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Possible role of cytoskeleton in intracellular arrangement and regulation of mitochondria

Published online by Cambridge University Press:  09 January 2003

Florence Appaix ,
Andrey V. Kuznetsov ,
Yves Usson ,
Laurence Kay ,
Tatiana Andrienko ,
Jose Olivares ,
Tuuli Kaambre ,
Peeter Sikk ,
Raimund Margreiter  and
Valdur Saks
Florence Appaix
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Andrey V. Kuznetsov
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Yves Usson
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Laurence Kay
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Tatiana Andrienko
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Jose Olivares
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Tuuli Kaambre
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Peeter Sikk
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Raimund Margreiter
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
Valdur Saks
Affiliation:
Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France, Department of Transplant Surgery, University Hospital Innsbruck, Innsbruck, Austria, RFMQ-TIMC Laboratory, UMR 5525 CNRS, Institute Albert Bonniot, Grenoble, France, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia and Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia
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Abstract

The origin of significant differences between the apparent affinities of heart mitochondrial respiration for exogenous ADP in isolated mitochondria in vitro and in permeabilized cardiomyocytes or skinned fibres in situ is critically analysed. All experimental data demonstrate the importance of structural factors of intracellular arrangement of mitochondria into functional complexes with myofibrils and sarcoplasmic reticulum in oxidative muscle cells and the control of outer mitochondrial membrane permeability. It has been shown that the high apparent Km for exogenous ADP (250-350 µM) in permeabilized cells and in ghost cells (without myosin) and fibres (diameter 15-20 µm) is independent of intrinsic MgATPase activity. However, the Km may be decreased significantly by a selective proteolytic treatment, which also destroys the regular arrangement of mitochondria between sarcomeres and increases the accessibility of endogenous ADP to the exogenous pyruvate kinase-phosphoenolpyruvate system. The confocal microscopy was used to study the changes in intracellular distribution of mitochondria and localization of cytoskeletal proteins, such as desmin, tubulin and plectin in permeabilized cardiac cells during short proteolytic treatment. The results show the rapid collapse of microtubular and plectin networks but not of desmin localization under these conditions. These results point to the participation of cytoskeletal proteins in the intracellular organization and control of mitochondrial function in the cells in vivo, where mitochondria are incorporated into functional complexes with sarcomeres and sarcoplasmic reticulum.Experimental Physiology (2003) 88.1, 175-190.

Type
Special Review Series - Biogenesis and Physiological Adaptation of Mitochondria
Information
Experimental Physiology , Volume 88 , Issue 1 , January 2003 , pp. 175 - 190
Copyright
© The Physiological Society 2003

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