Abstract
The protective effect of ADP on unspecific Ca2+ release and collapse of the transmembrane potential was analyzed in mitochondria from kidneys of rats. The presence of ADP in the incubation mixture prevents Ca2+ leakage and collapse of δω in sucrose-containing medium, but fails to do so in KCl medium. The effect of the adenine nucleotide in sucrose media correlates with an increase in the level of reduced pyridine nucleotides; the increase was due to a stimulatory effect on the activity of glutamic dehydrogenase. It also was observed that in KCl media, in the presence and in the absence of ADP the rate of NADH oxidation through the respiratory chain was higher than in sucrose; in this latter medium a high level of reduced pyridine nucleotides was found, in comparison to KCl media. It is proposed that the role of ADP is to increase glutamic dehydrogenase activity and in consequence to provoke a higher rate of formation of NADH which in turn controls Ca2+ release.
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References
Akerman, K. E. O., and Wikström, M. K. F. (1976).FEBS Lett. 68, 191–197.
Beatrice, M. C., Palmer, J. W., and Pfeiffer, D. R. (1980).J. Biol. Chem. 255, 8663–8671.
Beatrice, M. C., Stiers, D. L., and Pfeiffer, D. R. (1984).J. Biol. Chem. 259, 1279–1287.
Bellomo, G., Jewell, S. A., Thor, H., and Orrenius, S. (1982).Proc. Natl. Acad. Sci. USA 79, 6842–6846.
Bryla, J., and Jolanta, M. D. (1977).Biochim. Biophys. Acta 462, 273–282.
Chávez, E., Briones, R., Michel, B., Bravo, C., and Jay, D. (1985).Arch. Biochem. Biophys. 242, 493–497.
Crompton, M., Capano, M., and Carafoli, E., (1976).Eur. J. Biochem. 69, 453–462.
Denton, R. M., and McCormack, J. G. (1980).FEBS Lett. 119, 1–8.
Fiscum, G., and Cockrell, R. S. (1978).FEBS Lett. 92, 125–128.
Godinot, C., and Gautheron, D. (1972).Biochimie 54, 245–256.
Gómez-Puyou, A., Tuena, M., Sandoval, F., Chávez, E., and Peña, A. (1972).Biochemistry 11, 97–102.
Harris, E. J. (1979).Biochem. J. 178, 673–680.
Haworth, R. A., and Hunter, D. F. (1980)J. Membr. Biol. 54, 231–236.
Hunter, D. F., and Haworth, R. A. (1974).Arch. Biochem. Biophys. 195, 453–459.
Jarvisalo, J. O., Kilpio, J., and Saris, N. E. L. (1980).Environ. Res. 22, 217–223.
Jurkowitz, M. S., and Brierley, G. P. (1984).J. Bioenerg. Biomembr. 14, 435–449.
Jurkowitz, M. S., Geisbuhler, T., Jung, D. W., and Brierley, G. P. (1983).Arch. Biochem. Biophys. 223, 120–128.
Kendrick, N. C. (1976).Anal. Biochem. 76, 487–501.
Krebs, E. G., and Bravo, J. A. (1979).Annu. Rev. Biochem. 48, 923–959.
Lehninger, A. L., Carafoli, E., and Rossi, C. S. (1967). InAdvances in Enzymology (Nord, F. F., ed.), Interscience, New York, Vol. 29, pp. 259–320.
Lehninger, A. L., Vercesi, A., and Babanunmi, E. (1978).Proc. Natl. Acad. Sci. USA 75, 1690–1694.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randal, R. J. (1951).J. Biol. Chem. 193, 265–275.
Moore, C. L. (1971).Biochem. Biophys. Res. Commun. 42, 298–304.
Nicholls, D. G., and Crompton, M. (1980).FEBS Lett. 111, 261–268.
Nicholls, D. G. and Akerman, K. (1982).Biochim. Biophys. Acta 683, 57–88.
Palmer, J. W., and Pfeiffer, D. R. (1981).J. Biol. Chem. 256, 6742–6750.
Panov, A., Filippova, J., and Lyakhovich, V. (1980).Arch. Biochem. Biophys. 189, 107–122.
Peng, C. F., Straub, K. D., Kam, J. J., Murphy, M. L., and Wadkins, C. L. (1977).Biochim. Biophys. Acta 462, 403–413.
Reed, K. C., and Bygrave, F. L. (1974).Biochem. J. 140, 143–155.
Rossi, C. S., and Lehninger, A. L. (1964).J. Biol. Chem. 239, 3971–3980.
Siliprandi, D., Siliprandi, N., and Toninello, A. (1983).Eur. J. Biochem. 130, 173–175.
Toninello, A., Siliprandi, D., and Siliprandi, N. (1983).Biochem. Biophys. Res. Commun. 111, 792–797.
Vasington, F. D., and Murphy, J. V. (1962).J. Biol. Chem. 237, 2670–2677.
Weiner, M. W., and Lardy, H. (1973).J. Biol. Chem. 248, 7682–7687.
Wolkowitz, P. E., and McMillin-Wood, J. (1981).Arch. Biochem. Biophys. 209, 408–422.
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Chávez, E., Jay, D. Control of mitochondrial Ca2+ retention by ADP-stimulated glutamic dehydrogenase. J Bioenerg Biomembr 19, 571–580 (1987). https://doi.org/10.1007/BF00770038
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DOI: https://doi.org/10.1007/BF00770038