[en] In isolated Acanthamoeba castellanii mitochondria respiring in state 3 with external NADH or succinate, the linoleic acid-induced purine nucleotide-sensitive uncoupling protein activity is able to uncouple oxidative phosphorylation. The linoleic acid-induced uncoupling can be inhibited by a purine nucleotide (GTP) when quinone (Q) is sufficiently oxidized, indicating that in A. castellanii mitochondria respiring in state 3, the sensitivity of uncoupling protein activity to GTP depends on the redox state of the membranous Q. Namely, the inhibition of the linoleic acid-induced uncoupling by GTP is not observed in uninhibited state 3 respiration as well as in state 3 respiration progressively inhibited by complex III inhibitors, i.e., when the rate of quinol (QH(2))-oxidizing pathway is decreased. On the contrary, the progressive decrease of state 3 respiration by declining respiratory substrate availability (by succinate uptake limitation or by decreasing external NADH concentration), i.e., when the rate of Q-reducing pathways is decreased, progressively leads to a full inhibitory effect of GTP. Moreover, in A. castellanii mitochondria isolated from cold-treated cells, where a higher uncoupling protein activity is observed, the inhibition of the linoleic acid-induced proton leak by GTP is revealed for the same low values of the Q reduction level.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Jarmuszkiewicz, Wieslawa
Swida, A.
Czarna, M.
Antos, N.
Sluse-goffart, Claudine; Université de Liège - ULiège
Sluse, Francis ; Université de Liège - ULiège > Département des sciences de la vie > Bioénergétique et physiologie cellulaire
Language :
English
Title :
In phosphorylating Acanthamoeba castellanii mitochondria the sensitivity of uncoupling protein activity to GTP depends on the redox state of quinone.
Publication date :
2005
Journal title :
Journal of Bioenergetics and Biomembranes
ISSN :
0145-479X
eISSN :
1573-6881
Publisher :
Kluwer Academic/Plenum Publishers, New York, United States - New York
Andreyev, A. Y., Bondareva, T. O., Dedukhova, V. I., Mokhova, E. N., Skulachev, V. P., Tsofina, L. M., Volkov, N. L., and Vygodina, T. V. (1989). Eur. J. Biochem. 182, 585-592.
Considine, M. J., Goodman, M., Echtay, K. S., Laloi, M., Whelan, J., Brand, M. D., and Sweetlove, L. J. (2003). J. Biol. Chem. 278, 22298-22302.
Echtay, K. S., and Brand, M. D. (2001). Biochem. Soc. Trans. 29, 763-768.
Echtay, K. S., Roussel, D., St.-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roubuck, S. J., Morrison, A., Pickering, S., Clapham, J. C., and Brand, M. D. (2002). Nature 415, 96-99.
Echtay, K. S., Winkler, E., Frischmuth, K., and Klingenberg, M. (2001). Proc. Natl. Acad. Sci. 98, 1416-1421.
Echtay, K. S., Winkler, E., and Klingenberg, M. (2000). Nature 408, 609-613.
Goglia, F., and Skulachev, V. P. (2003). FASEB J. 17, 1585-1591.
Gray, M. W., Burger, G., and Lang, B. F. (1999). Science 283, 1476-1482.
Hoefnagel, M. H. N., and Wiskich, J. T. (1996). Plant Physiol. 110, 1329-1335.
Jaburek, M., and Garlid, K. D. (2003). J. Biol. Chem. 278, 25825-25831.
Jaburek, M., Varecha, M., Gimeno, R. E., Dembski, M., Ježek, P., Zhang, M., Burn, P., Tartaglia, L. A., and Garlid, K. D. (1999). J. Biol. Chem. 274, 26003-26007.
Jarmuszkiewicz, W., Almeida, A. M., Sluse-Goffart, C. M., Sluse, F. E., and Vercesi, A. E. (1998a). J. Biol. Chem. 273, 34882-34886.
Jarmuszkiewicz, W., Almeida, A. M., Vercesi, A. E., Sluse, F. E., and Sluse-Goffart, C. M. (2000b). J. Biol Chem. 275, 13315-13320.
Jarmuszkiewicz, W., Antos, N., Swida, A., Czarna, M., and Sluse, F. E. (2004a). FEBS Lett. 569, 178-184.
Jarmuszkiewicz, W., Behrendt, M., Navet, R., and Sluse, F. E. (2003). FEBS Lett. 532, 459-464.
Jarmuszkiewicz, W., Czarna, M., Sluse-Goffart, C. M., and Sluse, F. E. (2004c). Acta Biochem. Pol. 51, 533-538.
Jarmuszkiewicz, W., Fraczyk, O., and Hryniewiecka, L. (2001). Acta Biochem. Pol. 48, 729-737.
Jarmuszkiewicz, W., Milani, G., Fortes, F., Schreiber, A. Z., Sluse, F. E., and Vercesi, A. E. (2000a). FEBS Lett. 467, 145-149.
Jarmuszkiewicz, W., Navet, R., Alberici, L. C., Douette, P., Sluse-Goffart, C. M., Sluse, F. E., and Vercesi, A. E. (2004b). J. Bioenerg. Biomembr. 36(5), 493-502.
Jarmuszkiewicz, W., Sluse-Goffart, C. M., Hryniewiecka, L., Michejda, J., and Sluse, F. E. (1998b). J. Biol. Chem. 273, 10174-10180.
Jarmuszkiewicz, W., Sluse-Goffart, C. M., Hryniewiecka, L., and Sluse, F. E. (1999). J. Biol. Chem. 274, 23198-23202.
Jarmuszkiewicz, W., Wagner, A. M., Wagner, M. J., and Hryniewiecka, L. (1997). FEBS Lett. 411, 110-114.
Ježek, P. (2002). Int. J. Biochem. Cell Biol. 34, 1190-1206.
Kamo, N., Muratsugu, N., Hongoh, R., and Kobatake, Y. (1979). J. Membr. Biol. 49, 105-121.
Klingenberg, M. (1990). Trends Biochem. Sci. 15, 108-112.
Ricquier, D., and Bouillaud, F. (2000). Biochem. J. 345, 161-179.
Samartsev, V. N., Mokhova, E. N., and Skulachev, V. P. (1997). FEBS Lett. 412, 251-257.
Skulachev, V. P. (1998). Biochim. Biophys. Acta 1363, 100-124.
Sluse, F. E., and Jarmuszkiewicz, W. (2002). FEBS Lett. 510, 117-120.
Tablot, D. A., Lambert, A. J., and Brand, M. D. (2004). FEBS Lett. 556, 111-115.
Tudella, V. G., Curti, C., Soriani, F. M., Santos, A., and Uyemura, S. A. (2003). Int. J. Biochem. Cell Biol. 36, 162-172.
Uyemura, S. A., Luo, S., Moreno, S. N. J., and Docampo, R. (2000). J. Biol. Chem. 275, 9709-9715.
Van den Bergen, C. W., Wagner, A. M., Krab, K., and Moore, A. L. (1994). Eur. J. Biochem. 226, 1071-1078.
Wainright, P. O., Hinkle, G., Sogin, M. L., and Stickel, S. K. (1993). Science 260, 340-342.
Wieckowski, M. R., and Wojtczak, L. (1997). Biochem. Biophys. Res. Commun. 232, 414-417.
Žáčková, M., Kramer, R., and Ježek, P. (2000). Int. J. Biochem. Cell Biol. 32, 499-508.
Žáčková, M., Škobisová, E., Urbánková, E., and Ježek, P. (2003). J. Biol. Chem. 278, 20761-20769.