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The influence of the cytosolic oncotic pressure on the permeability of the mitochondrial outer membrane for ADP: implications for the kinetic properties of mitochondrial creatine kinase and for ADP channelling into the intermembrane space

  • Substrate and Creatine Kinase Isoenzyme Compartmentation
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Summary

Cytosolic proteins as components of the physiological mitochondrial environment were substituted by dextrans added to media normally used for incubation of isolated mitochondria. Under these conditions the volume of the intermembrane space decreases and the contact sites between the both mitochondrial membranes increase drastically. These morphological changes are accompanied by a reduced permeability of the mitochondrial outer compartment for adenine nucleotides as it was shown by extensive kinetic studies of mitochondrial enzymes (oxidative phosphorylation, mi-creatine kinase, mi-adenylate kinase). The decreased permeability of the mitochondrial outer membrane causes increased rate dependent concentration gradients in the micromolar range for adenine nucleotides between the intermembrane space and the extramitochondrial space. Although all metabolites crossing the outer membrane exhibit the same concentration gradients, considerable compartmentations are detectable for ADP only due to its low extramitochondrial concentration. The consequences of ADP-compartmentation in the mitochondrial intermembrane space for ADP-channelling into the mitochondria are discussed.

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Author notes

  1. Frank Norbert Gellerich

    Present address: Department of Transplant Surgery, Clinical and Interdisciplinary Bioenergetics, University Hospital of Innsbruck, Austria

Authors and Affiliations

  1. Dept. of in vivo NMR spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Bolognalaan 50, NL-3584 CJ, Utrecht, The Netherlands

    Frank Norbert Gellerich & Klaas Nicolay

  2. Institut für Biochemie der Medizinischen Fakultät der Universität Magdeburg, Germany

    Matthias Kapischke & Wolfram Kunz

  3. Klinik für Orthopädie der Medizinischen Fakultät der Universität Magdeburg, Germany

    Wolfram Neumann

  4. Fakultät für Biologie, Universität Konstanz, Germany

    Dieter Brdiczka

  5. Laboratory of Bioenergetics, Cardiology Research Center, Moscow, Russia

    Andrey Kuznetsov

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  1. Frank Norbert Gellerich
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Gellerich, F.N., Kapischke, M., Kunz, W. et al. The influence of the cytosolic oncotic pressure on the permeability of the mitochondrial outer membrane for ADP: implications for the kinetic properties of mitochondrial creatine kinase and for ADP channelling into the intermembrane space. Mol Cell Biochem 133, 85–104 (1994). https://doi.org/10.1007/BF01267949

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