Measurement of Muscle Protein Synthetic Rate from Serial Muscle Biopsies and Total Body Protein Turnover in Man by Continuous Intravenous Infusion of l-[α-15N]lysine

Halliday, D.; McKeran, R O

doi:10.1042/cs0490581

Cited by 74 publications

(51 citation statements)

References 14 publications

(16 reference statements)

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“…The synthesis rate of the sarcoplasmic protein fraction was almost double that ofthe myofibrillar protein fraction in the heart, and the rate for total mixed muscle proteins was intermediate. Halliday & McKeran (1975) Millward & Garlick (1972), but no difference was found by Sender & Garlick (1973) in a heart perfused in vitro.…”

Section: Discussionmentioning

confidence: 80%

Protein synthesis during right-ventricular hypertrophy after pulmonary-artery stenosis in the dog

Everett¹,

Taylor²,

Sparrow³

1977

Biochemical Journal

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The rate of protein synthesis in the heart of normal dogs and those with pulmonary-artery stenosis was measured by a continuous intravenous infusion of ['4C]tyrosine. The protein-synthesis rate of both ventricles was the same in normal dogs and averaged 7.5 % per day. The right ventricle hypertrophied rapidly after the acute imposition of pulmonary-artery stenosis, the wet weight increasing by 84% after 24 days, with the rate of increase being most rapid over the first 5 days. The left ventricle remained largely unaffected and served as an internal control. During hypertrophy there was an increased incorporation of [14C]tyrosine into protein without a significant change in the specific radioactivity of free tyrosine in the ventricles. After 5 days of stenosis the synthesis rate ofthe total mixed proteins ofthe right ventricle had increased to 13.6 % per day, compared with 6.2 % in the control left ventricle. This increase in synthesis was reflected in both the myofibrillar and sarcoplasmic proteins. After 5 days the protein-synthesis rate decreased, but still remained significantly elevated above that in the control left ventricle by 24 days of stenosis.

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Section: Discussionmentioning

confidence: 80%

Protein synthesis during right-ventricular hypertrophy after pulmonary-artery stenosis in the dog

Everett¹,

Taylor²,

Sparrow³

1977

Biochemical Journal

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“…The FSRs for mitochondrial protein fraction were calculated by using the following equation (16,21):…”

Section: Methodsmentioning

confidence: 99%

Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts

Stump

Short

Bigelow

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

410

369

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Mitochondria are the primary site of skeletal muscle fuel metabolism and ATP production. Although insulin is a major regulator of fuel metabolism, its effect on mitochondrial ATP production is not known. Here we report increases in vastus lateralis muscle mitochondrial ATP production capacity (32-42%) in healthy humans (P < 0.01) i.v. infused with insulin (1.5 milliunits͞kg of fat-free mass per min) while clamping glucose, amino acids, glucagon, and growth hormone. Increased ATP production occurred in association with increased mRNA levels from both mitochondrial (NADH dehydrogenase subunit IV) and nuclear [cytochrome c oxidase (COX) subunit IV] genes (164 -180%) encoding mitochondrial proteins (P < 0.05). In addition, muscle mitochondrial protein synthesis, and COX and citrate synthase enzyme activities were increased by insulin (P < 0.05). Further studies demonstrated no effect of low to high insulin levels on muscle mitochondrial ATP production for people with type 2 diabetes mellitus, whereas matched nondiabetic controls increased 16 -26% (P < 0.02) when four different substrate combinations were used. In conclusion, insulin stimulates mitochondrial oxidative phosphorylation in skeletal muscle along with synthesis of gene transcripts and mitochondrial protein in human subjects. Skeletal muscle of type 2 diabetic patients has a reduced capacity to increase ATP production with high insulin levels.cytochrome c oxidase ͉ NADH dehydrogenase subunit IV ͉ amino acids ͉ citrate synthase

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“…Skeletal muscle, constituting 40% of the total protein content [22], amino acid flux over peripheral tissues [23,24], incorporation of stable isotopes by the constant infusion technique [25,26] and the flooding dose technique [27], and determination of the concentration and size distribution of ribosomes [4,17]. Although informative data concerning alterations in muscle protein metabolism may be obtained, none of these methods discriminate between myofibrillar and sarcoplasmatic proteins or give information about specific proteins.…”

Section: Discussionmentioning

confidence: 99%

Starvation Changes Muscle Myosin Heavy Chain Messenger RNA Accumulation.

Blomqvist

Decken

Vinnars

et al. 1991

J. Clin. Biochem. Nutr.

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SummaryThe level of mRNA specific for myosin heavy chain in percutaneous biopsy specimens of skeletal muscle was analyzed in 6 healthy volunteers before and following 3 days of total starvation. Total RNA was isolated and hybridized to a radioactively labeled cDNA probe specific for myosin heavy chain of the beta type. Increasing concentrations of total RNA were applied to the membrane filters used in the hybridization analysis. Slopes of the linear function of radioactivity versus RNA concentration were calculated by linear regression. Following starvation the amount of hybridizable mRNA specific for myosin heavy chain decreased in relation to the total RNA. The decrease was individually specific, the mean value of the slopes after starvation being 91.6±2.8% that of the control (prestarvation) level (p<0.01). The low serum concentrations of insulin and C-peptide and the rise in glucagon together with the increase in urinary nitrogen excretion characterized the fasting condition of the 6 healthy volunteers. The analysis of mRNA specific for a single myofibrillar protein gave information on the physiological state of protein synthesis in muscle and indicated a fall in synthetic capacity due to the diminished availability of mRNA. The diminished level of myosin heavy chain mRNA in relation to total RNA confirmed previous findings of a decrease in muscle protein synthesis during short-term starvation. The decrease in mRNA added to the known decrease in ribosomal RNA.

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Measurement of Muscle Protein Synthetic Rate from Serial Muscle Biopsies and Total Body Protein Turnover in Man by Continuous Intravenous Infusion of l-[α-15N]lysine

Cited by 74 publications

References 14 publications

Protein synthesis during right-ventricular hypertrophy after pulmonary-artery stenosis in the dog

Protein synthesis during right-ventricular hypertrophy after pulmonary-artery stenosis in the dog

Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts

Starvation Changes Muscle Myosin Heavy Chain Messenger RNA Accumulation.

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