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-AC 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-AC. (III) The Bax-AC 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-AC effect was as well suppressed by hexokinase phosphorylating glucose.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Vyssokikh MY,Zorova L,Zorov D,Heimlich G,Jürgensmeier JJ,Brdiczka Ddoi
10.1023/a:1020383108620keywords:
subject
Has Abstractpub_date
2002-01-01 00:00:00pages
93-6issue
1-2eissn
0301-4851issn
1573-4978journal_volume
29pub_type
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