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Effects of meal consumption on whole body leucine and alanine kinetics in young adult men

Published online by Cambridge University Press:  07 March 2008

Leonard J. Hoffer
Affiliation:
Laboratory of Human Nutrition and Clinical Research Center, Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Russell D. Yang
Affiliation:
Laboratory of Human Nutrition and Clinical Research Center, Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Dwight E. Matthews
Affiliation:
Departments of Medicine and Pediatrics, Washington University School of Medicine, St Louis, Missouri 63110, USA
Bruce R. Bistrian
Affiliation:
The Cancer Research InstituteNew England Deaconess Hospital, Boston, Massachusetts 02215, USA
Dennis M. Bier
Affiliation:
Departments of Medicine and Pediatrics, Washington University School of Medicine, St Louis, Missouri 63110, USA
Vernon R. Young
Affiliation:
Laboratory of Human Nutrition and Clinical Research Center, Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
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Abstract

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1. The effects of meal consumption on plasma leucine and alanine kinetics were studied using a simultaneous, primed, continuous infusion of L-[I-13C]leucine and L-[3,3,3-2H3]alanine in four healthy, young, adult male subjects. The study included an evaluation of the effect of sampling site on plasma amino acid kinetics, with blood being drawn simultaneously from an antecubital and dorsal heated hand vein.

2. In comparison with the postabsorptive state, the ingestion of small hourly meals resulted in a 35% increase in plasma leucine flux and a 77% increase in leucine oxidation. Calculated entry of leucine into the plasma compartment from endogenous sources decreased by 65%. Plasma alanine flux more than doubled, indicating a significant enhancement in de now alanine synthesis. 13C enrichment of leucine in venous and arterialized plasma did not differ significantly, but alanine flux calculated from isotopic measurement in venous plasma was substantially greater than that based on analysis of arterialized blood plasma.

Type
Papers of direct relevance to Clinical and Human Nutrition
Copyright
Copyright © The Nutrition Society 1985

References

REFERENCES

Abumrad, N. N., Rabin, D., Diamond, M. P. & Lacy, W. W. (1981). Metabolism 30, 936940.CrossRefGoogle Scholar
Clugston, G. A. & Garlick, P. J. (1982). Human Nutrition: Clinical Nutrition 36 C, 5770.Google Scholar
Cooper, A. J. L. (1976). Journal of Biological Chemistry 251, 10881096.CrossRefGoogle Scholar
FAO (1970). FAO Nutritional Studies, no. 24. Rome: Food and Agriculture Organization.Google Scholar
Garlick, P. J., Clugston, G. A., Swick, R. W. & Waterlow, J. C. (1980). American Journal of Clinical Nutrition 33, 19831986.CrossRefGoogle Scholar
Krebs, H. A. (1972). Advances in Enzyme Regulation 10, 397420.CrossRefGoogle Scholar
McGuire, E. A. H., Helderman, J. H., Tobin, H. D., Andres, R. & Berman, M. (1976). Journal of Applied Physiology 41, 565573.CrossRefGoogle Scholar
Matthews, D. E., Ben-Galim, E. & Bier, D. M. (1979). Analytical Chemistry 51, 8084.CrossRefGoogle Scholar
Matthews, D. E., Motil, K. J., Rohrbaugh, D. K., Burke, J. F., Young, V. R. & Bier, D. M. (1980). American Journal of Physiology 238, E473E479.Google Scholar
Motil, K. J., Bier, D. M., Matthews, D. E., Burke, J. F. & Young, V. R. (1981 a). Metabolism 30, 783791.CrossRefGoogle ScholarPubMed
Motil, K. J., Matthews, D. E., Bier, D. M., Burǵe, J. F., Munro, H. N. & Young, V. R. (1981 b). American Journal of Physiology 240, E712E721.Google Scholar
Munro, H. N. (1964). In Mammalian Protein Metabolism, vol. 1, pp. 381481 [Munro, H. N.and Allison, J. B., editors]. New York: Academic Press.CrossRefGoogle Scholar
Munro, H. N. (editor) (1970). In Mammalian Protein Metabolism, vol.4, pp. 299386. New York: Academic Press.CrossRefGoogle Scholar
Pell, J. M., Caldarone, E. M. & Bergman, E. N. (1983). Biochemical Journal 214, 10151018.CrossRefGoogle Scholar
Rennie, M. J., Edwards, R. H. T., Halliday, D., Matthews, D. E., Wolman, S. L. & Millward, D. J. (1982). Clinical Science 63, 519523.CrossRefGoogle Scholar
Robert, J. J., Bier, D. M., Zhao, X. H., Matthews, D. E. & Young, V. R. (1982). Metabolism 31, 12121218.CrossRefGoogle ScholarPubMed
Wahren, J., Felig, P. & Hagenfeldt, L. (1976). Journal of Clinical Investigation 57, 987999.CrossRefGoogle Scholar
Waterlow, J. C., Garlick, P. J. & Millward, J. C. (1978). Protein Turnover in Mammalian Tissues and in the Whole Body. New York:North-Holland.Google Scholar
Young, V. R. & Bier, D. M. (1981). Proceedings of the Nutrition Society 40, 343359.CrossRefGoogle Scholar
Young, V. R., Munro, H. N.,Matthews, D. E. & Bier, D. M. (1983). In New Aspects of Clinical Nutrition, pp. 4373 [Kleinberger, Gand Deutsch, E, editors]. Basel: Karger.Google Scholar