The mitochondrial permeability transition from yeast to mammals

被引:108
作者
Azzolin, Luca [1 ]
von Stockum, Sophia [1 ]
Basso, Emy [1 ]
Petronilli, Valeria [1 ]
Forte, Michael A. [2 ]
Bernardi, Paolo [1 ]
机构
[1] Univ Padua, Dept Biomed Sci, CNR Inst Neurosci, I-35121 Padua, Italy
[2] Oregon Hlth & Sci Univ, Vollum Inst, Portland, OR 97201 USA
关键词
Mitochondria; Permeability transition; Calcium; Cyclosporin; Cyclophilin; CA-2&-INDUCED MEMBRANE TRANSITION; PROGRAMMED CELL-DEATH; MALIC ENZYME-ACTIVITY; CYCLOSPORINE-A; SACCHAROMYCES-CEREVISIAE; CYCLOPHILIN-D; LIVER-MITOCHONDRIA; INORGANIC-PHOSPHATE; CYTOCHROME-C; MOLECULAR-MECHANISM;
D O I
10.1016/j.febslet.2010.04.023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Ca2+-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) Ca2+-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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2504 / 2509
页数:6
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