The mitochondrial permeability transition from yeast to mammals

作者：Azzolin Luca; von Stockum Sophia; Basso Emy; Petronilli Valeria; Forte Michael A; Bernardi Paolo^*

来源：FEBS LETTERS, 2010, 584(12): 2504-2509.

DOI：10.1016/j.febslet.2010.04.023

• Mitochondria
• Permeability transition
• Calcium
• Cyclosporin
• Cyclophilin

Regulated permeability changes have been detected in mitochondria across species. We review here their key features, with the goal of assessing whether a "permeability transition" similar to that observed in higher eukaryotes is present in other species. The recent discoveries (i) that treatment with cyclosporin A (CsA) unmasks an inhibitory site for inorganic phosphate (Pi) [Basso, E., Petronilli, V., Forte, M. A. and Bernardi, P. (2008) Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. J. Biol. Chem. 283, 26307-26311], the classical inhibitor of the permeability transition of yeast and (ii) that under proper experimental conditions a matrix Ca(2+)-dependence can be demonstrated in yeast as well [Yamada, A., Yamamoto, T., Yoshimura, Y., Gouda, S., Kawashima, S., Yamazaki, N., Yamashita, K., Kataoka, M., Nagata, T., Terada, H., Pfeiffer, D. R. and Shinohara Y. (2009) Ca(2+)-induced permeability transition can be observed even in yeast mitochondria under optimized experimental conditions. Biochim. Biophys. Acta 1787, 1486-1491] suggest that the mitochondrial permeability transition has been conserved during evolution.

• 出版日期2010-6-18