Effect of exercise and recovery on muscle protein synthesis in human subjects

Carraro, Fabio; Stuart, Charles Alexander; Hartl, Wolfgang H.; Rosenblatt, Judah; Wolfe, Robert R.

doi:10.1152/ajpendo.1990.259.4.e470

Cited by 165 publications

(158 citation statements)

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“…10 completed a session of weight-lifting exercise 2 h prior to the initiation of the tracer infusion experiment. We believe that the prior bout of exercise was the cause of this subject's elevated rate of muscle protein synthesis because (i) Carraro et al 11 have observed an increased rate of muscle protein synthesis during recovery from mild aerobic exercise, and (ii) we have observed an increase in muscle protein synthesis rate in an additional 7 individuals studied in the same manner as those reported here, after a session of resistance exercise (manuscript in Preparation).…”

Section: Resultssupporting

confidence: 67%

“…[1][2][3][4][5][6][7][8][9][10][11][12][13] For example, the published values for quadriceps muscle protein synthesis rate in healthy normal subjects are 0.035-0.063% h −1 (SD = 0.009) by Nair et al, 13 0.033-0.064% h −1 (SD = 0.012) by Gibson et al, 1 and 0.036-0.063% h −1 (SD = 0.011) by Nair et al 8 These ranges and standard deviations compare closely with the values reported in the present study (0.023-0.070% h −1 , SD = 0.014) if subject no. 10 is excluded.…”

Section: Resultsmentioning

confidence: 99%

“…Over the last decade, measurement of the rate of skeletal muscle protein synthesis in vivo [1][2][3][4][5][6][7][8][9][10][11] has been achieved by infusing subjects with a stable isotopically labeled amino acid (e.g. (1-13 C)leucine, valine, phenylalanine) and measuring the rate of incorporation of the labeled amino acid into muscle protein.…”

Section: Introductionmentioning

confidence: 99%

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Measurement of muscle protein fractional synthetic rate by capillary gas chromatography/combustion isotope ratio mass spectrometry

Yarasheski

Smith

Rennie

et al. 1992

Biol. Mass Spectrom.

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The measurement of skeletal muscle protein fractional synthetic rate using an infusion of (1-13 C)leucine and measuring the isotopic abundance of the tracer in skeletal muscle protein by preparative gas chromatography (GC)/ninhydrin isotope ratio mass spectrometry (IRMS) is laborious and subject to errors owing to contamination by 12 C. The purpose of this study was to compare muscle ( 13 C)leucine enrichment measured with the conventional preparative GC/ ninhydrin IRMS approach to a new, continuous-flow technique using capillary GC/combustion IRMS. Quadriceps muscles were removed from four Sprague-Dawley rats after each was infused at a different rate with (1-13 C)leucine for 6-8 h. Muscle leucine enrichment (at.% excess) measured by both methods differed by less than 4%, except at low ( 13 C)leucine enrichments (<0.03 at.% excess). In addition, capillary GC/combustion IRMS was used to assess muscle ( 13 C)leucine enrichment and fractional muscle protein synthesis rate in ten normal young men and women infused with (1,2-13 C 2 )leucine for 12-14 h. This approach reduced the variability of the isotope abundance measure and gave estimates of muscle protein synthesis rate (0.050 ± 0.011% h −1 (mean ± SEM); range = 0.023-0.147% h −1 ) that agree with published values determined using the standard analytical approach. The measurement of ( 13 C)leucine enrichment from skeletal muscle protein by capillary GC/combustion IRMS provides a simple, acceptable and practical alternative to preparative GC/ninhydrin IRMS.

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Section: Resultssupporting

confidence: 67%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Measurement of muscle protein fractional synthetic rate by capillary gas chromatography/combustion isotope ratio mass spectrometry

Yarasheski

Smith

Rennie

et al. 1992

Biol. Mass Spectrom.

View full text Add to dashboard Cite

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“…In humans, resistance exercise increases protein synthesis [97][98][99][100][101][102][103][104][105][106] and improves protein balance during the recovery phase in the skeletal muscle, 8,107,108 but not during acute bouts of resistance exercise. 109 Similar to resistance exercise, low intensity aerobic training 110 causes a significant increase in fractional synthetic rate in the leg muscle. In contrast, in female deltoid muscle, neither resistance nor swimming exercise, when performed separately, had a significant effect on net muscle protein synthesis, but when combined stimulated increased muscle protein synthesis above baseline levels.…”

Section: A Correspondence Between Immune and Muscle Cellsmentioning

confidence: 99%

Heat shock response and autophagy—cooperation and control

2015

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Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

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“…Each subject underwent a percutaneous biopsy of vastus lateralis before beginning medication and at the end of 8 weeks of treatment. The muscle biopsy was performed after an overnight fast and 2 h of quiet recumbency as previously described (9). Patients were instructed to maintain their prestudy activity and diet programs throughout the 8-week study.…”

Section: Patients and Clinical Protocolmentioning

confidence: 99%

Overexpression of GLUT5 in Diabetic Muscle Is Reversed by Pioglitazone

2007

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OBJECTIVE -This study was undertaken to quantify the expression of muscle GLUT in type 2 diabetes and to determine if treatment with an insulin-enhancing thiazolidenedione drug, pioglitazone, would alter its expression.RESEARCH DESIGN AND METHODS -Twelve patients with type 2 diabetes were randomly assigned to treatment with either pioglitazone or placebo in a double-blinded 8-week protocol. Protein and mRNA for GLUT4 and GLUT5 were quantified in muscle homogenates from biopsies of vastus lateralis before and after treatment. The five additional GLUT family isoforms expressed in muscle had mRNA quantified in these samples.RESULTS -Baseline and posttreatment repeat measurements of GLUT4 protein were not different from control measurements. Compared with normal subjects, GLUT5 protein increased 2.5-fold, and GLUT5 mRNA was 82% higher in the pretreatment samples from the diabetic subjects. Concentrations of mRNA for the six other GLUTs (GLUT1, GLUT3, GLUT4, GLUT8, GLUT11, and GLUT12) were not different from control subjects before or after treatment. The proportion of type I (red) fibers (46%) in diabetic muscle was not affected by pioglitazone treatment. Pioglitazone treatment decreased muscle GLUT5 mRNA and protein by 52 and 40%, respectively, whereas placebo did not alter GLUT5 expression. Both red and white fibers had higher GLUT5 expression in the baseline diabetic muscle samples, and a pioglitazonerelated decrease in GLUT5 protein also occurred in both.CONCLUSIONS -GLUT5 was dramatically increased in diabetic muscle, and pioglitazone treatment reversed this overexpression. The role of this fructose transporter expression in the insulin-enhancing effect of pioglitazone in muscle is unclear. Diabetes Care 30:925-931, 2007T hiazolidenedione drugs facilitate insulin action in patients with type 2 diabetes manifested by improved glycemic control and a decrease in endogenous insulin secretion (1,2). Drugs from this class robustly bind to the nuclear factor peroxisome proliferator-activator receptor-␥ and activate multiple gene cassettes (1,3). There are differences in some of the genes activated by members of this class (troglitazone, rosiglitazone, and pioglitazone), but changes in many genes are similar for these three drugs (1,4,5). The specific genes whose activation or suppression are responsible for enhanced insulin action are unclear. The study we describe here was designed to determine if pioglitazone-induced enhanced insulin action on glucose uptake could be associated with an increase in expression of one or more GLUTs in skeletal muscle. We have previously shown (6) that seven members of the GLUT family of hexose transporters are expressed in human skeletal muscle, with mRNAs for GLUT4, GLUT5, and GLUT12 predominating. Among these facilitative hexose transporters, GLUT5 is unique in that it transports only fructose (7). High dietary fructose (but not glucose) content has been shown to directly increase intestinal expression of Glut5 in a rat model (8). The current study demonstrated that mRNA concentratio...

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Effect of exercise and recovery on muscle protein synthesis in human subjects

Cited by 165 publications

References 1 publication

Measurement of muscle protein fractional synthetic rate by capillary gas chromatography/combustion isotope ratio mass spectrometry

Measurement of muscle protein fractional synthetic rate by capillary gas chromatography/combustion isotope ratio mass spectrometry

Heat shock response and autophagy—cooperation and control

Overexpression of GLUT5 in Diabetic Muscle Is Reversed by Pioglitazone

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