Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1807, Issue 4, Pages 458-469Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2011.01.010
Keywords
Cardiomyocytes; Creatine kinase; HL-1 cells; Mitochondrial interactosome; beta-tubulin isotypes; Warburg effect
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Funding
- INSERM, France
- Agence Nationale de la Recherche, France [ANR-07-BLAN-0086-01]
- Estonian Science Foundation [7823]
- Estonia Ministry of Education and Science [SF0180114Bs08]
- National Council of Science and Technology of Mexico (CONACYT)
- Austrian Science Fund (FWF) [P 22080-B20]
- Austrian Science Fund (FWF) [P 22080] Funding Source: researchfish
- Agence Nationale de la Recherche (ANR) [ANR-07-BLAN-0086] Funding Source: Agence Nationale de la Recherche (ANR)
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Mitochondria-cytoskeleton interactions were analyzed in adult rat cardiomyocytes and in cancerous non-beating HL-1 cells of cardiac phenotype. We show that in adult cardiomyocytes beta II-tubulin is associated with mitochondrial outer membrane (MOM). beta I-tubulin demonstrates diffused intracellular distribution, beta III-tubulin is colocalized with Z-lines and beta IV-tubulin forms microtubular network. HL-1 cells are characterized by the absence of beta II-tubulin, by the presence of bundles of filamentous beta IV-tubulin and diffusely distributed beta I- and beta III-tubulins. Mitochondrial isoform of creatine kinase (MtCK), highly expressed in cardiomyocytes, is absent in HL-1 cells. Our results show that high apparent K-m for exogenous ADP in regulation of respiration and high expression of MtCK both correlate with the expression of beta II-tubulin. The absence of beta II-tubulin isotype in isolated mitochondria and in HL-1 cells results in increased apparent affinity of oxidative phosphorylation for exogenous ADP. This observation is consistent with the assumption that the binding of beta II-tubulin to mitochondria limits ADP/ATP diffusion through voltage-dependent anion channel of MOM and thus shifts energy transfer via the phosphocreatine pathway. On the other hand, absence of both beta II-tubulin and MtCK in HL-1 cells can be associated with their more glycolysis-dependent energy metabolism which is typical for cancer cells (Warburg effect). (C) 2011 Elsevier B.V. All rights reserved.
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