Hostname: page-component-78c5997874-8bhkd Total loading time: 0 Render date: 2024-11-20T03:22:55.484Z Has data issue: false hasContentIssue false

Tissue localization of threonine oxidation in pigs

Published online by Cambridge University Press:  24 July 2007

Nathalie Le Floc’h
Affiliation:
Station de Recherches Porcines, INRA 35590 Saint Gilles, France
Jean-noёl Thibault
Affiliation:
Station de Recherches Porcines, INRA 35590 Saint Gilles, France
Bernard Sève
Affiliation:
Station de Recherches Porcines, INRA 35590 Saint Gilles, France
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Two experiments were designed to determine the tissue distribution of threonine oxidation through the threonine dehydrogenase (EC 1.1.1.103) pathway in pigs. The first experiment was conducted on eleven Piétrain x Large White piglets. The piglets were slaughtered at 5, 12 or 20 kg after 1 h of infusion with L-[U-14C]threonine (55 kBq/kg) mixed with unlabelled threonine (100 mg/kg). In the second experiment, four Piétrain x Large White and four Large White piglets (10 kg body weight) were infused with L-[1-13C]threonine (50 mg'kg) mixed with 50 mg'kg unlabelled threonine for 1 h, then killed for tissue sampling. In the two experiments, threonine dehydrogenase specific activity and threonine and glycine specific radioactivities and enrichments were measured in several tissues and in plasma. The higher level of labelling of threonine in the pancreas than in the liver suggested either a lower protein degradation rate or a faster rate of threonine transport in the liver than in the pancreas. Threonine dehydrogenase activity was found only in the liver and the pancreas. Whereas liver and pancreas threonine dehydrogenase specific activities were similar, glycine specific radioactivity and enrichment were 12- to 14-fold higher in the pancreas than in the liver. This is probably the consequence of a higher production rate of glycine from sources other than threonine (protein degradation, de novo synthesis from serine) in the liver than in the pancreas. Our results showed that Large White pigs could oxidize more threonine than Piétrain x Large White pigs. This could be related to the difference in growth performance and dietary N efficiency for protein deposition between these two genotypes.

Type
Animal Nutrition
Copyright
Copyright © The Nutrition Society 1997

References

REFERENCES

Ballèvre, O., Buchan, V., Rees, W. D., Fuller, M. F. & Garlick, P. J. (1991). Sarcosine kinetics in pigs by infusion of [l-14C]sarcosine: use for refining estimates of glycine and threonine kinetics. American Journal of Physiology 260, E662–E668.Google ScholarPubMed
Ballèvre, O., Cadenhead, A., Calder, A. G., Rees, W. D., Lobley, G. E., Fuller, M. F. & Garlick, P. J. (1990). Quantitative partition of threonine oxidation in pigs: effect of dietary threonine. American Journal of Physiology 259, E483–E491.Google Scholar
Bird, M. I., Nunn, P. B. & Lord, L. A. J. (1984). Formation of glycine and aminoacetone from L-threonine by rat liver mitochondria. Biochimica et Biophysica Acta 802, 229236.Google Scholar
Corring, T. (1975). Endogenous proteins excreted in the pancreatic juice of swine. Annales de Biologie Animale Biochimie Biophysique 15, 115118.Google Scholar
Cortamira, N. O., Sève, B., Lebreton, Y. & Ganier, P. (1991). Effect of dietary tryptophan on muscle, liver and whole-body protein synthesis in weaned pigs: relationship to plasma insulin. British Journal of Nutrition 66, 423435.Google Scholar
Davis, A. T. & Austic, R. E. (1982). Threonine degrading enzymes in chicken. Poultry Science 61, 21072111.CrossRefGoogle ScholarPubMed
Davis, A. T. & Austic, R. E. (1994). Dietary threonine imbalance alters threonine dehydrogenase activity in isolated hepatic mitochondria of chicks and rats. Journal of Nutrition 124, 16671677.Google Scholar
Garlick, P. J., Millward, D. J. & James, W. P. T. (1973). The diurnal response of muscle and liver protein synthesis in vivo in meal-fed rats. Biochemical Journal 136, 935945.Google Scholar
Girard-Globa, A., Bourdel, G. & Lardeux, B. (1980). Regulation of protein synthesis and enzyme accumulation in the rat pancreas by amount and timing of dietary protein. Journal Of Nutrition 110, 13801390.Google Scholar
Green, M. L. & Elliott, W. H. (1964). The enzymic formation of aminoacetone from threonine and its further metabolism. Biochemical Journal 92, 537549.CrossRefGoogle ScholarPubMed
Hartshorne, D. & Greenberg, D. M. (1964). Studies on liver threonine dehydrogenase. Archives of Biochemistry and Biophysics 105, 173178.CrossRefGoogle ScholarPubMed
Husek, P. (1991). Rapid derivatization and gas chromatographic determination of amino acids. Journal of Chromatography 552, 289299.CrossRefGoogle Scholar
Kang-Lee, Y. A. E. & Harper, A. E. (1978). Threonine metabolism in vivo: effect of threonine intake and prior induction of threonine dehydratase in rats. Journal of Nutrition 108, 163175.CrossRefGoogle ScholarPubMed
Le Floc'h, N., Obled, C. & Sève, B. (1995). In vivo threonine oxidation rate is dependent on threonine dietary supply in growing pigs fed low to adequate levels. Journal of Nutrition 125, 25502562.Google ScholarPubMed
Le Floc'h, N., Obled, C. & Sève, B. (1996). In vivo threonine oxidation in growing pigs fed on diets with graded levels of threonine. British Journal of Nutrition 75, 825837.Google Scholar
Le Floc'h, N., Sève, B. & Henry, Y. (1994). The addition of glutamic acid or protein to a threonine-deficient diet differentially affects growth performance and threonine dehydrogenase activity in fattening pigs. Journal of Nutrition 124, 19871995.Google Scholar
Leterme, P., Théwis, A., Genot, L., François, E. & Wathelet, B. (1993). Determination of the true ileal digestibility of amino acids in pigs by means of 15N-labelled diets. Preliminary results. In Nitrogen Flow in Pig Production and Environmental Consequences. EAAP Publication no. 69, pp. 4954 [Verstegen, M. W. A., den Hartog, L. A., van Kempen, G. J. M. and Metz, J. H. M., editors]. Wageningen: Pudoc Scientific Publishers.Google Scholar
Peng, Y., Gubin, J., Harper, A. E., Vavich, M. G. & Kemmerer, A. R. (1973). Food intake regulation: amino acid toxicity and changes in rat brain and plasma amino acids. Journal of Nutrition 103, 608617.Google Scholar
Ponter, A. A., Cortamira, N. O., Sève, B., Salter, D. N. & Morgan, L. M. (1994). The effects of energy source and tryptophan on the rate of protein synthesis and on hormones of the entero-insular axis in the piglet. British Journal of Nutrition 71, 661674.Google Scholar
Quiniou, N. (1995). Effect of growth potential on energy utilisation in pigs: contribution to modelling nutritional requirements and body composition. PhD thesis. Ecole Nationale Supérieure Agronomique de Rennes.Google Scholar
Simon, O., Bergner, H., Münchmeyer, R. & Zebrowska, T. (1982). Studies on the range of tissue protein synthesis in pigs: the effect of thyroid hormones. British Journal of Nutrition 48, 571582.Google Scholar
Simon, O., Münchmeyer, R., Bergner, H., Zebrowska, T. & Buraczewska, L. (1978). Estimation of rate of protein synthesis by constant infusion of labelled amino acids in pigs. British Journal of Nutrition 40, 243252.Google Scholar
Simon, O., Zebrowska, T., Bergner, H. & Münchmeyer, R. (1983). Investigations on the pancreatic and stomach secretion in pigs by means of continuous infusion of 14C-amino acids. Archiv für Tierernährung 33, 922.CrossRefGoogle ScholarPubMed
Statistical Analysis Systems (1989). SAS User's Guide: Statistics. Cary, NC: SAS Institute Inc.Google Scholar
Tressel, T., Thompson, R., Zieske, L. R., Menendez, M. I. T. S. & Davis, L. (1986). Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production. Journal of Biological Chemistry 261, 1642816437.CrossRefGoogle ScholarPubMed