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Tissue- and substrate-dependent responses of oxidative phosphorylation to dietary protein level in chicks

Published online by Cambridge University Press:  09 March 2007

Masahiro Tanaka ,
Teru Ishibashi ,
Katsuyuki Okamoto  and
Masaaki Toyomizu
Masahiro Tanaka
Affiliation:
Animal Nutrition, Department of Agriculture and Graduate School of Science and Technology, Niigata University, 2-8050 Ikarashi, Niigata, 950-21, Japan
Teru Ishibashi
Affiliation:
Animal Nutrition, Department of Agriculture and Graduate School of Science and Technology, Niigata University, 2-8050 Ikarashi, Niigata, 950-21, Japan
Katsuyuki Okamoto
Affiliation:
Animal Nutrition, Department of Agriculture and Graduate School of Science and Technology, Niigata University, 2-8050 Ikarashi, Niigata, 950-21, Japan
Masaaki Toyomizu
Affiliation:
Animal Nutrition, Department of Agriculture and Graduate School of Science and Technology, Niigata University, 2-8050 Ikarashi, Niigata, 950-21, Japan
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Abstract

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The ADP:O values in both cardiac and hepatic mitochondria have significantly decreased with an increase in protein level after 7, 14 and 21 d of feeding (Toyomizu et al. 1992). The present studies were undertaken to clarify tissue-specific effects of dietary protein levels on oxidative phosphorylation in the liver, kidney, skeletal muscles and small intestine and to characterize oxidative metabolism with diverse substrates in the liver. Chicks were fed on semi-purified diets of different protein levels (7, 25, 43 and 61% of metabolizable energy content) for 21 d. The responses of protein levels to oxidative phosphorylation showed tissue-dependency; although liver mitochondria of chickens fed on higher- protein diets exhibited reduced ADP:O values and state 3, neither changes in ADP:O value nor state 3 and state 4 rates were observed in the isolated mitochondria from kidney and skeletal muscles. Small intestinal mucosal mitochondria from chickens fed on a high (61%)-protein-energy diet showed significantly reduced ADP:O value and respiratory control ratio when compared with medium-protein- energy diets (25 and 43%). In liver mitochondria showing the most sensitive dependency to the levels of dietary protein, the ADP:O value decreased with increasing protein levels when pyruvate + malate- or glutamate-requiring complexes I, III and IV of the electron transport chain were used as substrates, but it did not change when succinate-requiring complexes II, III and IV or ascorbate + tetramethyl-p- phenylenediamine requiring complex IV was used. These results imply that impaired oxidative phosphorylation capacities with increasing dietary protein levels may be associated with functional damage to the respiratory chain for electron flow from NAD-linked substrates to the ubiquinone pool.

Keywords

Dietary proteinOxidative phosphorylationTissue specificityChicken
Type
Metabolic Responses to Dietary Protein
Information
British Journal of Nutrition , Volume 70 , Issue 2 , September 1993 , pp. 459 - 469
Copyright
Copyright © The Nutrition Society 1993

References

REFERENCES

Akiba, Y. & Matsumoto, T. (1978). Effects of force-feeding and dietary cellulose on liver lipid accumulation and lipid composition of liver and plasma in growing chicks. Journal qf Nutrition 108, 739–748.CrossRefGoogle ScholarPubMed
Chance, B. & Williams, G. R. (1956). The respiratory chain and oxidative phosphorylation. Advances in Enzymology 17, 65–134.Google ScholarPubMed
Chappell, J. B. (1964). The oxidation of citrate, isocitrate and cis-aconitate by isolated mitochondria. Biochemical Journal 90, 225–237.CrossRefGoogle ScholarPubMed
Chappell, J. B. & Perry, S. V. (1954). Biochemical and osmotic properties of skeletal muscle mitochondria. Nature 173, 1094–1095.CrossRefGoogle ScholarPubMed
Christophersen, B. O. & Bremer, J. (1972). Erucic acid – an inhibitor of fatty acid oxidation in the heart. Biochimica et Biophysica Acta 280, 506–514.CrossRefGoogle ScholarPubMed
Clandinin, M. T. (1978). The role of dietary long chain fatty acids in mitochondrial structure and function. Effects on rat cardiac mitochondrial respiration. Journal of Nutrition 108, 273–281.CrossRefGoogle ScholarPubMed
Forbes, J. M. (1986). The Voluntary Food Intake ofFarm Animals, pp. 86–113. London: Butterworth & Co. Ltd.CrossRefGoogle Scholar
Goldspink, D. F. & Kelly, F. J. (1984). Protein turnover and growth in the whole body, liver and kidney of the rat from the foetus to senility. Biochemical Journal 217, 507–516.CrossRefGoogle ScholarPubMed
Goldspink, D. F., Lewis, S. E. M. & Kelly, F. J. (1984). Protein synthesis during the developmental growth of the small and large intestine of the rat. Biochemical Journal 217, 527–534.CrossRefGoogle ScholarPubMed
Gomez, F., Ramos-Galvan, R., Cravioto, J., Frenk, S., Vazquez Santaella, J. & de la Pena, C. (1956). Fat absorption in chronic severe malnutrition in children. Lancet ii, 121–122.CrossRefGoogle Scholar
Hatefi, Y. (1985). The mitochondrial electron transport and oxidative phosphorylation system. Annual Review of Biochemistry 54, 1015–1069.CrossRefGoogle ScholarPubMed
Holemans, K. & Lamhrechts, A. (1955). Nitrogen metabolism and fat absorption in malnutrition and in kwashiorkor. Journal of Nutrition 56, 477–494.CrossRefGoogle ScholarPubMed
Hill, F. W. & Dansky, L. M. (1954). Studies of the energy requirements of chickens. I. The effect of dietary energy level on growth and feed consumption. Poultry Science 33, 112–119.CrossRefGoogle Scholar
Hoppel, C., DiMarco, J. P. & Tandler, B. (1979). Riboflavin and rat hepatic cell structure and function: mitochondrial oxidative metabolism in deficiency states. Journal of Biological Chemistry 254, 4164–4170.CrossRefGoogle ScholarPubMed
Houtsmuller, U. M. T., Struijk, C. B. & Van der Beek, A. (1970). Decrease in rate of ATP synthesis of isolated rat heart mitochondria induced by dietary erucic acid. Biochimica et Biophysica Acta 218, 564–566.CrossRefGoogle ScholarPubMed
Jaworek, D., Gruber, W. & Bergmeyer, H. U. (1974). Adenosine-5-diphosphate and adenosine-5- monophosphate. In Methods qf Enzymatic Analysis, pp. 2127–2131. [Bergmeyer, H. U., editor]. New York: Academic Press.CrossRefGoogle Scholar
Johnston, D. W. (1971). The absence of brown adipose tissue in birds. Comparative Biochemistry and Physiology 40A, 1107–1108.CrossRefGoogle Scholar
Lawrence, C. B. & Davies, N. T. (1986). A novel, simple and rapid method for the isolation of mitochondria which exhibit respiratory control, from rat small intestinal mucosa. Biochiniica et Biophysica Acta 848, 35–40.CrossRefGoogle ScholarPubMed
Lee, C. P., Martens, M. E., Jankulovska, L. & Neymark, M. A. (1979). Defective oxidative metabolism of myodystrophic skeletal muscle mitochondria. Muscle and Nerve 2, 340–348.CrossRefGoogle ScholarPubMed
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the fohn phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle Scholar
Martens, M. E., Peterson, P. L. & Lee, C. P. (1991). In vitro effects of glucocorticoid on mitochondrial energy metabolism. Biochimica et Biophysiccr Acta 1058, 152–160.CrossRefGoogle ScholarPubMed
Nicholls, D. G. (1982). Bioenergetics, An Introduction to the Chemiosmotic Theory, pp. 99–132. London: Academic Press.Google Scholar
Powell, T. S., Douglas, C. R., Stonerock, R. H. & Harms, R. H. (1972). Feed intake of hens fed various levels of energy from feed and/or sucrose-water. Poultry Science 51, 1851.Google Scholar
Reeds, P. J. (1989). Regulation of protein turnover. In Animal Growth Regulation, pp. 183–189 [Campion, D. R., Hausman, G J. and Martin, R. J., editors]. New York and London: Plenum Press.CrossRefGoogle Scholar
Rothwell, N. J. & Stock, M. J. (1987). Effect of environmental temperature on energy balance and thermogenesis in rats fed normal or low protein diets. Journal of Nutrition 117, 833–837.CrossRefGoogle ScholarPubMed
Rothwell, N. J., Stock, M. J. & Tyzbir, R. S. (1983). Mechanisms of thermogenesis induced by low protein diets. Metabolism 32, 257–261.CrossRefGoogle ScholarPubMed
SAS Institute Inc. (1985). SAS User's Guide: Statistics, version 5, pp. 433–506. Cary, NC: SAS Institute Inc.Google Scholar
Takeuchi, Y., Morii, H., Tamura, M., Hayaishi, O. & Watanabe, Y. (1991). A possible mechanism of mitochondrial dysfunction during cerebral ischemia: inhibition of mitochondrial respiration activity by arachidonic acid. Archives of Biochemistry and Biophysics 289, 33–38.CrossRefGoogle ScholarPubMed
Tinker, D. A., Brosnan, J. T. & Herzberg, G. R. (1986). Interorgan metabolism of amino acids, glucose, lactate, glycerol and uric acid in the domestic fowl (Gallus domesticus). Biochemical Journal 240, 829–836.CrossRefGoogle ScholarPubMed
Toyomizu, M. & Clandinin, M. T. (1993). Effects of dietary protein and fat level on oxidative phosphorylation in rat heart mitochondria. British Journal of Nutrition 69, 97–102.CrossRefGoogle ScholarPubMed
Toyomizu, M., Kirihara, D., Tanaka, M., Hayashi, K. & Tomita, Y. (1992). Dietary protein level alters oxidative phosphorylation in heart and liver mitochondria of chicks. British Journal of Nutrition 68, 89–99.CrossRefGoogle ScholarPubMed
Trayhurn, P., Ashwell, M., Jennings, G., Richard, D. & Stirling, D. M. (1987). Effect of warm or cold exposure on GDP binding and uncoupling protein in rat brown fat. American Journal of Physiology 252, E237–E243.Google ScholarPubMed
Truswell, A. S. (1975). Carbohydrate and lipid metabolism in protein-calorie malnutrition. In Protein-Calorie Malnutrition, pp, 119–141 [Olson, R. E., editor]. New York: Academic Press.CrossRefGoogle Scholar
Webster, A. J. F. (1981). The energetic efficiency of metabolism. Proceedings qf Nutritional Society 40, 121–128.CrossRefGoogle ScholarPubMed