Amino Acid and Energy Metabolism in Septic and Traumatized Patients

Clowes, G. H. A.; Randall, Henry T.; Cha, Chung-Ja

doi:10.1177/014860718000400225

Cited by 169 publications

(27 citation statements)

References 32 publications

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“…As an acute phase protein, fibrinogen is commonly observed to increase under stressed situations (21)(22)(23). Metabolic changes from trauma injury or stress are generalized by an increase in whole body protein turnover rate, with a net loss of host body protein (21)(22)(23).…”

Section: Discussionmentioning

confidence: 99%

“…Metabolic changes from trauma injury or stress are generalized by an increase in whole body protein turnover rate, with a net loss of host body protein (21)(22)(23). Specifically, there is an increase of amino acid release from the muscle and an increase of amino acid uptake in the splenic bed (22). This shift of amino acid sources from muscle to the liver is hypothesized to be beneficial because it facilitates the liver's synthesis of proteins, which are critical for survival (24).…”

Section: Discussionmentioning

confidence: 99%

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Fibrinogen Availability and Coagulation Function after Hemorrhage and Resuscitation in Pigs

Martini

2011

Mol Med

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Fibrinogen Availability and Coagulation Function after Hemorrhage and Resuscitation in Pigs

Martini

2011

Mol Med

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“…Considering that the mean fraction of forearm made up of muscle tissue is about 0.6 (58), that forearm blood flow in forearm muscle is about 70% of total flow (58), that muscle is on the average 40% of body weight, that phenylalanine is about 4-5% of actin composition (59), and that muscle is composed by 20% proteins, the change in net phenylalanine release from the forearm after rhGH would account for a less negative muscle balance of about 18-20 g/d. This is in keeping with an increase in muscle mass of about 20 g/d observed in GH-deficient patients during GH repletion therapy (54).…”

Section: Discussionmentioning

confidence: 99%

Effects of recombinant human growth hormone on muscle protein turnover in malnourished hemodialysis patients.

Garibotto¹,

Barreca²,

Russo³

et al. 1997

J. Clin. Invest.

106

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To assess the effect of recombinant human growth hormone (rhGH) on muscle protein metabolism in uremic patients with malnutrition, forearm [ 3 H]phenylalanine kinetics were evaluated in six chronically wasted (body weight 79% of ideal weight) hemodialysis (HD) patients in a self-controlled, crossover study. Forearm protein dynamics were evaluated before, after a 6-wk course of rhGH (5 mg thrice weekly) and after a 6-wk washout period. After rhGH: ( a ) forearm phenylalanine net balance-the difference between phenylalanine incorporation into and phenylalanine release from muscle proteins-decreased by 46% ( Ϫ 8 Ϯ 2 vs. Ϫ 15 Ϯ 2 nmol/min·100 ml at the baseline and Ϫ 11 Ϯ 2 after washout,

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“…Glutamine synthetase increases dramatically in atrophic muscle as a result of chronic exposure to glucocorticoids (26) or denervation (16). Glutamine synthetase catalyzes de novo glutamine synthesis from glutamate and ammonia, thus maintaining glutamine homeostasis under conditions of increased glutamine demand by other tissues (13) or as a result of its limited supply. Muscle atrophy induces glutamine efflux, thereby depleting muscle glutamine stores (28).…”

Section: Rna Processing Protein Biosynthesis and Modificationmentioning

confidence: 99%

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

Salem

Kenney

Rexroad

et al. 2006

Physiological Genomics

115

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Salem M, Kenney PB, Rexroad CE 3rd, Yao J. Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model. Physiol Genomics 28: 33-45, 2006. First published August 1, 2006; doi:10.1152/physiolgenomics.00114.2006.-Muscle atrophy is a physiological response to diverse physiological and pathological conditions that trigger muscle deterioration through specific cellular mechanisms. Despite different signals, the biochemical changes in atrophying muscle share many common cascades. Muscle deterioration as a physiological response to the energetic demands of fish vitellogenesis represents a unique model for studying the mechanisms of muscle degradation in non-mammalian animals. A salmonid microarray, containing 16,006 cDNAs, was used to study the transcriptome response to atrophy of fast-switch muscles from gravid rainbow trout compared with sterile fish. Eighty-two unique transcripts were upregulated and 120 transcripts were downregulated in atrophying muscles. Transcripts having gene ontology identifiers were grouped according to their functions. Muscle deterioration was associated with elevated expression of genes involved in the catheptic and collagenase proteolytic pathways; the aerobic production, buffering, and utilization of ATP; and growth arrest; whereas atrophying muscle showed downregulation of genes encoding a serine proteinase inhibitor, enzymes of anaerobic respiration, muscle proteins as well as genes required for RNA and protein biosynthesis/processing. Therefore, gene transcription of the trout muscle atrophy changed in a manner similar to mammalian muscle atrophy. These changes result in an arrest of normal cell growth, protein degradation, and decreased glycolytic cellular respiration that is characteristic of the fast-switch muscle. For the first time, other changes/mechanisms unique to fish were discussed including genes associated with muscle atrophy. atrophy; Oncorhynchus mykiss SEVERAL PHYSIOLOGICAL and pathological conditions can cause muscle atrophy by triggering unique responses through distinct cellular stimuli. Transcriptional mechanisms of muscle wastage are well characterized at the transcriptome level in mammalian models as a response to nutritional restriction (7), fasting, severe diseases, including cancer, renal failure, diabetes (41, 42), and sepsis (42), as well as muscle disuse or denervation (4, 57). Some studies have dealt with fish muscle atrophy at the level of individual genes/mechanisms (46, 51, 58, 60 -62). The molecular basis of mammalian muscle atrophy has received considerable attention in the literature (25,30). Losing muscle mass results from elevated rate of proteolysis and decreased rate of protein synthesis. Despite the significant amount of literature (30,32,42), the specific roles of the proteolytic systems in degrading mammalian muscle still are unclear. Moreover, we recently showed that fish use different muscle degrading proteolytic strategies compared with mammals (58). The ubiquitin-proteasome pathway,...

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Amino Acid and Energy Metabolism in Septic and Traumatized Patients

Cited by 169 publications

References 32 publications

Fibrinogen Availability and Coagulation Function after Hemorrhage and Resuscitation in Pigs

Fibrinogen Availability and Coagulation Function after Hemorrhage and Resuscitation in Pigs

Effects of recombinant human growth hormone on muscle protein turnover in malnourished hemodialysis patients.

Microarray gene expression analysis in atrophying rainbow trout muscle: a unique nonmammalian muscle degradation model

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