Measurement of tissue protein synthesis rates in vivo: a critical analysis of contrasting methods.

The extension of the flooding method for measuring the rate of protein synthesis, from animal to human tissues, has led to criticism. This is based on the observation that in human muscle, unlike animal tissues, the rate of synthesis in the fasting state measured with constant infusion is lower than that obtained with the flooding technique. Moreover, incorporation of infused tracer can be enhanced with a simultaneous flood, although an inhibition of incorporation has also been reported. Explanations for these observed discrepancies are explored. Evidence from studies in human muscle both with flooding and with a nonisotopic technique have given no indication of a stimulation of protein synthesis during flooding. It is therefore concluded that the most likely explanation for the discrepancy between methods is that changes in the isotopic enrichment of the precursor amino acid, which are minimized by the flooding procedure, are not adequately accounted for with the constant infusion method.

[1]  P. Essén,et al.  Muscle protein synthesis after operation: effects of intravenous nutrition. , 1993, The European journal of surgery = Acta chirurgica.

[2]  D. Chinkes,et al.  Assessment of the mathematical issues involved in measuring the fractional synthesis rate of protein using the flooding dose technique. , 1993, Clinical science.

[3]  D. McMillan,et al.  Elevated circulating interleukin-6 is associated with an acute-phase response but reduced fixed hepatic protein synthesis in patients with cancer. , 1991, Annals of surgery.

[4]  C. Scrimgeour,et al.  Increase in anterior tibialis muscle protein synthesis in healthy man during mixed amino acid infusion: studies of incorporation of [1-13C]leucine. , 1989, Clinical science.

[5]  E. Aurousseau,et al.  Contribution of liver, skin and skeletal muscle to whole-body protein synthesis in the young lamb , 1988, British Journal of Nutrition.

[6]  J. Cortner,et al.  Direct measurement of apolipoprotein B synthesis in human very low density lipoprotein using stable isotopes and mass spectrometry. , 1986, Journal of lipid research.

[7]  D. J. Millward,et al.  Myofibrillar protein turnover. Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation. , 1983, The Biochemical journal.

[8]  D. J. Millward,et al.  Myofibrillar protein turnover. Synthesis of protein-bound 3-methylhistidine, actin, myosin heavy chain and aldolase in rat skeletal muscle in the fed and starved states. , 1983, The Biochemical journal.

[9]  F. Ballard Regulation of protein accumulation in cultured cells. , 1982, The Biochemical journal.

[10]  R. Conde,et al.  Role of protein degradation in the growth of livers after a nutritional shift. , 1976, The Biochemical journal.

[11]  E. Fern,et al.  Compartmentation of albumin and ferritin synthesis in rat liver in vivo. , 1976, The Biochemical journal.

[12]  A. Lajtha,et al.  A METHOD FOR MEASURING BRAIN PROTEIN SYNTHESIS RATES IN YOUNG AND ADULT RATS , 1975, Journal of neurochemistry.

[13]  E. Khairallah,et al.  Compartmentation of free amino acids for protein synthesis in rat liver. , 1974, The Biochemical journal.

[14]  E. Fern,et al.  The specific radioactivity of the precursor pool for estimates of the rate of protein synthesis. , 1973, The Biochemical journal.