Proton selective substate of the mitochondrial permeability transition pore: Regulation by the redox state of the electron transport chain
Proton selective substate of the mitochondrial permeability transition pore: Regulation by the redox state of the electron transport chain
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DOI:
10.1021/bi980820c
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发表时间:
1998-09-22
期刊:
影响因子:
2.9
通讯作者:
Pfeiffer, DR
中科院分区:
文献类型:
--
作者:
Broekemeier, KM;Klocek, CK;Pfeiffer, DR
The permeability transition pore of rat liver mitochondria can be closed by chelating free Ca2+, with respect to the passage of large molecules such as mannitol and sucrose. However, an apparent H+-conducting substrate remains open under these conditions, as indicated by the persistence of maximal O-2 consumption rates and by the failure to recover a membrane potential. Agents which favor a closed pore, such as cyclosporin A, ADP, Mg2+, or bovine serum albumin, do not close the H+-conducting substate, but it closes spontaneously when respiration becomes limited by the availability of O-2. Closure provoked by an O-2 limitation requires free Mg2+ in the sub-micromolar concentration range and becomes less efficient with increasing time spent in the presence of free Ca2+. The H+-conducting substate is apparently regulated by the redox status of the electron transport chain, with a reduced form favoring closure. A physical association (or equivalence) between the pore and one of the respiratory chain complexes is supported. These characteristics suggest that the transition is irreversible in vivo, if it involves a small fraction of total mitochondria, and would lead to their elimination and/or replacement by the cell. The implications of this proposal are considered, as they relate to a possible role for the transition in cellular apoptosis and the elimination of mitochondria containing mutated DNA.