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The substrate-specific impairment of oxidative phosphorylation in liver mitochondria from high-protein-fed chickens

Published online by Cambridge University Press:  09 March 2007

Masaaki Toyomizu
Affiliation:
Departments of Animal Nutrition, Faculty of Agriculture and Graduate School of Science and Technology, Niigata University, 2–8050 Ikarashi, Niigata, 950–21, Japan
Masahiro Tanaka
Affiliation:
Departments of Animal Nutrition, Faculty of Agriculture and Graduate School of Science and Technology, Niigata University, 2–8050 Ikarashi, Niigata, 950–21, Japan
Makoto Kojima
Affiliation:
Plant Pathology, Faculty of Agriculture and Graduate School of Science and Technology, Niigata University, 2–8050 Ikarashi, Niigata, 950–21, Japan
Teru Ishibashi
Affiliation:
Departments of Animal Nutrition, Faculty 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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Chickens fed on semi-purified low (7%) or high (61%) protein-energy diets for 14 or 17 d were used for determinations of oxidative phosphorylation and specific amounts of mitochondrial protein in liver. The ADP: oxygen (ADP:O) values obtained when pyruvate + malate were used as substrates were significantly reduced in the high-protein-fed group after the 4th day compared with those for the group fed the low-protein diet, while the differences in ADP:O values between the two treatments when L-glutamate was used as substrate were found to be significant on the 14th day. At any feeding period no significant differences in ADP:O values were observed between the two groups when α-ketoglutarate, malate, or octanoate + malate were used as substrates, nor in specific amounts of mitochondrial protein in liver. The dependency of the pyruvate + malate-supported respiration rate on the temperature in the reaction medium was also determined. The results of an Arrhenius plot showed that transition temperatures, and the lower and upper energies of activation, were similar for the groups fed on low- and high-protein diets. Furthermore, no morphological changes in mitochondria were observed among chickens fed on diets with various protein levels for 14 d. From these results we concluded that the reduction of ADP: O value with pyruvate + malate or L-glutamate substrates in chickens fed on a high-protein diet was substrate-specific, and was not due to functional damage to the respiratory chain for electron flow from NAD-linked substrates to the ubiquinone pool, nor to modulation of properties of the inner mitochondrial membrane.

Type
Dietary protein and oxidative phosphorylation
Copyright
Copyright © The Nutrition Society 1995

References

Akaike, H. (1974). A new look at the statistical model identification. Institute of Electrical and Electronics Engineers Transactions on Automatic Control AC-19, 716723.Google Scholar
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 of Nutrition 108, 739748.Google Scholar
Chance, B. & Williams, G. R. (1956). The respiratory chain and oxidative phosphorylation. Advances in Enzymology 17, 65134.Google Scholar
Chappell, J. B. (1964). The oxidation of citrate, isocitrate and cis-aconitate by isolated mitochondria. Biochemical Journal 90, 225237.Google Scholar
Echegoyen, S., Oliva, E. B., Sepulveda, J., Diaz-Zagoya, J. C., Espinosa-Garcia, M. T., Pardo, J. P. & Martinez, F. (1993). Cholesterol increase in mitochondria: its effect on inner-membrane functions, submitochondrial localization and ultrastructural morphology. Biochemical Journal 289, 703708.CrossRefGoogle ScholarPubMed
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, 41644170.Google Scholar
Iwaya-Inoue, M., Sakaguchi, K. & Kaku, S. (1989). Statistical studies using AIC method to decide the question of “Break” or “Straight” in Arrhenius plots of water proton NMR relaxation times in chilling-sensitive Vigna and insensitive Pisum seedlings. Plant Cell Physiology 30, 309316.CrossRefGoogle Scholar
Jaworek, D., Gruber, W. & Bergmeyer, H. U. (1974). Adenosine-5′ -diphosphate and adenosine-5′- monophosphate. In Methods of Enzymatic Analysis, Vol. 4, pp. 21272131 [Bergmeyer, H. U., editor]. New York: Academic Press.Google Scholar
Krahenbuhl, S., Chang, M., Brass, E. P. & Hoppel, C. L. (1991). Decreased activities of ubiquinol: ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c: oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria. Journal of Biological Chemistry 266, 2099821003.CrossRefGoogle Scholar
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, 265275.CrossRefGoogle Scholar
Rafael, J., Patzelt, J., Schäfer, H. & Elmadfa, I. (1984). The effect of essential fatty acid deficiency on basal respiration and function of liver mitochondria in rats. Journal of Nutrition 114, 255262.Google Scholar
Sottocasa, G. L., Kuylenstierna, B., Ernster, L. & Bergstrand, A. (1967). An electron-transport system associated with the outer membrane of liver mitochondria: a biochemical and morphological study. Journal of Cell Biology 32, 415438.Google Scholar
Statistical Analysis Systems (1985). SAS User's Guide, Statistics, 5th edn. Cary, NC: SAS Institute Inc.Google Scholar
Spurr, A. R. (1969). A low-viscosity epoxy resin embedding medium for electron microscopy. Journal of Ultrastructure Research 26, 3143.CrossRefGoogle ScholarPubMed
Tanaka, M., Ishibashi, T., Okamoto, K. & Toyomizu, M. (1993). Tissue- and substrate-dependent responses of oxidative phosphorylation to dietary protein level in chicks. British Journal of Nutrition 70, 459469.Google Scholar
Tanaka, M., Ishibashi, T. & Toyomizu, M. (1995). Time course of oxidative phosphorylation in liver mitochondria of chickens fed on high-protein diet. British Poultry Science 36, 143154.Google Scholar
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, 97102.Google Scholar
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, 8999.Google Scholar
Wander, R. C. & Berdanier, C. D. (1985). Effects of dietary carbohydrate on mitochondrial composition and function in two strains of rats. Journal of Nutrition 115, 190199.Google Scholar
Wolfe, J. & Bagnall, C. (1979). Statistical tests to decide between straight line segments and curves as suitable fits to Arrhenius plots or other data. In Low Temperature Stress in Crop Plants, pp. 527533 [Lyons, J. M., Graham, D. and Raison, J. K., editors]. New York: Academic Press.Google Scholar
Yamauchi, K., Isshiki, Y., Zhou, Z.-X. & Nakahiro, Y. (1990). Scanning and transmission of microscopic observations of bacteria adhering to ileal epithelial cells in growing broiler and white leghorn chickens. British Poultry Science 31, 129137.Google Scholar
Zaragozá, R., Renau-Piqueras, J., Portolés, M., Hernández-Yago, J., Jordá, A. & Grisoía, S. (1987). Rats fed prolonged high protein diets show an increase in nitrogen metabolism and liver megamitochondria. Archives of Biochemistry and Biophysics 258, 426435.CrossRefGoogle ScholarPubMed
Zsigmond, E. & Clandinin, M. T. (1986). Modulation of mitochondrial ATPase sensitivity to inhibitors and stimulators by diet-induced changes in membrane lipid. International Journal of Biochemistry 18, 505511.Google Scholar