Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle.

Tiao, Greg; Hobler, Scott C.; Wang, Jing Jing; Meyer, Tory A.; Luchette, Fred A.; Fischer, Josef E.; Hasselgren, Per Olof

doi:10.1172/jci119143

Cited by 236 publications

(122 citation statements)

References 34 publications

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“…The increase in 26S proteasome activity during detraining is in agreement with studies reporting increased expression during muscle catabolism (e.g. sepsis, Tiao et al 1997 …”

supporting

confidence: 91%

Human Physiology

1999

The Journal of Physiology

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The purpose of the experiment, which had ethical committee approval, was to investigate for the first time the effect of carbohydrate (CHO) ingestion on post-exercise glycogen resynthesis, measured simultaneously in human liver and skeletal muscle, and subsequent exercise capacity. Ten healthy, well-trained and familiarized males cycled at 70 % maximal oxygen uptake for 83 ± 8 min, on six separate occasions. Subjects then ingested 1 g (kg body massr l (BM) glucose (18'5% w/v; condition A) or sucrose (18'5% w/v; B), or an equivalent volume of placebo (control; C). Over the following 4 h, muscle and liver glycogen content was measured by 13C MRS (occasions 1-3).Liver spectra and volume measurements were obtained pre-and post-exercise, within 30 min after CHO ingestion and hourly thereafter. Muscle spectra and volume measurements were obtained from 30-60 min and hourly thereafter. Subsequent exercise capacity was measured on occasions 4-6. To do this, the above procedures were repeated with the omission of the glycogen measurements and, at the end of the 4 h recovery period, exercise time to exhaustion was measured. Values are given as means ± S.E.M. Data were analysed by two-way repeated measures ANOVA. Liver and muscle glycogen content declined during the initial bout of exercise by ~60 % in all trials (P < 0'05). No glycogen was resynthesized during the control trial. Liver glycogen resynthesis was evident following glucose (13 ± 8 g) and sucrose (25 ± 5 g) ingestion, both of which were different from control (P < 0'01).A relationship between the CHO load (g) and change in liver glycogen content (g) was evident after 30, 90, 150 and 210 min of recovery (r = 0'59-0'79, P < 0'05). Furthermore, a modest relationship existed between the change in liver glycogen content (g) and subsequent exercise capacity. Significant changes in muscle glycogen resynthesis were not demonstrated, due perhaps to the small CHO load and the large inter-individual variation in glycogen measurements.Peak blood glucose was highest following glucose ingestion (P < 0'05). Ammonia production tended to be lower during exercise bout 2 following CHO ingestion (P = 0'069). No significant difference in exercise capacity was found (C: 35 ± 5; A: 40 ± 5; B: 46 ± 6 min).Therefore, 1 g (kg BMr 1 glucose or sucrose is sufficient to initiate post-exercise liver glycogen resynthesis, which Journal of Physiology (1999) It has been reported than an increase in cellular creatine (Cl') availability can increase lean tissue mass (Kreider et al. 1988) and stimulate mitochondrial respiration (Wyss et al. 1992). As a decrease in cellular Cr availability has been implicated in the disruption of energy metabolism in failing myocardium (Conway et al. 1998), this raises the possibility that Cr supplementation may be beneficial in cardiac disease states. However, there are presently little or no data available concerning the effects of Cr supplementation on myocardial creatine accumulation and creatine transporter mRNA (CrT mRNA) content. Therefore, the aim of t...

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“…The increase in 26S proteasome activity during detraining is in agreement with studies reporting increased expression during muscle catabolism (e.g. sepsis, Tiao et al 1997 …”

supporting

confidence: 91%

Human Physiology

1999

The Journal of Physiology

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“…& Takaki Yoshikawa yoshikawat@kcch.jp which, as well as acting as mediators of both immune and systemic responses to injury [6], cause muscle catabolism characterized by a rapid decrease in the protein content and accelerated amino acid release [7,8]. The levels of these cytokines reportedly peak and decrease to normal levels by day 7 [9].…”

Section: Introductionmentioning

confidence: 99%

Body composition analysis within 1 month after gastrectomy for gastric cancer

et al. 2015

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Background A significant body weight loss (BWL) is observed during 1 month after gastrectomy for gastric cancer. However, it remains unclear which body component mainly accounts for the weight loss. Methods Two-hundred forty-four patients who underwent gastrectomy for gastric cancer between May 2010 and October 2013 were examined. Body weight and composition were evaluated by a bioelectrical impedance analyzer within 1 week before surgery (first measurement), at 1 week after surgery (second measurement), and at 1 month after surgery (third measurement). The changes in the early period were defined as the differences until the second measurement, and those in the late period were defined as the differences from the second to the third measurement. Results Total BWL within 1 month was -3.4 kg, and the rate of body weight at 1 month to the preoperative body weight was 94.1 %. BWL was significantly greater in the early period than in the late period (-2.1 kg vs -1.2 kg, p \ 0.001). In the early period, loss of lean body mass was significantly greater than loss of fat mass (-1.5 kg vs -0.6 kg, p \ 0.001). The same trend was observed when the subset of patients who had surgical morbidities was excluded.Conclusion BWL during the first week after surgery was significantly greater than that during the subsequent 3 weeks. Furthermore, loss of lean body mass accounted for a significant part of the BWL during the first week.

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“…Furthermore, Hasselgren and Fischer [12] showed that dexamethasone (DEX) stimulates proteasome-and calcium-dependent proteolysis in the same cells [13]. Other studies [12,14] confirmed that sepsis induces proteolysis by activation of the ubiquitin-proteasome system, and that this activation was regulated by GCs [15]. These findings represent a unique situation where the increased GC levels described with sepsis are associated with upregulated GR levels in muscle cells, in contrast to most cells, where increased GCs levels are associated with GR downregulation.…”

Section: Introductionmentioning

confidence: 99%

TNF-α and glucocorticoid receptor interaction in L6 muscle cells: A cooperative downregulation of myosin heavy chain

2007

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Sepsis is associated with increased expression of TNF-α with subsequent activation of nuclear factorkappa B (NF-κB). The glucocorticoid receptor (GR) and NF-κB function as mutual antagonists and induction of the latter is believed to play a major role in the acquired glucocorticoid resistance that occurs in some septic patients. GR expression and function has been reported to be elevated in septic muscle suggesting a limited effect of the activated NF-κB on GR function in this context. In this study, the L6 myocyte cell line was used as an in vitro model for a sepsis-like condition in skeletal muscle. While short or long term treatment with TNF-α had no effect on GR expression, glucocorticoid-dependent downregulation of GR occurred with a kinetic profile that is accelerated relative to that observed in most cells. This downregulation was not affected by co-treatment or prior priming of L6 cells with TNF-α. The synthetic glucocorticoid, dexamethasone (DEX) blunted TNF-α-stimulated NF-κB activation in L6 cells. However, although effective at activating an NF-κB transcriptional response, TNF-α treatment exerted a minimal effect in myoblasts and no effect in myotubes on GR transcriptional activity. This limited impact of TNF-α on GR activity was not universal as TNF-α and DEX exerted an additive effect on the reduction in myosin heavy chain (MHC) protein expression caused by either agent alone. Thus, the selective perseverance of GR function in the presence of increased levels of glucocorticoids and TNF-α during sepsis or other inflammatory states may exacerbate muscle protein breakdown.

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Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle.

Cited by 236 publications

References 34 publications

Human Physiology

Human Physiology

Body composition analysis within 1 month after gastrectomy for gastric cancer

TNF-α and glucocorticoid receptor interaction in L6 muscle cells: A cooperative downregulation of myosin heavy chain

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