During four days of fasting in rats skeletal muscle protein synthesis fell pro-gressively, whereas skeletal muscle protein breakdown was unchanged until the third and fourth days when it rose dramatically. In contrast, the synthetic rate of smooth muscle protein was unchanged during three days of fasting despite a loss of protein content, indicating an abrupt rise in protein breakdown in this tissue on the first day of fasting which was sustained thereafter. Urinary excretion of Nτ-methylhistidine was significantly increased throughout fasting. The concentration of free Nτ-methylhistidine in plasma and in muscle tissue was elevated throughout the period of fasting. This elevation was not caused by reduced renal clearance, but appears to have been mainly the result of increased breakdown of Nτ-methylhistidine-containing proteins in tissues other than skeletal muscle.
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February 01 1986
Different patterns of protein turnover in skeletal and gastrointestinal smooth muscle and the production of Nτ-methylhistidine during fasting in the rat
Peter W. Emery;
Peter W. Emery
1Department of Nutrition, Kings College (KQC), London W8 7AH
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Laura Cotellessa;
Laura Cotellessa
2Department of Medicine, University College, London WC1E 6JJ
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Mark Holness;
Mark Holness
2Department of Medicine, University College, London WC1E 6JJ
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Christine Egan;
Christine Egan
3Department of Physiology, University of Dundee, Dundee DD1 4HN
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Michael J. Rennie
Michael J. Rennie
3Department of Physiology, University of Dundee, Dundee DD1 4HN
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Publisher: Portland Press Ltd
Received:
November 11 1985
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1986 Plenum Publishing Corporation
1986
Biosci Rep (1986) 6 (2): 143–153.
Article history
Received:
November 11 1985
Citation
Peter W. Emery, Laura Cotellessa, Mark Holness, Christine Egan, Michael J. Rennie; Different patterns of protein turnover in skeletal and gastrointestinal smooth muscle and the production of Nτ-methylhistidine during fasting in the rat. Biosci Rep 1 February 1986; 6 (2): 143–153. doi: https://doi.org/10.1007/BF01115000
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