Molecular interaction between cyclophilin D and adenine nucleotide translocase in cytochrome c release: does it determine whether cytochrome c release is dependent on permeability transition or not?
We propose a model for the mechanism of permeability transition (PT) related cytochrome c release. It is likely that the Ca(2+) requirement for the induction of the mitochondrial permeability transition pore (MPTP) opening might be due to the Ca(2+)-dependent interaction between cyclophilin D and ANT. We show here that the modification of adenine nucleotide translocase (ANT), which is one of the components of MPTP, can induce two different types of the cytochrome c release. One is dependent on classical PT, resulting in mitochondrial swelling, and is inhibited by cyclosporin A. The other is PT-independent, without swelling, and is insensitive to cyclosporin A.
Machida
Kiyotaka
K
Antibiotics Laboratory, Riken, Hirosawa 2-1, Saitama 351-0198, Japan.
Osada
Hiroyuki
H
D017209:Apoptosis / Q000187:drug effects / Q000502:physiology; D000081406:Peptidyl-Prolyl Isomerase F; D021983:Cyclophilins / Q000378:metabolism*; D045304:Cytochromes c / Q000378:metabolism*; D018922:HL-60 Cells; D006801:Humans; D008928:Mitochondria / Q000502:physiology*; D000226:Mitochondrial ADP, ATP Translocases / Q000378:metabolism*; D010539:Permeability; D011758:Pyrroles / Q000494:pharmacology
D000081406:Peptidyl-Prolyl Isomerase F; C121809:MT 21; D011758:Pyrroles; D045304:Cytochromes c; D000226:Mitochondrial ADP, ATP Translocases; D021983:Cyclophilins