HSP70 chaperone precursors.On the other hand, proteins interacting with MSF are largely directed to the Tom70-Tom37 heterodimer (10). Precursors are then transferred from the Tom receptors to Tom40 and the small Tom proteins 5, 6, and 7, which form an aqueous channel through which the precursor protein passes.
Proteins are then sorted to the outer membrane, to the inner membrane, or to the translocase of the inner membrane (Tim), another protein complex that allows movement of precursor proteins to either the matrix or the inner membrane. Those proteins involved in the translocation of the precursor to the matrix are Tim17, Tim23, and Tim44. Tim17 and Tim23 act as integral membrane proteins, spanning the mitochondrial inner membrane and having domains associated with both the matrix and intermembrane space. In a manner similar to the Tom receptor complexes, Tim17 and Tim23 bind the precursor protein, prevent any untimely folding that would inhibit the precursor from translocating into the matrix, and form an aqueous pore through which the precursor can travel. Coingestion of protein with carbohydrate during recovery from endurance exercise stimulates skeletal muscle protein synthesis in humans.

In contrast, Tim44 is a peripheral membrane protein that is secured to the inner face of the inner mitochondrial membrane. Along with these proteins, the inner membrane phospholipid cardiolipin is imperative for protein translocation because it appears to orient the precursor into the correct position for interaction with the Tim44-mtHSP70 complex. The number within each import machinery component refers to its size in kDa.Two other elements are required for correct import of precursor proteins into the matrix. Combined ingestion of protein and carbohydrate improves protein balance during ultra- endurance exercise.
After its arrival in the matrix, the NH2-terminal signal sequence is cleaved by a mitochondrial processing peptidase (MPP) to form the mature protein. It is then refolded into its active conformation by a mitochondrial chaperonin system consisting in part of 60-kDa heat shock protein (HSP60) and 10-kDa chaperonin (Cpn10).
The vast majority of work that defines the components of the protein import machinery, as well as their cellular function, has been done in Saccharomyces cerevisiae and Neurospora crassa. For example, the kinetics of matrix precursor protein that import into skeletal muscle SS and IMF mitochondrial fractions, the ATP and cardiolipin dependence of the process, and the relationship to mitochondrial respiration have all been defined (13).
IMF mitochondria import precursor proteins more rapidly than SS mitochondria, and there is a direct relationship between the capacity for mitochondrial respiration (and thus ATP production) and the rate of protein import. It has also been shown that a number of protein import machinery components are induced in response to chronic contractile activity.
Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects. This differential effect on protein targeting to mitochondrial compartments provides an example of how contractile activity can result in an altered mitochondrial protein stoichiometry. The accelerated rate of protein import into the matrix can be reproduced in cardiac mitochondria obtained from animals treated with thyroid hormone. When C2C12 cells were incubated with [35S] methionine and the import of radiolabeled MDH into mitochondria was measured, a greater rate of import was found during the progress of mitochondrial biogenesis occurring coincident with muscle differentiation. These data suggest that the import of matrix-destined proteins is controlled, at least in part, by the expression of Tom20. The protein import pathway represents an example of intracellular trafficking that is important for organelle biogenesis, and it may, under some conditions, determine the increase in mitochondrial content as a result of chronic exercise. Co-ingestion of protein and leucine stimulates muscle protein synthesis rates to the same extent in young and elderly lean men.
If the import rate was slow enough to limit mitochondrial biogenesis, then a pool of precursor proteins in the cell cytosol would be measurable.
In the absence of such a pool, the assumption is that newly synthesized precursor proteins are rapidly taken up by mitochondria, and the kinetics does not limit the synthesis of the organelle as a whole.
Progress in the area of protein import will advance substantially as additional mammalian homologues of the import machinery are identified. Recently, the first disease that can solely be attributed to a mutation in a protein component of the import machinery has been identified. A mutation in deafness dystonia protein (DPP) results in a neurodegenerative disorder characterized by muscle dystonia, sensorineural deafness, and blindness. DPP has been shown to be a mitochondrial protein that closely resembles Tim8p, a protein of the intermembrane space involved in the import process. Exercise effects on PIMAs noted above, exercise has been shown to induce the expression of several protein import machinery components, occurring coincident with an increased rate of translocation into the mitochondria. In turn, activity-induced changes have been observed in Tom20, Hsp60 and mtHSP70 protein and cpn10 mRNA levels, as well as cytosolic concentrations of Hsp70 and MSF (13-15). Coincident with these changes is acceleration in the rate of protein import into the matrix.
Coingestion of carbohydrate with protein does not further augment postexercise muscle protein synthesis.
Thus, the upregulation of protein import machinery components appears to be an important aspect of mitochondrial biogenesis which occurs with contractile activity. This diversity is important given that the characterization of an assortment of upstream promoter regions of genes encoding mitochondrial proteins has revealed considerable variability in their composition. NRF-1 and NRF-2 are implicated in the transcriptional control of multiple mitochondrial genes including mitochondrial transcription factor A (Tfam) and identified mitochondrial transcription specificity factors TFB1M and TFB2M, while Egr-1 is associated with promoting transcription of the electron transport chain protein cytochrome C oxidase (COX). The NRF-1 transcription factor has been shown to activate Tfam which enhances the capacity for assembly of protein complexes within the mitochondria. Importantly, Tfam activity appears to increase in response to contractile activity and exercise suggesting enhanced mitochondrial protein assembly with endurance training.
The initial cellular perturbations associated with the onset of muscle activity leading to the activation of these transcription factors are beginning to be defined (Figure-3).
Postexercise nutrient intake timing in humans is critical to recovery of leg glucose and protein homeostasis. The initial cellular perturbations associated with the onset of muscle activity leading to the activation and increment of these transcription factors are beginning to be defined. The potential for ROS to induce oxidative damage has significant implications for the cellular integrity of highly metabolic, long-lived and post-mitotic tissues such as brain, heart, and skeletal muscle. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men.
Thus, ROS-induced accumulations in faulty proteins, oxidized fatty acids, and mtDNA mutations would result in a progressive, feed-forward, and irreversible cycle of cellular dysfunction that leads to the onset of phenotypes associated with aging.
The role of mitochondria in promoting sarcopenia was uncovered by studies showing that muscle fibers containing dysfunctional mitochondria were atrophied compared to fibers that did not.
As well, these authors and other groups (34-36) have reported that histochemical analyses of skeletal muscle fibers revealed an increase in the number of ragged red fibers, characterized by elevated levels of succinate dehydrogenase and a deficiency in COX activity. Within mitochondria reside proteins, which upon release from the organelle, can initiate a cascade of proteolytic events that converge onto the nucleus leading to the fragmentation of DNA. Thus, the intimate connection between mitochondrial function and the viability of skeletal muscle suggests that this organelle plays a significant role in the progression of aging. Indeed, it is evident that in skeletal muscle of aged individuals, the induction of apoptosis is greater when compared with younger subjects. Whey protein stimulates postprandial muscle protein accretion more effectively than do casein and casein hydrolysate in older men.
Alternation in mitochondrial content and morphology with agingElectron microscopic (EM) analyses reveal that the volume of mitochondria within skeletal muscle declines by 66% with age when compared with younger counterparts (38).
Similar EM findings are documented in a human study, revealing a 25% decrease in the density of mitochondria within the vastus lateralis muscle of males and females aged greater than 60 years (39). Numerous studies have investigated whether aging has an effect on cardiolipin content or oxidation in cardiac muscle. One study in skeletal muscle has illustrated that cardiolipin content in 36-monthold rats is not decreased when compared with 6-month-old rats in isolated SS and IMF mitochondria (41). However, whether cardiolipin is oxidatively modified with age in skeletal muscle remains to be determined.
The morphology of mitochondria may also be altered with age in skeletal muscle, in that a proportion of the organelles are enlarged, depolarized, and non-functional. When compared with the elongated morphology of mitochondria in skeletal muscles of young animals, mitochondria tend to be more rounded in shape within aged skeletal muscle, suggesting that mitochondrial fusion events may be impaired in skeletal muscle. Indeed, decreased OPA1 protein expression has been documented in experimentally-generated, giant mitochondria which may have physiological relevance to the morphology of mitochondria seen in aged individuals (42). Aged muscle also exhibits characteristics of decreased mitochondrial respiratory capacity and ETC enzyme activities.
As a result of decreased enzyme and complex activities, ATP synthesis and content within aged skeletal muscle is reduced. Thus, there is an increased probability of affecting cellular processes reliant on a constant supply of ATP, such as muscle contractions, protein turnover, and the maintenance of membrane potential. Skeletal muscle oxidative capacity is a reflection of the ability of working muscle to regenerate ATP through aerobic metabolism. Studies support that whole body maximal oxygen consumption (VO2max) declines with age and there is reduced aerobic capacity per kilogram of muscle in late-middle aged individuals.
Assessments of mitochondrial respiration that was stimulated with a variety of substrates in the presence of ADP revealed that this parameter decreased in aged skeletal muscle.
At rest, muscle ATP synthesis was reduced in 30-month, compared with 7-month-old mice (46).

The selection of muscle studied, and the method of preparation are also not standardized, such that measurements have been made using either whole muscle homogenates or isolated mitochondrial populations. It is very possible that these skeletal muscle mitochondrial populations are affected differentially by the aging process.
Ingestion of whey hydrolysate, casein, or soy protein isolate: Effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. Thus, it is controversial whether mitochondrial dysfunction is due to aging per se, or whether the lack of regular physical activity is the major reason for the divergent age-related phenotypes of skeletal muscle.
Causes for the alternations in mitochondrial biogenesis associated with aged skeletal muscleThe impairment in mitochondrial biogenesis may be due to a plethora of causes that lead to the propagation of mitochondrial dysfunction. Dysregulated experssion of mitochondrial genesDeclines in mitochondrial content and function may be related to the altered expression of nuclear genes encoding mitochondrial proteins (NUGEMPS) in skeletal muscle of the elderly. The huge reliance of mitochondria on the nuclear genome suggests that impaired protein synthesis rates could lead to the decline in mitochondrial biogenesis that is observed with old age, especially if the transcription of NUGEMPS is decreased with age.
This increased expression of ribosomal subunits may represent a compensatory response for decreased translational efficiency, particularly because protein synthesis has been illustrated to decrease with age. However, in response to the decline in mitochondrial respiratory function, compensatory increases in mtDNA content in tissues such as skeletal muscle, kidney, and cardiac muscle have been observed.
Similarly in humans, mtDNA content was significantly decreased in muscle biopsies obtained from 67-year-old subjects (50), whereas Welle et al. It has been illustrated that in skeletal muscle of aged humans the rate of mitochondrial protein synthesis is decreased and this may have contributed to the decrease in COX and CS activities observed.
Impaired regulation of protein degradtionMitochondrial function and morphology depend on the balance between protein synthesis and assembly, and the clearance of damaged or improperly assembled proteins. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. These effects likely manifest as decreased ATP synthesis, increased ROS generation, accumulated mtDNA mutations and cell death, characteristics which are observed in skeletal muscle of aging individuals. The major pathways that contribute to mitochondrial protein quality control include intramitochondrial proteases and autophagy. Studies have illustrated that with increasing age, the activity and expression of the intramitochondrial Lon protease is reduced, reflected by an accumulation of dysfunctional aconitase (52). Decreased activity of the Lon protease is likely due to oxidative modifications by elevated ROS levels within the mitochondrial matrix. In the cytosolic environment, lipofuscin has been implicated in contributing to the progressive decline in mitochondrial protein turnover and the onset of dysfunction that occurs with age. Lipofuscin, referred to as the aging pigment, is a non-degradable protein that is the product of incomplete autophagic degradation followed by the peroxidation of remaining contents within the lysosome by reactive oxygen species. Thus, it appears that the activities of these housekeeping pathways related to protein quality control are altered with aging, resulting in the accumulation of damaged mitochondria and cellular dysfunction.
Elevated damege to macromolecules by ROSResearch unequivocally indicates that ROS production increases in aging skeletal muscle (54). Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise.
One consequence of increased aberrant ROS production is oxidative damage to complex V leading to a decrease in ATP synthesis and content within skeletal muscle.
Additionally, increases in oxidative modifications in DNA occur with age, reflected by higher levels of 8-oxodeoxyguanosine, (8-oxoG) and the corresponding repair enzyme, 8-oxoguanine-DNA glycosylase 1 (OGG1) in skeletal muscle.
Increased levels of protein carbonyls have also been associated with aging skeletal muscle.
Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage. One study suggests that there is no change in the content of MnSOD in SS and IMF mitochondria from tibialis anterior and extensor digitorum longus muscles of aged, compared with young animals.
In cardiac muscle, IMF mitochondria exhibit increased levels of GPX, CAT, and MnSOD with age, whereas SS mitochondria exhibit increased levels of GPX and MnSOD and a decrease in CAT activity (62).
Because it is clear that oxidative modifications to mitochondrial macromolecules are indeed occurring in skeletal muscle with age, it is likely that the increased ROS production overwhelms the buffering capacity of the antioxidant enzymes that are available.
Elevated mutation in mtDNAAn important component of the free radical theory of aging is that mitochondrial dysfunction is a result of accumulated oxidative damage to mtDNA, leading to mutations in coding regions for ETC proteins.
The last point is especially critical because mtDNA contains no introns or spacer regions (63), thus even point mutations could lead to the expression of faulty proteins. It is accepted that ROS generation by skeletal muscle mitochondria increases with age and is accompanied by an increase in mtDNA mutations, impaired energy production, mitochondrial dysfunction, and a greater susceptibility to undergo apoptotic signalling that results in the downfall of skeletal muscle function.
In addition, mtDNA deletion mutations appear to be highly localized in small regions of muscle fibers in mosaic patterns, rather than distributed ubiquitously throughout aged skeletal muscle. Genetically altered mice lacking DNA polymerase gamma (Polg) activity exhibited an elevated accumulation of random mtDNA point mutations, in conjunction with a severe deficiency in ATP synthesis and the early onset of aging-related phenotypes.
Resistance exercise enhances myofibrillar protein synthesis with graded intakes of whey protein in older men. However, these occurred in the absence of increased ROS production, protein carbonylation or mtDNA damage (66). Uncoupling of oxidative phosphorylationCoupling of the energy generated from electron transfer through the respiratory complexes to the synthesis of ATP is a major function of the mitochondrial network. However, the flow of protons through complex V can be bypassed and redirected through protein channels which serve to uncouple respiration. The result of uncoupling is a decrease in ATP synthesis, despite increased oxygen consumption and respiratory rates (69).
Another study supplemented this finding with the observation that uncoupling occurs in human skeletal muscle of subjects greater than 65 year of age that was accompanied with reduced ATP content (70).
In the same study, it was determined that uncoupling affects muscles with a high type II fibre composition, compared with those that are composed of predominately type I fibers (41). Potential causes for uncoupling of oxidative phosphorylation occurring with age may involve the increased activity and expression of uncoupling protein 3 (UCP3) that can be stimulated by oxidative stress. An increased activity of UCP3 has been proposed to lend protection to the cell, in response to increased oxidative stress that occurs with age.
Whether the expression of uncoupling proteins in skeletal muscle is altered with aging is not well established. Some studies have observed a trend for increased UCP3 content (43), whereas others have suggested there is an age-related decrease or no change in this protein content (46, 71). Potential of exercise to attenuate age-related mitochondrial dysfunctionAlthough it has long been established that exercise training increases, and muscle disuse decreases, the activity of mitochondrial oxidative enzymes in skeletal muscle, a lack of consideration of this notion in aging studies has led to discrepancies in our overall understanding of the effect of aging on muscle mitochondrial function.
This likely happens through increases in expression of the coactivator PGC-1a and the specific transcription factors NRF-1 and Tfam, the main regulators of organelle biogenesis and protein expression.
One can assume that if mitochondrial function deteriorates with age, organelle biogenesis induced by exercise may attenuate this age-related decline, and therefore may have a protective role. However, despite the fact that exercise-induced increases in enzyme activities and mitochondrial content have been reported in aging individuals, less is known about the effects of exercise on the expansion of mtDNA mutations, ROS balance, and apoptosis in aged skeletal muscle. For example, in patients suffering from mitochondrial diseases due to mtDNA mutations, the introduction of an exercise program to improve muscle oxidative capacity and mitochondrial function has been approached with caution. In those patients, exercise induced mitochondrial biogenesis but also increased both wild-type and mutant mtDNA, worsening the heteroplasmy ratio in muscle fibers (73). However, in view of the evidence that chronic exercise can attenuate proapoptotic protein release from mitochondria in young animals, and reduce ROS production in intermyofibrillar mitochondria, it is worth investigating whether exercise can attenuate he enhanced apoptotic susceptibility evident in muscle from aged individuals. This may occur through the exercise-induced increase in mitochondrial content, a better redistribution of electrons through the electron transport chain, and (or) a better coupling between oxygen consumption and ATP synthesis in the exercised muscle of old animals.
ConclussionSkeletal muscle is a remarkably adaptive tissue that is capable of changing its morphological, physiological, and biochemical properties in response to various perturbations.
Mitochondrial biogenesis is a very complex cellular process that requires the coordination of several mechanisms involving nuclear-mitochondrial corporation, mitochondrial protein expression and import, mtDNA gene expression, transcription factors activity, assembly of multisubunit enzyme complexes, regulation of mitochondrial fission and fusion as well as mitochondrial turnover.

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