An integrative approach to in-vivo protein synthesis measurement: from whole tissue to specific proteins

Guillet, Christelle; Boirie‌, Yves; Walrand, Stéphane

doi:10.1097/00075197-200409000-00005

Cited by 29 publications

(16 citation statements)

References 39 publications

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“…127 However, muscle biopsies are required for precise quantification of skeletal muscle protein synthesis. Even though these have not been reported in human patients with cirrhosis, whole body amino acid kinetic studies showed lower rates of protein synthesis in patients with cirrhosis than in controls.…”

Section: Pathogenesis and Mechanisms Of Sarcopenia In Cirrhosismentioning

confidence: 99%

Malnutrition in Cirrhosis: Contribution and Consequences of Sarcopenia on Metabolic and Clinical Responses

Periyalwar¹,

Dasarathy²

2012

Clinics in Liver Disease

212

232

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Section: Pathogenesis and Mechanisms Of Sarcopenia In Cirrhosismentioning

confidence: 99%

Malnutrition in Cirrhosis: Contribution and Consequences of Sarcopenia on Metabolic and Clinical Responses

Periyalwar¹,

Dasarathy²

2012

Clinics in Liver Disease

212

232

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“…In addition to the inconvenience of long term administration of amino acid tracers and difficulties in determining the true precursor labeling, these methods are hampered by low isotopic labeling of protein products and difficulties with data interpretation related to determining the precursor-product labeling ratio. Classical protein turnover studies were also often limited to investigating of the kinetics of an individual or mixed protein pool in whole body or specific organs (5). Recent advances in protein sequencing allowed the assessment of the turnover rates of multiple individual proteins simultaneously (6).…”

mentioning

confidence: 99%

Plasma Proteome Dynamics: Analysis of Lipoproteins and Acute Phase Response Proteins with 2H2O Metabolic Labeling

Willard

Rachdaoui

et al. 2012

Molecular & Cellular Proteomics

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Understanding the pathologies related to the regulation of protein metabolism requires methods for studying the kinetics of individual proteins. We developed a 2 H 2 O metabolic labeling technique and software for protein kinetic studies in free living organisms. This approach for proteome dynamic studies requires the measurement of total body water enrichments by GC-MS, isotopic distribution of the tryptic peptide by LC-MS/MS, and estimation of the asymptotical number of deuterium incorporated into a peptide by software. We applied this technique to measure the synthesis rates of several plasma lipoproteins and acute phase response proteins in rats. Samples were collected at different time points, and proteins were separated by a gradient gel electrophoresis.2 H labeling of tryptic peptides was analyzed by ion trap tandem mass spectrometry (LTQ MS/MS) for measurement of the fractional synthesis rates of plasma proteins. The high sensitivity of LTQ MS in zoom scan mode in combination with 2 H label amplification in proteolytic peptides allows detection of the changes in plasma protein synthesis related to animal nutritional status. Our results demonstrate that fasting has divergent effects on the rate of synthesis of plasma proteins, increasing synthesis of ApoB 100 but decreasing formation of albumin and fibrinogen. We conclude that this technique can effectively measure the synthesis of plasma proteins and can be used to study the regulation of protein homeostasis under physiological and pathological conditions.

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“…Skeletal muscles are the major deposit of protein molecules (about 40% of body weight in young males with 20-22% body mass index, (expressed as kg.m −2 ), and nearly 60% of total body protein in humans. Other organs or tissues contain proteins such as the liver which synthesizes plasma proteins (including albumin which represents nearly 50% of liver proteins), immune cells (mainly leucocytes), intestinal tract proteins (digestive enzymes), bone and dermal collagen [1]. For any cell or tissue, protein balance reflects the net protein synthesis and protein degradation which differs drastically among tissues and organs, between cell compartments.…”

Section: General View Of Protein Metabolism In Humansmentioning

confidence: 99%

Protein metabolism and physical training: any need for amino acid supplementation?

Poortmans

Carpentier

2016

Nutrire

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Muscle mass is the major deposit of protein molecules with dynamic turnover between net protein synthesis and degradation. In human subjects, invasive and non-invasive techniques have been applied to determine their skeletal muscle catabolism of amino acids at rest, during and after different forms of physical exercise and training. The aim of this review is to analyse the turnover flux and the relative oxidation rate of different types of muscle proteins after one bout of exercise as well as after resistance and endurance condition of training. Protein feeding in athletes appears to be a crucial nutrition necessity to promote the maintenance of muscle mass and its adaptation to the need imposed by the imposed technical requirements. In resting human individuals, the recommended protein daily allowance is about 0.8 g (dry weight) kg −1 body weight per 24 h knowing that humans are unable to accumulate protein stores in muscle tissues. Nevertheless, practical feeding recommendations related to regular exercise practice are proposed to athletes by different bodies in order to foster their skills and performance. This review will examine the results obtained under endurance and resistance type of exercise while consuming single or repeated doses of various ingestions of protein products (full meat, essential amino acids, specific amino acids and derivatives, vegetarian food). From the scientific literature, it appears that healthy athletes (and heavy workers) should have a common diet of 1.25 g kg −1 24 h to compensate the exercise training muscle protein degradation and their resynthesis within the following hours. A nitrogen-balance assay would be recommended to avoid any excessive intake of protein. Eventually, a daily equilibrated food intake would be of primer importance versus inadequate absorption of some specific by-products.

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An integrative approach to in-vivo protein synthesis measurement: from whole tissue to specific proteins

Cited by 29 publications

References 39 publications

Malnutrition in Cirrhosis: Contribution and Consequences of Sarcopenia on Metabolic and Clinical Responses

Malnutrition in Cirrhosis: Contribution and Consequences of Sarcopenia on Metabolic and Clinical Responses

Plasma Proteome Dynamics: Analysis of Lipoproteins and Acute Phase Response Proteins with 2H2O Metabolic Labeling

Protein metabolism and physical training: any need for amino acid supplementation?

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