Hostname: page-component-848d4c4894-x24gv Total loading time: 0 Render date: 2024-05-25T12:10:27.628Z Has data issue: false hasContentIssue false
  • English
  • Français

Measurement of muscle proteolysis and the impact on muscle wasting

Published online by Cambridge University Press:  28 February 2007

Steven Nissen
Steven Nissen
Affiliation:
Department of Animal Science, College of Agriculture, Iowa State University, Ames, Iowa 50011, USA
Rights & Permissions [Opens in a new window]

Abstract

An abstract is not available for this content so a preview has been provided. As you have access to this content, a full PDF is available via the ‘Save PDF’ action button.
Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Symposium on ‘New perspectives in the anorexia-cachexia syndrome’
Information
Proceedings of the Nutrition Society , Volume 56 , Issue 2 , July 1997 , pp. 793 - 799
Copyright
Copyright © The Nutrition Society 1997

References

REFERENCES

Cohn, S. H., Dombrowski, C. S., Pate, H. R. & Robertson, J. S. (1969). A whole-body counter with an invariant response to radionuclide distribution and body size. Physics in Medicine and Biology 14, 645–658.CrossRefGoogle ScholarPubMed
Cohn, S. H., Vartsky, D. & Yasumura, S. (1980). Compartmental body composition based on total-body nitrogen, potassium and calcium. American Journal of Physiology 239, 524–530.Google ScholarPubMed
Forbes, G. B. & Reina, J. C. (1970). Adult lean body mass declines with age: some longitudinal observations. Metabolism 19, 653–663.CrossRefGoogle ScholarPubMed
Garlick, P. J., Wernerman, J., McNurlan, M. A., Essen, P., Lobley, G. E., Milne, E., Calder, G. A. & Vinnars, E. (1989). Measurement of the rate of protein synthesis in muscle of postabsorptive young men by injection of 'flooding dose( of [l-13C]leucine. Clinical Science 77, 329–336.CrossRefGoogle Scholar
Harris, C. I. & Milne, G. (1980). The urinary excretion of Nt-methyl histidine in sheep: an invalid index of muscle protein breakdown. British Journal of Nutrition 44, 129–140.CrossRefGoogle Scholar
Harris, C. I. & Milne, G. (1981 a). The urinary excretion of N-tau-methyl histidine by cattle: validation as an index of muscle protein breakdown. British Journal of Nutrition 45, 411–422.CrossRefGoogle ScholarPubMed
Harris, C. I. & Milne, C. (1981 b). The inadequacy of urinary (N-tau)-methyl histidine excretion in the pig as a measure of muscle protein breakdown. British Journal of Nutrition 45, 423–429.CrossRefGoogle ScholarPubMed
Harris, C. I., Milne, G., Lobley, G. E. & Nicholas, G. A. (1977). 3-Methylhistidine as a measure of skeletal-muscle protein catabolism in the adult New Zealand white rabbit. Biochemical Society Transactions 5, 706–708.CrossRefGoogle ScholarPubMed
Heymsfield, S. B., Arteaga, C., McManus, C., Smith, J. & Moffitt, S. (1983). Measurement of muscle mass in humans: validity of the 24-hour urinary creatinine method. American Journal of Clinical Nutrition 37, 478–494.CrossRefGoogle ScholarPubMed
Hill, G. L. (1992). Metabolic Management of Patients Undergoing Major Surgery, pp. 19–32. London: Churchill Livingstone.Google Scholar
Johnson, P., Harris, C. I. & Perry, S. V. (1967). 3-Methylhistidine in actin and other muscle proteins. Biochemical Journal 105, 361–370.CrossRefGoogle ScholarPubMed
Long, C. L., Birkhahn, R. H., Geiger, J. W., Betts, J. E., Schiller, W. R. & Blakemore, W. S. (1981). Urinary excretion of 3-methylhistidine: An assessment of muscle protein catabolism in adult normal subjects and during malnutrition, sepsis and skeletal trauma. Metabolism 30, 765–776.CrossRefGoogle ScholarPubMed
Long, C. L., Dillard, D. R., Bodzin, J. H., Geiger, J. W. & Blakemore, W. S. (1988). Validity of 3- methylhistidine excretion as an indicator of skeletal muscle protein breakdown in humans. Metabolism 37, 844–849.CrossRefGoogle ScholarPubMed
Lukaski, H. C., Mendez, J., Buskirk, E. R. & Cohn, S. H. (1981). Relationship between endogenous 3- methylhistidine excretion and body composition. American Journal of Physiology 240, E302–E307.Google ScholarPubMed
Mussini, E., Colombo, L., De Ponte, G. & Marcucci, F. (1984). Low 3-methylhistidine levels in skeletal muscles of genetically dystrophic mice. Research Communications in Chemical Pathology and Pharmacology 43, 477–486.Google ScholarPubMed
Nissen, S., Sharp, R., Rathmacher, J. A., Rice, J., Fuller, J. C. Jr, Connelly, A. S. & Abumrad, N. N. (1996). The effect of the leucine metabolite β-hydroxy β-methylbutyrate on muscle metabolism during resistance-exercise training. Journal of Applied Physiology 81, 2095–2104.CrossRefGoogle ScholarPubMed
Rathmacher, J. A., Flakoll, P. J. & Nissen, S. L. (1995). A compartmental model of 3-methylhistidine metabolism in humans. American Journal of Physiology 296, E193–E198.Google Scholar
Rathmacher, J. A., Link, G. A., Flakoll, P. J. & Nissen, S. L. (1992). Gas chromatographic/mass spectrometric analysis of stable isotopes of 3-methylhistidine in biological fluids: application to plasma kinetics in vivo. Biological Mass Spectrometry 21, 560–566.CrossRefGoogle ScholarPubMed
Rathmacher, J. A., Link, G. & Nissen, S. (1993). Measurement of 3-methylhistidine production in lambs by using compartmental-kinetic analysis. British Journal of Nutrition 69, 743–755.CrossRefGoogle ScholarPubMed
Rennie, M. J. & Millward, D. J. (1983). 3-Methylhistidine excretion and the urinary 3-methylhistidinekreatinine ratio are poor indicators of skeletal muscle protein breakdown. Clinical Science 65, 217–225.CrossRefGoogle ScholarPubMed
Rennie, M. J., Smith, K. & Watt, P. W. (1994). Measurement of human tissue protein synthesis: an optimal approach. American Journal of Physiology 266, 298–307.Google ScholarPubMed
Sjolin, J., Stjernstrom, H., Arturson, G., Andersson, E., Friman, G. & arsson, J. (1989 a). Exchange of 3-methyl- histidine in the splanchnic region in human infection. American Journal of Clinical Nutrition 50, 1407–1414.CrossRefGoogle Scholar
Sjolin, J., Stjernstrom, H., Henneberg, S., Andersson, E., Martensson, J., Friman, G. & Larsson, J. (1989 b). Splanchnic and peripheral release of 3-methylhistidine in relation to its urinary excretion in human infection. Metabolism 38, 23–29.CrossRefGoogle ScholarPubMed
Smith, K., Barua, J. M., Watt, P. W., Scrimgeour, C. M. & ennie, M. J. (1992). Flooding with L-[l-13C]leucine stimulates human muscle protein incorporation of continuously infused L-[ l-13C]valine. American Journal of Physiology 262, E372–E376.Google Scholar
Wassner, S. J. & Li, J. B. (1982). Nt-methylhistidine release: contributions of rat skeletal muscle, GI tract, and skin. American Journal of Physiology 243, E293–E297.Google Scholar
Windsor, J. A. & Hill, G. L. (1988). Risk factors for postoperative pneumonia: the importance of protein depletion. Annals of Surgery 208, 29–296.CrossRefGoogle ScholarPubMed