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The Mitochondrial Creatine Phosphokinase is Associated with Inner Membrane Cardiolipin

  • Michele Müller
  • Dominique Cheneval
  • Ernesto Carafoli
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 194)

Abstract

Inorganic phosphate (Pi) and negatively charged SH-group reagents solubilize the membrane bound mitochondrial creatine phosphokinase (m-CPK) into the medium (1,2). The rebinding of the solubilized m-CPK to the inner mitochondrial membrane is inhibited by adriamycin, a drug widely used in cancer chemotherapy, (3). Adriamycin binds specifically to mitochondrial cardiolipin (4,5) and has been found to inhibit the activity of cardiolipin-dependent proteins, such as cytochrome c oxidase and the phosphate transport protein (6–8). It has been proposed that m-CPK and the ADP/ATP translocator form a tightly coupled functional complex (9,10). The proposal, however, is not universally accepted (11). In this report we present evidence that m-CPK binds to membrane-associated cardiolipin in a reaction that is inhibited by adriamycin in mitochondria as well as in liposomes.

Keywords

Mitochondrial Membrane Creatine Kinase Heart Mitochondrion Mitochondrial Creatine Kinase Rebind Experiment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Michele Müller
    • 1
  • Dominique Cheneval
    • 1
  • Ernesto Carafoli
    • 1
  1. 1.Laboratory of BiochemistrySwiss Federal Institute of Technology (ETH)ZurichSwitzerland

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