Abstract
Essentiality of selenium (Se) for Japanese quail,Coturnix coturnix japonica, was confirmed using a formulated semipurified low-Se diet (basal) (0.05 ppm). Selenium-deficiency symptoms appeared in quails on this diet within 15 d, which corresponded to low levels of hemolysate glutathione peroxidase (GSH-Px) activity. Selenium administration at 0.05 and 2.0 ppm levels resulted in an increase of hemolysate GSH-Px activity by 64 and 116%, respectively, in both short- and long-term experiments. Growth over a 2-mo period increased the hemolysate GSH-Px activity by 120% at each level of dietary Se. A differential response was exhibited by hepatic mitochondrial and soluble GSH-Px activity to Se supplementation, the former increasing progressively with increments of Se at 0.05, 2.0, and 4.0 ppm by 45, 70 and 150%, respectively. The soluble GSH-Px activities of tissues, such as liver, kidney, and testis, and RBC membrane-bound activity remained unchanged in long-term studies at different levels of Se. Replenishment of Se to quails maintained on low-Se diets reflected no change in RBC membrane-bound and liver-soluble GSH-Px activities, although the activity in hemolysate increased consistently with Se. The GSH-Px activity in hemolysate was restored to the levels comparable to those of long-term studies only at Se administration at the 2.0-ppm level. The differential response of mitochondrial and soluble GSH-Px activities to Se and other related observations on mitochondrial functions suggest an additional role for Se in mitochondrial membrane processes and glutathione-related metabolic regulations.
Similar content being viewed by others
References
K. Schwarz,Fed. Proc. 20, 666 (1961).
J. N. Thompson and M. L. Scott,J. Nutr. 97, 335 (1969).
E. D. Walter and L. S. Jensen,J. Nutr. 80, 327 (1963).
Y. Niyo, R. D. Glock, F. K. Ramsey, and R. C. Ewan,Am. J. Vet. Res. 38, 1479 (1977).
R. J. Shamberger,Biochemistry of the elements (Biochemistry of Selenium) E. Frieden, ed., Plenum, NY, NY, 1983, pp. 31–54.
T. C. Stadtman, inAdvances in Enzymology, vol. 48, A. Meister, ed., 1979, pp. 1–28.
J. T. Rotruck, A. L. Pope, H. E. Ganther, D. G. Hafeman, and W. G. Hoekstra,Science 179, 588 (1973).
R. F. Burk, A. M. Mackinnon, and F. R. Simon,Biochem. Biophys. Res. Commun. 56, 431 (1974).
D. C. Turner and T. C. Stadtman,Arch. Biochem. Biophys. 154, 366 (1973).
K. P. Mc Connell, R. M. Burton, T. Kute, and P. J. Higgins,Biochem. Biophys. Acta. 588, 113 (1979).
G. N. Schrauzer, D. A. White, and C. J. Schneider,Bioinorg. Chem. 8, 387 (1978).
D. Medina and C. J. Oborn,Cancer Res. 44, 4361 (1984).
L. Flohé, inFree Radicals in Biology, vol 5, AP, New York, NY, 1982, pp. 223–249.
F. Schneider and L. Flohé,Hoppe Seylers Z. Physiol. Chem. 348, 540 (1967).
S. Oh, H. E. Ganther, and W. G. Hoekstra,Biochemistry 13, 1825 (1974).
Y. Awasthi, E. Bentler, and S. Srivastava,J. Biol. Chem. 250, 5144 (1975).
J. J. Zakowski and A. L. Tappel,Biochem. Biophys. Acta 445, 558 (1976).
L. Flohé, W. A. Gunzler, and R. Ladenstein, inGlutathione—Metabolism and Function, I. M. Arias and W. B. Jakoby, eds., Rave, NY, NY, 1976.
A. Wendel, inEnzymatic Basis of Detoxification, vol 1, AP, ed., New York, NY, 1980, pp. 333–353.
O. Epp, R. Ladenstein, and A. Wendel,Eur. J. Biochem. 133, 51 (1983).
S. T. Omaye and A. L. Tappel,J. Nutr. 104, 747 (1974).
P. J. Smith and A. L. Tappel,Nature 247, 392 (1974).
G. F. Combs, Jr., C. H. Liu, Z. H. Lu, and Q. Su,J. Nutr. 144, 964 (1984).
D. E. Paglia and W. N. Valentine,J. Lab. Clin. Med. 70, 158 (1967).
R. A. Lawrence and R. F. Burk,Biochem. Biophys. Res. Commun. 71, 952, (1976).
O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall,J. Biol. Chem. 193, 265 (1951).
M. J. Ihnet,J. Assoc. Off. Anal. Chem. 57, 368, (1974).
N. Vasanihy and K. Laliha, manuscript under preparation
D. G. Hafeman, R. A. Sunde, and W. G. Hoekstra,J. Nutr. 104, 580 (1974).
H. Sies and K. Moss,Eur. J. Biochem. 84, 377 (1978).
L. Flohé and W. Schlegal,Hoppe Seylers Z. Physiol Chem. 352, 1401 (1971).
M. E. Tappel, J. Chaudière, and A. L. Tappel,Comp. Biochem. Physiol. 73B (4), 945 (1982).
J. R. Prohaska,Biochem. Biophys. Res. Commun. 76, 437 (1980).
R. E. Pinto and W. Bartley,Biochem. J. 112, 109 (1969).
L. Flohé and R. Zimmermann,Biochem. Biophys. Acta 223, 210 (1970).
W. H. Habig, M. J. Pabst, G. Fleishner, Z. Gatmaitan, I. M. Arias, and W. B. Jakoby,Proc. Natl. Acad. Sci. USA 71, 3879 (1974).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Narayanaswami, V., Padma Bai, R., Babu, M. et al. Selenium-mediated biochemical changes in Japanese quail. Biol Trace Elem Res 10, 79–89 (1986). https://doi.org/10.1007/BF02795560
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF02795560
Index Entries
- Selenium, and related biochemical changes
- selenium deficiency in the Japanese quail,Coturnix coturnix japonica
- selenium and experimental deficiency and repletion-biochemical studies
- selenium and metabolic regulation
- glutathione peroxidase in selenium deficiency in quails, uncomplicated
- glutathione peroxidase activities in tissues of Japanese quail
- glutathione peroxidase and growth-related changes
- glutathione peroxidase, differential responses to selenium at subcellular level