In yeast, Ca2+ and octylguanidine interact with porin (VDAC) preventing the mitochondrial permeability transition
Por:
Gutiérrez-Aguilar M., Pérez-Vázquez V., Bunoust O., Manon S., Rigoulet M., Uribe S.
Publicada:
1 ene 2007
Resumen:
In yeast, Ca2+ and long chain alkylguanidines interact with mitochondria modulating the opening of the yeast mitochondrial unspecific channel. Mammalians possess a similar structure, the mitochondrial permeability transition pore. The composition of these pores is under debate. Among other components, the voltage-dependent anion channel has been proposed as a component of either pore. In yeast from an industrial strain, octylguanidine and calcium closed the yeast mitochondrial unspecific channel. Here, the effects of the cations Ca2+ or octylguanidine and the voltage-dependent anion channel effector decavanadate were evaluated in yeast mitochondria from either a wild type or a voltage-dependent anion channel deletion laboratory strain. It was observed that in the absence of voltage-dependent anion channel, the yeast mitochondrial unspecific channel was desensitized to Ca2+, octylguanidine or decavanadate but remained sensitive to phosphate. It is thus suggested that in yeast mitochondria, the voltage-dependent anion channel has a cation binding site where Ca2+ and octylguanidine interact, conferring cation sensitivity to the yeast mitochondrial unspecific channel. © 2007 Elsevier B.V. All rights reserved.
Filiaciones:
Instituto de Fisiología Celular UNAM, México, D. F., Mexico
Institut de Biochimie et Génétique Cellulaires, Université de Bordeaux-2 Victor Segalen, Bordeaux, France
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