Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translocator. Hexokinase activity suppresses this effect |
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| Authors: | Vyssokikh Miklail Y Zorova Ljubava Zorov Dmitry Heimlich Gerd Jürgensmeier Juliane J Brdiczka Dieter |
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| Institution: | (1) A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia;(2) Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Russia;(3) Department of Biology, University of Konstanz, D-78457 Konstanz |
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| Abstract: | The mechanism by which external Bax releases cytochrome c is still controversial and may also depend on the type of mitochondria and the actual localisation of cytochrome c. Outer membrane porin acquires high binding affinity for hexokinase by interacting with the adenine nucleotide translocator (ANT) in the contact sites. (I) The hexokinase protein was thus used as a tool to isolate the contact site forming complex between outer membrane porin and inner membrane ANT from a TritonX100 extract of brain membranes. (II) A significant amount of cytochrome c was co-purified with the isolated hexokinase porin ANT complexes that were reconstituted in phospholipid vesicles. Bax- C released the endogenous cytochrome c from the vesicles without forming unspecific pores. This was shown by loading the vesicles with malate that was not liberated by Bax-C. (III) The Bax-C effect was dependent on a specific association of cytochrome c with the porin ANT complex, as dissociation of the complex by bongkrekate abolished the Bax dependent cytochrome c liberation. (IV) The Bax-C effect was as well suppressed by hexokinase phosphorylating glucose. |
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| Keywords: | mitochondria structure apoptosis growth factor protein kinase B/Akt |
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